Products

VEGF 165, also known as Vascular Endothelial Growth Factor 165, is a protein that plays a critical role in angiogenesis, the process of forming new blood vessels from pre-existing ones. It belongs to the vascular endothelial growth factor family and is one of the most well-studied isoforms of VEGF.    Product Properties Synonyms   VEGF-165；VEGF; VEGFA; MVCD1;  VPF; RP1-261G23.1;   Uniprot No. P15692-4 Source Recombinant Human VEGF165 Protein is expressed from HEK293 without tag. It contains Ala27-Arg191 Molecular Weight The protein has a predicted MW of 19.2 kDa. Due to glycosylation, the protein migrates to 20-30 kDa based on Tris-Bis PAGE result. Biological Activity ED50 < 3 ng/ml, measured in a cell proliferation assay using HUVEC cells. Purity > 95% by SDS-PAGE and HPLC Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Reconstitution It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 -6 months, -85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells.Human Vimentin shares 97-98% aa identity with mouse, rat, ovine, bovine and canine Vimentin. Vimentin is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell. Vimentin helps maintain the lipid composition of cellular membranes, and caspase cleavage of Vimentin is a key event in apoptosis.   Product Properties Synonyms FLJ36605, VIM Accession P08670 GeneID 7431 Source E.coli-derived Human Vimentin, Ser2-Glu466. Molecular Weight Approximately 53.5 kDa. AA Sequence STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in 30 % Acetonitrile and 0.1 % TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 4 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Vitronectin (VTN) is a glycoprotein that is involved in cell adhesion, migration, and survival. It is a multifunctional protein that plays a role in processes such as blood coagulation, wound healing, and tissue regeneration. VTN also has potential therapeutic applications for diseases such as cancer and cardiovascular disease.   Product Properties Synonyms V75 ; Vitronectin ; VN Uniprot No. P04004 Source Recombinant Human VTN Protein is expressed from HEK293 Cells with His tag at the N-terminal. It contains Asp20-Leu478. Molecular Weight The protein has a predicted MW of 54.23 kDa. And it migrates as 72-100 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Human Wnt-3a protein is a signaling protein that belongs to the Wnt family. It plays a crucial role in various developmental processes, including cell fate determination, tissue patterning, and organogenesis. Wnt-3a protein is secreted by cells and acts as a ligand, binding to specific receptors on the surface of target cells to activate intracellular signaling pathways.   Product Properties Synonyms   Wingless-type MMTV Integration Site Family, Member 3a   Uniprot No.  P56704 Source HEK293 cells-derived human Wnt-3a protein, Ser19-Lys352, with C-terminal His tag. Molecular Weight The protein has a predicted MW of 39.4 kDa. And it migrates as 43 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 50% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in PBS，the concentration is 0.015 mg/ml.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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Wnt3a, one of Wnt family members, plays key roles in regulating pleiotropic cellular functions, including self-renewal, proliferation, differentiation, and motility. The Wnt family comprises 19 human proteins, including Wnt1, Wnt2, Wnt2b (Wnt13), Wnt3, Wnt3a, Wnt4, Wnt5a, Wnt5b, Wnt6, Wnt7a, Wnt7b, Wnt8a, Wnt8b, Wnt9a (Wnt14), Wnt9b (Wnt14b), Wnt10a, Wnt10b, Wnt11, and Wnt16. These genes encode secreted glycoproteins that are rich in cysteine. Wnts can combine with cell membrane receptors that play a critical role in autocrine regulation and/or participate in paracrine modification by binding to adjacent cell membrane receptors. The signal transduction pathway mediated by Wnt genes is called the Wnt signaling pathway. Accumulating evidence has suggested that Wnt3a promotes or suppresses tumor progression via the canonical Wnt signaling pathway depending on cancer type. In addition, the roles of Wnt3a signaling can be inhibited by multiple proteins or chemicals. Human Wnt-3a shares 96% aa identity with mouse mouse, bovine and canine Wnt-3a, and 89%, 86% and 84% aa identity with chicken, Xenopus and zebrafish Wnt-3a, respectively. It also shares 87% aa identity with Wnt3. During embryonic development, Wnt-3a is necessary for proper development of the hippocampus, anterior-posterior patterning, somite development, and tailbud formation. Wnt-3a also promotes self-renewal of  hematopoietic stem cells, neural stem cells, and embryonic stem cells. Product Properties Synonyms Wingless-type MMTV Integration Site Family, Member 3 Uniprot No. P56704 GeneID 8978 Source HEK293 cells-derived Human wnt-3a, Ser19-Lys352 Molecular Weight Approximately 63.3 kDa AA Sequence SY PIWWSLAVGP QYSSLGSQPI LCASIPGLVP KQLRFCRNYV EIMPSVAEGI KIGIQECQHQ  FRGRRWNCTT VHDSLAIFGP VLDKATRESA FVHAIASAGV AFAVTRSCAE GTAAICGCSS RHQGSPGKGW KWGGCSEDIE FGGMVSREFA DARENRPDAR SAMNRHNNEA GRQAIASHMH LKCKCHGLSG SCEVKTCWWS QPDFRAIGDF LKDKYDSASE MVVEKHRESR GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS SHGIDGCDLL CCGRGHNARA ERRREKCRCV FHWCCYVSCQ ECTRVYDVHT CK Tag Fc Purity > 75% as determined by SDS-PAGE. Activity Measured by its binding ability in a ELISA method. Immobilized Human Wnt-3a at 10 μg/ml (100 μl/well) can bind bind Wnt-3a mouse monoclonal antibody. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. Transportation and Storage Methods Transport with ice packs. Store at -20°C to -80°C with a one-year shelf life. It is recommended to aliquot and freeze for the first use to avoid repeated freeze-thaw cycles. Cautions 1.Avoid repeated freezing and thawing. 2.For your safety and health, please wear a lab coat and use disposable gloves during operations. 3.This product is for research use only!

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  Name Catalog No. Size Recombinant Human XCR1 Protein-VLP C230755E 20 μg C230755S 100 μg C230755M 100 μg C230755L 1 mg   Product Properties   Synonyms XCR1 / CCXCR1 / GPR5 Source HEK293 Cells AA sequence Accession #P46094:Met1 - Tyr333 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Activin A, a homodimer of activin βA subunits, is a member of the transforming growth factor (TGF)-β super-family. Activin A is produced by the placenta during human pregnancy, has been recognized as a multifunctional cytokine expressed in a wide range of tissues and cells with roles in regulation of wound repair, cell differentiation, apoptosis, embryogenesis, and inflammation. The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A has been proposed in several pathological processes such as carcinogenesis and fibrosis, and this cytokine may also be involved in the pathogenesis of various inflammatory disorders such as inflammatory bowel disease and rheumatoid arthritis.   Product Properties Synonyms Activin A, activin AB alpha polypeptide, erythroid differentiation factor, Erythroid differentiation protein, FSH-releasing protein, inhibin beta A chain Accession P08476 GeneID 3624 Source Insect Cell-derived Human/Mouse/Rat Activin A/Inhibin beta A protein, Gly311 - Ser426. Molecular Weight Approximately 26 kDa. AA Sequence GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSS LSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE analyses. Biological Activity Test in processing. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 300 mM NaCl, with 5% Trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile 10mM HCl to a concentration of 0.1-0.3 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup, where BMP2-7 belong to the TGF-β superfamily. It plays a leading role in embryonic dorsal-ventral patterning, organogenesis, limb bud formation, and bone formation and regeneration. Mature human BMP-2 has 100% amino acid sequence identity with mouse and rat BMP-2. It shares 85% sequence identity with human BMP-4 and less than 51% sequence identity with other BMPs. Normal bone formation is a carefully regulated long-term process involving the continuous expression of growth regulatory factors by osteoblasts during proliferation and eventual differentiation. This orderly sequence of osteoblast gene expression indicates a cascade effect, which BMP-2 can initiate and maintain. BMP-2 also promotes the maintenance and repair of colonic epithelium, inhibits the synthesis and release of neuronal dopamine, induces apoptosis in medulloblastoma cells, and is necessary for myocardial contractility.   Product Properties   Synonyms BDA2, BMP2, BMP-2, BMP-2A, SSFSC Source E.coli-derived human BMP-2, Gln283-Arg396, with an N-terminal Met Endotoxin < 0.1 EU per μg by the LAL method. Purity > 95% by SDS-PAGE  and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM sodium citrate, pH 3.5. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water.   Storage    The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Transforming growth factor-beta 1 (TGF-β1) is a major pluripotential cytokine with a pronounced immunosuppressive effect. TGF-β1 is a key regulator of diverse biological processes in many tissues and cell types, its can be tumorsuppressive through the activation of the Smadmediated signaling pathway.   Product Properties Synonyms CEDLAP, DPD1, latency-associated peptide, TGF beta, TGF beta1 Uniprot No. P01137 Source HEK293-derived Human TGF-β1, Ala279-Ser390. Molecular Weight The protein has a predicted 12.8 kDa Purity > 95% as determined by SDS-PAGE. Biological Activity Measured by the (CAGA)12—luciferase reporter assay. The EC50 for this effect is 1.092 ng/mL. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Dissolved in sterile PBS buffer. Concentration 0.5 mg/ml   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Activin A, a homodimer of activin βA subunits, is a member of the transforming growth factor (TGF)-β super-family. Activin A is produced by the placenta during human pregnancy, has been recognized as a multifunctional cytokine expressed in a wide range of tissues and cells with roles in regulation of wound repair, cell differentiation, apoptosis, embryogenesis, and inflammation.   Product Properties   Synonyms Activin A, activin AB alpha polypeptide, inhibin beta A chain Source Human/Murine/Rat Activin A Protein is expressed from CHO cell.It contains Gly311 - Ser426. Endotoxin < 0.01 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from 0.2 μm filtered concentrated solution in 30% acetonitrile and 0.1 % TFA. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile 4 mM HCl to a concentration of 0.1-0.5 mg/ml.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Mouse aFGF, encoded by the FGF1 gene, is a member of the fibroblast growth factor (FGF) family. Fibroblast growth factor was found in pituitary extracts in 1973 and then tested in a bioassay that caused fibroblasts to proliferate. After further fractionating the extract using acidic and basic pH, two different forms have isolated that named "acidic fibroblast growth factor" (FGF-1) and "basic fibroblast growth factor" (FGF-2). Murine aFGF shares 52 % amino acid sequence identity with bFGF. Murine aFGF shares 96 % amino acid sequence identity with human aFGF, so it exhibits considerable species crossreactivity between murine and human aFGF. In mammalian FGF receptor family has 4 members, FGFR1, FGFR2, FGFR3, and FGFR4, and 1, 2, 3 have 2 sub-types “b”, “c” . aFGF can bind and activate all 7 different FGFRs. Affinity between aFGF and its receptors can be increased by heparin or heparan sulfate proteoglycan. aFGF plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.   Product Properties Synonyms Fibroblast growth factor 1；FGF-1；Acidic fibroblast growth factor；HBGF-1 Accession P61148 GeneID 14164 Source E.coli-derived mouse Acidic Fibroblast Growth Factor protein, Phe16-Asp155 Molecular Weight Approximately 15.8 kDa. AA Sequence FNLPLGNYKK PKLLYCSNGG HFLRILPDGT VDGTRDRSDQ HIQLQLSAES AGEVYIKGTE TGQYLAMDTE GLLYGSQTPN EECLFLERLE ENHYNTYTSK KHAEKNWFVG LKKNGSCKRG PRTHYGQKAI LFLPLPVSSD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 0.2 ng/ml, corresponding to a specific activity of > 5.0 × 106 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Bcl-xL is a member of the Bcl-2 family of proteins that regulates outer mitochondrial membrane permeability. Bcl-xL is an anti- apoptotic member that prevents release of cytochrome c from the mitochondria intermembrane space into the cytosol. Bcl-xL is present on the outer mitochondrial membrane and is also found on other membranes in some cell types. Natural Bcl-xL contains a carboxyl-terminal mitochondria targeting sequence. Recombinant Bcl-xL missing the mitochondrial targeting sequence maintains its ability to neutralize pro- apoptotic Bcl-2 family members. Neutralization by Bcl-xL appears to be through binding the BH3 region of pro- apoptotic Bcl-2 family members. This activity does not require the mitochondrial targeting sequence.   Product Properties Synonyms Apoptosis regulator Bcl-X; bcl2-L-1 Accession Q64373 GeneID 12048 Source E.coli-derived Human Mouse Bcl-xL, Ser2-Arg212, with an N-terminal Met. Molecular Weight Approximately 23.7 kDa. AA Sequence SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Test in Process. Endotoxin Less than 0.1 EU/µg of rMuBcl-xL as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4, 5% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms BD1 Protein, DEFB-1 Protein, DEFB101 Protein, BD1 Protein Accession P56386 GeneID 13214 Source E.coli-derived mouse Beta-defensin 1 protein, Val22-Ser69 Molecular Weight Approximately 5.2 kDa. AA Sequence VGILTSLGRR TDQYKCLQHG GFCLRSSCPS NTKLQGTCKP DKPNCCKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using CD34+ dendritic cells is in a concentration range of 100.0-1000.0 ng/ml. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 k Da proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Four human β-defensins have been identified and they are expressed on some leukocytes and at epithelial surfaces. Because β-defensins is cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane.   Product Properties Synonyms Defensin beta 14, Beta-defensin 14,BD-14, Defensin, beta 14 Accession Q7TNV9 GeneID 244332 Source E.coli-derived mouse Beta-defensin 14 protein, Phe23-Lys67 Molecular Weight Approximately 5.2 kDa. AA Sequence FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms Beta-defensin 2, Beta-defensin 4A, BD-2, Defensin beta2 Accession P82020 GeneID 13215 Source E.coli-derived mouse Beta-defensin 2 protein, Ala21-Lys71. Molecular Weight Approximately 5.5 kDa. AA Sequence AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using immature human dendritic cells is in a concentration of 10-100 ng/ml. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms BD-3 Protein, DEFB-3 Protein, DEFB103 Protein, DEFB3 Protein, BD-3 Protein, BD3 Protein, BP-3 Protein, BP3 Protein Accession Q9WTL0 GeneID 27358 Source E.coli-derived mouse Beta-defensin 3 protein, Lys23-Lys63 Molecular Weight Approximately 4.6 kDa. AA Sequence KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by anti-microbial activity against E.coli. is less than 20 μg/ml, corresponding to a specific activity of > 50 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Betacellulin (BTC) is a new member of the EGF family of cytokines that is comprised of at least ten proteins including EGF, TGF-alpha, amphiregulin, HB-EGF, and the various heregulins. All of these cytokines are synthesized as transmembrane precursors and are characterized by the presence of one or more EGF structural units in their extracellular domain. The soluble forms of these cytokines are released by proteolytic cleavage. BTC, a heparin-binding protein, was originally isolated from the conditioned media of mouse pancreatic beta tumor cells as a 32 kDa glycoprotein composed of 80 amino acid residues. The cDNA encoding human BTC was cloned from a human breast adenocarcinoma cell line (MCF-7) cDNA library. Human and mouse cDNAs encode BTC precursor proteins of 178 and 177 amino acid residues, respectively. At the amino acid sequence level, human BTC precursor protein exhibits 79% identity with that of the mouse BTC precursor. In a mouse cell line transfected with human BTC cDNA, three forms of soluble human BTC have been detected: the glycosylated, intact BTC composed of 80 amino acid residues, a truncated molecule lacking 12 amino acid residues from the amino terminus, and a second truncated molecule lacking 30 amino acid residues from the amino terminus. The biological activities of these BTC forms were shown to be identical. BTC can bind to the EGF receptor and is a potent mitogen for Balb/c 3T3 fibroblasts, retinal pigment epithelial cells and vascular smooth muscle cells.   Product Properties Synonyms BTC, probetacellulin Accession Q05928 GeneID 12223 Source E.coli-derived mouse Betacellulin protein, Asp32-Tyr111. Molecular Weight Approximately 9.0 kDa. AA Sequence DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.01 ng/mL, corresponding to a specific activity of > 1.0 × 10 8 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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FGF basic, also known as FGF-2 and HBGF-2, is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. Human FGF acidic shares 54% amino acid (aa) sequence identity with FGF basic and 17%-33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FG F acidic, respectively, andexhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FG F acidic that consists of the Nterminal 40% of themolecule and functions as a receptor antagonist. The effects of androgen and FGF-2 could be partly reversed with a specific anti-FGF-2 immunoglobulin G or by suramin, which inhibits binding of FGFs to their high affinity receptors. Additionally, bFGF is frequently used for a critical component of cell culture medium, e.g., human embryonic stem cell culture medium, serum-free culture systems.   Product Properties Synonyms bFGF, FGF basic, FGF2, FGF-2, fibroblast growth factor 2 (basic), HBGF-2, Prostatropin Accession P15655 GeneID 14173 Source E.coli-derived mouse bFGF, Pro10-Ser154, with an N-terminal Met. Molecular Weight Approximately 16.5 kDa. AA Sequence MPALPEDGGA AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH VKLQLQAEER GVVSIKGVCA NRYLAMKEDG RLLASKCVTE ECFFFERLES NNYNTYRSRK YSSWYVALKR TGQYKLGSKT GPGQKAILFL PMSAKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 1.0 ng/mL, corresponding to a specific activity of > 1.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Description Bone morphogenetic proteins (BMPs) constitute a subfamily of structurally related signaling proteins within the TGF-β superfamily. Members of this superfamily are widely distributed throughout the body and are involved in various physiological processes both prenatally and postnatally. Like BMP-7, BMP-4 is also involved in the development and maintenance of bone and cartilage. Reduced expression of BMP4 is associated with many skeletal diseases, including the hereditary condition progressive diaphyseal dysplasia. Mature mouse and human BMP-4 have 98% amino acid (aa) homology. This product features high activity, high purity, and low endotoxin levels. It has been validated and tested for bioactivity, endotoxin levels, and SDS-PAGE to ensure the consistency of biological activity and batch-to-batch uniformity. Our product is provided in a carrier-free form, making it highly suitable for research and production of cell culture, ELISA, or immunoblotting standards.   Product Properties Synonyms Bone Morphogenetic Protein 4;BMP4;BMP2B; BMP-2B; BMP2B1; Uniprot No. P21275 Source E.coil-derived Mouse BMP-4 protein,Lys303-Arg408 with His tag at the C-terminus Amino Acid MKKNKNCRRHSLYVDFSDVGWND WIVAPPGYQAFYCHGDCPFPLADHL NSTNHAIVQTLVNSVNSSIPKACCVP TELSAISMLYLDEYDKVVLKNYQEMV VEGCGCR Molecular Weight Approximately 14 kDa. Biological Activity Measure by its ability to induce alkaline phosphatase production by ATDC5 cells. The ED50 for this effect is 10 ng/mL. The specific activity of recombinant mouse BMP-4 is > 1 x 100000 IU/mg. Purity > 98% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1×PBS, pH4.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring  the  contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL.   Shipping and Storage Ice pack shipping. Store at -20°C with a one-year shelf life. Recommended to aliquot and freeze upon first use to avoid repeated freezing and thawing.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.   Usage 1. It is recommended to reconstitute the lyophilized powder with sterile water, ensuring that the solution concentration is not less than 100 μg/mL, and let it stand for at least 20 minutes to fully dissolve. 2. After reconstitution, the solution can be further diluted and aliquoted, stored at 2-8°C with a shelf life of 1 month, and at -20°C with a shelf life of 3 months; avoid repeated freezing and thawing. 3. When further diluting and aliquoting the reconstituted solution, a certain amount of carrier protein should be added (0.1% BSA, 10% FBS, or 5% HSA). For experiments that require serum-free conditions, it can be replaced with a 5% trehalose solution as the carrier.

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Chemokine (C-X-C motif) ligand 14 (CXCL14), also named BRAK, is a small cytokine belonging to the CXC chemokine family. Recombinant mouse CXCL14 contains 77 amino acid residues and it shares 97 % and 99 % a.a. sequence identity with human and rat CXCL14. CXCL14 serves as a chemoattractant for activated macrophages, immature dendritic cells and natural killer cells, as well as an antiangiogenic factor by preventing the migration of endothelial cells. CXCL14 also exerts an inhibitory effect on the CXCL12/ CXCR4 signaling pathway, which is involved in the maintenance of T‐helper (Th)2 bias, and promotes Th1 immune response under the physiological and pathological conditions. CXCL14 has been shown to be a highly selective chemoattractant for monocytes that have been treated with prostaglandin E2 or forskolin, agents that activate adenylate cyclase.   Product Properties Synonyms B-cell and Monocyte-activating Chemokine, Chemokine BRAK, Kidney-expressed Chemokine CXC, CXCL14, MIP-2G, Small-inducible Cytokine B14 Accession Q9WUQ5 GeneID 57266 Source E.coli-derived mouse BRAK/CXCL14 protein, Ser23-Glu99. Molecular Weight Approximately 9.4 kDa. AA Sequence SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 400 mM NaCl, pH 7.4, 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Cardiotrophin1 (CT1) is a member of the cytokine family which also includes IL-6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), and ciliary neurotrophic factor (CNTF). CT-1 is a pleiotropic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lung. Studies showed CT-1 which induces cardiac myocyte hypertrophy in vitro can bind to and activate the ILST/gp130 receptor. Rat CT1 encodes a 203 amino acid (a.a.) residue protein that lacks a hydrophobic signal peptide and it shares 94% a.a. and 79% a.a. sequence identity with human and murine CT-1.   Product Properties Synonyms CT-1CT1; CTF1 Accession Q60753 GeneID 13019 Source E.coli-derived Mouse CT-1, Met1-Ala203, with an N-terminal Met. Molecular Weight Approximately 21.5 kDa. AA Sequence MSQREGSLED HQTDSSISFL PHLEAKIRQT HNLARLLTKY AEQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSVLPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP GPEPVTVATL FTANSTAGIF SAKVLGFHVC GLYGEWVSRT EGDLGQLVPG GVA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1 EU/µg of rMuCT-1 as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris, 300 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Ciliary neurotrophic factor (CNTF) is one of a small number of proteins with neurotrophic activities distinct from nerve growth factor (NGF). The cDNA for human CNTF encodes a 200 amino acid residue polypeptide that lacks a signal sequence. Recombinant human CNTF containing 200 amino acids and it shares 82% and 83% a.a. sequence identity with mouse and rat CNTF. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. CNTF is structurally related to IL-6, IL-11, LIF and OSM. Among factors belonging to the CNTF family, CNTF, leukemia inhibitory factor, cardiotrophin-1, and oncostatin M induced a strong promyelinating effect.   Product Properties Synonyms ciliary neurotrophic factor, CNTF, HCNTF Accession P51642 GeneID 12803 Source E.coli-derived mouse CNTF, Ala2-Met198. Molecular Weight Approximately 22.5 kDa. AA Sequence AFAEQSPLTL HRRDLCSRSI WLARKIRSDL TALMESYVKH QGLNKNISLD SVDGVPVAST DRWSEMTEAE RLQENLQAYR TFQGMLTKLL EDQRVHFTPT EGDFHQAIHT LTLQVSAFAY QLEELMALLE QKVPEKEADG MPVTIGDGGL FEKKLWGLKV LQELSQWTVR SIHDLRVISS HHMGISAHES HYGAKQM Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 30 ng/mL, corresponding to a specific activity of > 3.3 × 10 4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in in 2 × PBS, pH 7.4, 2% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant Murine CTACK is a 10.9 kDa protein containing 95 amino acid residues.   Product Properties Synonyms CCL27 Accession Q9Z1X0 GeneID 20301 Source E.coli-derived Mouse CCL27 protein,Leu26-Asn120. Molecular Weight Approximately 10.9 kDa AA Sequence LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml. Endotoxin <1 EU/μg of protein as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4, with 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL16 is a member of the CXC chemokine family. Mouse CXCL16 has 246 a.a. and consists of a 26 a.a. residue putative signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucin-like spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail. Mouse and human CXCL16 share 49% overall aa identity and 70% similarity in the chemokine domains. CXCL16 is a transmembrane chemokine and is implicated in activated CD8+ T cell trafficking. CXCL16 mediates adhesion and phagocytosis of both Gram-negative and Gram-positive bacteria and is a strong chemoattractant for CXCR6+ T cells. It facilitates uptake of low density lipoproteins by macrophages, resulting in foam cell formation.   Product Properties Synonyms SR-PXOX, Scavenger Peceptor for Phosphatidylserine and Oxidized Low Density Lipoprotein, Small-inducible Cytokine B16, Transmembrane Chemokine CXCL16 Accession Q8BSU2 GeneID 66102 Source E.coli-derived mouse CXCL16 protein, Asn27-Pro114. Molecular Weight Approximately 9.9 kDa. AA Sequence NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using mouse lymphocytes is in a concentration of 20-1000 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CXCL3, also known as DCIP1 in mouse, CINC2 in rat, and GROγ in humans, is belonging to the CXC chemokine family. The amino acid sequence of mouse CXCL3 is 57 % identical to human CXCL3. CXCL3 plays a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils. CXCL3 was reportedly associated with the invasion and metastasis of various malignancies. As a member of the chemokine family, CXCL3 was previously known to participate in many pathophysiological events. CXCL3 was found to be upregulated in aggressive cancer cells.   Product Properties Synonyms chemokine (C-X-C motif) ligand 3, CINC-2, CINC-2b, CXCL3, Dcip1, Gm1960, GRO gamma, GRO3 oncogene, GRO3, GROG, GRO-gamma, Growth-regulated protein gamma, Macrophage inflammatory protein 2-beta, MGSA gamma, MIP2B, MIP-2b, MIP2-beta, SCYB3 Accession Q6W5C0 GeneID 330122 Source E.coli-derived mouse DCIP-1/CXCL3 protein, Ala28-Ser100. Molecular Weight Approximately 7.9 kDa. AA Sequence AVVASELRCQ CLNTLPRVDF ETIQSLTVTP PGPHCTQTEV IATLKDGQEV CLNPQGPRLQ IIIKKILKSG KSS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected human 293 cells is in a concentration range of 10-100 ng/ml. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Hedgehogs are synthesized as 45 kDa precursors that are cleaved autocatalytically. The 19 kDa N-terminal fragment remains membrane associated due to its cholesterol and palmitate modifications. Binding of this fragment to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip)\. Within the N-terminal peptide, mouse Dhh shares 97% and 100% amino acid (aa) sequence identity with human and rat Dhh, respectively. It shares 74% aa seqeuence identity with mouse Indian (Ihh) and Sonic hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1 which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. In humans, mutations of Dhh are associated with pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corpus luteum. Its upregulation in human ovarian cancer correlates positively with proliferative index and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in nerve fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.   Product Properties Synonyms DHH; HHG-3MGC35145 Accession Q61488 GeneID 13363 Source E.coli-derived Mouse DHH C23II, Cys23-Gly198 Molecular Weight Approximately 20.0 kDa. AA Sequence IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASGPAEGRVTRGSERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDEDGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 μg/ml. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 1 mM DTT, 0.05% Tween-80. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin- binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through -6. Members of The EGF family are characterized by a shared structural motif, the EGF-like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues. These disulfide bonds are essential for proper protein conformation and receptor binding. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region. EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization to transduce EGF family signals. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2.     Product Properties Synonyms Urogastrone, URG Accession P01132 GeneID 13645 Source E.coli-derived Mouse EGF, Asn977-Arg1029. Molecular Weight Approximately 6.0 kDa. AA Sequence NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/mL, corresponding to a specific activity of > 1.0×107 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also called prokineticin 1 (PK1), is a member of the prokineticin family of secreted proteins that share a common structural motif containing ten conserved cysteine residues that form five pairs of disulfide bonds. The mature region in mouse is 93% and 87% aa identical to the mature regions in rat and human. Mouse EG- VEGF stimulates proliferation and survival of liver sinusoidal endothelial cells, and, in mouse, EG-VEGF acts to induce monocyte migration and stimulate hematopoiesis.   Product Properties Synonyms EGVEGF, Mambakine, PROK1, Prokineticin 1 Accession Q14A28 GeneID 246691 Source E.coli-derived Mouse EG-VEGF protein, Ala20-Phe105. Molecular Weight Approximately 9.6 kDa. AA Sequence AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as Measured in a cell proliferation assay using EJG bovine adrenal-derived endothelial cells. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.4, with 3% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Product Properties Synonyms   EPO; Erythropoietin; EP; MVCD2; Epoetin   Source HEK293 Cells Molecular Weight The recombinant mouse Epo predicts a molecular mass of 18.6 kDa. AA Sequence NP_031968.1 ((Met1-Arg192) Biological Activity Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is typically 2-10 ng/mL. Purity > 95% by SDS-PAGE. Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2. This product is for research use only.

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Fatty acid binding proteins (FABP) are small cytoplasmic lipid binding proteins that are expressed in a tissue specific manner and are involved in intracellular lipid transport. All FABPs bind free fatty acids, cholesterol, and retinoids, which differ in their selectivity, affinity and binding mechanism (1). Circulating FABP levels are used as indicators of tissue damage. Some FABP polymorphisms have been associated with disorders of lipid metabolism and the development of atherosclerosis (2). FABPs are structurally conserved, consisting of a water-filled, ligand-binding pocket surrounded by ten anti-parallel beta-barrel structures, capped by an N-terminal helix-turn-helix motif. The helical N-terminus is involved in the regulation of FA transfer from membranes (3).FABP1, also known as liver FABP (L-FABP) is highly expressed in the liver, intestine, kidney and lung (1). FABP1 binds free fatty acids and their co-enzyme A derivatives. FABP1 is unique among other members in FABP family, attributed to its ability to bind multiple ligands at once. It has a larger solvent-accessible core in comparison to other FABPs, and this allows for more diverse binding to substrates (1). Mouse FABP1 is 127 amino acids (aa) in length. It is a two beta-sheet molecule that contains an acetylated initiating methionine. Full-length mouse FABP1 shares 94% and 84% aa identity with rat and human FABP1, respectively (4).   Product Properties Synonyms FABP1; FABPL; fatty acid binding protein 1, liver; fatty acid-binding protein, liver; LFABP; L-FABP; L-FABPFatty acid-binding protein 1; Liver-type fatty acid-binding protein Accession P12710 GeneID 14080 Source E.coli-derived Mouse FABP1, with an N-terminal Met Molecular Weight Approximately 14.2 kDa. AA Sequence MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The binding affinity of rMuFABP1 for the synthetic ligand cis-parinaric acid has been measured by fluorescence titration. Half maximal fluorescence of 2.5 μM rMuFABP1 is achieved with approximately 5 μM cis-paranaric acid. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 2 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fgf-8 is a member of the fibroblast growth factor (FGF) family that was initially identified as an androgen-inducible growth factor in a mammary carcinoma cell line. Fgf-8 is one of the key signaling molecules implicated in the initiation, outgrowth, and patterning of vertebrate limbs. The cloned 1.26-kb cDNA contained an open reading frame encoding 212 amino acid residues with 84%, 86%, and 80% amino acid identities to those of Xenopus, chick, and mouse, respectively. None of the FGF-8 isoforms exhibited activity to FGFR1b, 2b, 3b, but FGFR2c, 3c and FGFR4 can be activated by several FGF-8 isoforms. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration, and it is required for normal brain, eye, ear and limb development during embryogenesis. FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells.    Product Properties Synonyms AIGF, AIGFKAL6, HBGF-8, FGF-8c Accession P37237 GeneID 14179 Source E.coli-derived mouse FGF-8, Gln23-Arg268. Molecular Weight Approximately 28.1 kDa. AA Sequence QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 5.0 ng/mL, corresponding to a specific activity of >2.0×105 IU/mg in the presence of 10 μg/ml of heparin. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor 16 (FGF-16) belongs to the large FGF family. All FGF family members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain that allows for a common tertiary structure. FGF-16 was originally identified in rat heart tissue by homology based polymerase chain reaction. Murine FGF-16 cDNA predicts a 207 aa precursor protein with one N-linked glycosylation site. FGF-16 lacks a typical signal peptide, but is efficiently generated by mechanisms other than the classical protein secretion pathway. Among FGF family members, FGF-16 is most similar to FGF-9, sharing 73% aa sequence homology. Murine FGF-16 shares 99.5% and 99% aa sequence identity with the human and rat FGF-16, respectively   Product Properties Synonyms Fibroblast growth factor 16；FGF-16 Accession Q9ESL8 GeneID 80903 Source E.coli-derived mouse FGF 16 protein, Met1-Arg207 Molecular Weight Approximately 23.8 kDa. AA Sequence MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Data not available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in 20 mM Tris-HCl, pH 9.0, 1 M NaCl, 0.02 % Tween-20, 10 % Glycerol. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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FGF-17 is a member of the FGF superfamily of heparin-binding mitogenic molecules characterized by the presence of a core, 120 amino acid (aa) beta-trefoil structure. The mRNA of FGF-17 was found in midgestation of embryo and multiple adult tissues, and is preferentially expressed in specific sites, such as embryonic brain, developing skeleton and arteries.   Product Properties Synonyms FGF-13 Protein; FGF-17 Protein; HH20 Protein Accession P63075 GeneID 1417 Source E.coli-derived mouse FGF 17 protein, Thr23-Thr216 Molecular Weight Approximately 22.5 kDa. AA Sequence TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0×105 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 700 mM NaCl, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast Growth Factor 18 (FGF-18) is a 20 kDa protein that plays an important role in skeletal development and bone homeostasis. Mature mouse FGF-18 shares 99% amino acid sequence identity with human and rat FGF-18. It is expressed in embryonic somites and the neural fold, adult lung, cerebellar and hippocampal neurons, hair follicle root sheath cells, and osteogenic mesenchymal cells. FGF-18 binds to FGF R2c, FGF R3c as well as the Golgi protein GLG1 and induces the proliferation of astrocytes and microglia, vascular endothelial cells, dermal fibroblasts, papilla cells, and keratinocytes. FGF-18 is required for normal skeletal development. It recruits osteoclasts and osteoblasts to the growth plate, promotes osteoclast formation and function, inhibits osteoblast differentiation, promotes skeletal vascularization, and induces chondrocyte hypertrophy and cartilage matrix formation.   Product Properties Synonyms zFGF5 Accession O89101 GeneID 14172 Source E.coli-derived Mouse FGF-18, Glu28-Gly207. Molecular Weight Approximately 21.0 kDa. AA Sequence EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor-9, also called FGF-9, is an approximately 26 kDa secreted glycoprotein of the FGF family. Secreted human FGF-9 is a 205-207 aa protein that lacks the N-terminal 1-3 aa and shares 98% sequence identity with mouse, rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc splice forms of FGF R1, R2 and R3 are variably reported. FGF-9 is an autocrine/paracrine growth factor considered to be important for the growth and survival of motorneurons and prostate. Meanwhile, FGF9 is a potent mitogen and survival factor required for morphogenesis during embryonic development and numerous biological functions at adulthood. FGF9 have been shown to improve systolic function after myocardial infarction in a clinical trial. FGF9 promotes cardiac vascularization during embryonic development but is only weakly expressed in the adult heart.   Product Properties Synonyms FGF9, FGF-9, Glia-activating factor, GAF, glia-activating factor, HBFG-9, HBGF-9 Accession P54130 GeneID 14180 Source E.coli-derived mouse FGF-9, Pro3-Ser208, with an N-terminal Met. Molecular Weight Approximately 23.4 kDa. AA Sequence MPLGEVGSYF GVQDAVPFGN VPVLPVDSPV LLNDHLGQSE AGGLPRGPAV TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY KDILSQS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active whencompared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 500 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.     Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession O3518 GeneID 20312 Source E.coli-derived mouse  Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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The glia maturation factor beta belongs to the actin-binding proteins ADF family, GMF subfamily. It contains an ADF-H domain, but the research of crystallography and NMR reveals that there are structures different between human and mouse ADF-H domain. GMF-β is involved in the differentiation, maintenance, and regeneration of the nervous system. It also inhibition of proliferation of tumor cells.   Product Properties Synonyms Glia maturation factor beta, GMF-beta, GMFB Accession Q9CQI3 GeneID 63985 Source E.coli-derived mouse Glia Maturation Factor beta protein, Ser-His142 Molecular Weight Approximately 16.6 kDa. AA Sequence SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity Data not available.   Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-β superfamily. It is a founding member of the GDNF family of ligands (GFL) and has been shown to interact with GFRA2 and GDNF family receptor alpha. Mature rat and human GDNF exhibit approximately 93% amino acid sequence identity and show considerable species cross-reactivity. Cells known to express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells. In embryonic midbrain cultures, recombinant human GDNF promoted the survival and morphological differentiation of dopaminergic neurons and increased their high-affinity dopamine uptake.   Product Properties Synonyms Astrocyte-derived trophic factor, ATF, ATF-1, ATF2, GDNF, HFB1-GDNF, HGDNF, HSCR3 Accession P48540 GeneID 14573 Source E.coli-derived mouse GDNF, Ser78-Ile211. Molecular Weight Approximately 29.9 kDa. AA Sequence SPDKQAAALP RRERNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 0.2 ng/mL, corresponding to a specific activity of > 5.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 0.05% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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GM-CSF is a powerful growth and differentiation factor which acts on hematopoietic progenitor cells and also activates differentiated granulocytes and macrophages.   Product Properties   Synonyms Granulocyte-Macrophage Colony-Stimulating Factor, GM-CSF, CSF-2, MGI-1GM, Pluripoietin-α Source Recombinant Mouse GM-CSF Protein is expressed from Yeast with N-HIS. It contains Ala18-Lys141. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4,with 1%BSA. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 2-7 days, 2~8 °C under sterile conditions after reconstitution.&nbsp; 3 months,&nbsp; -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used&nbsp;and avoid repeated freeze-thaw cycles. Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.   Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession cytokine D1 GeneID 20312 Source E.coli-derived Mouse Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Growth Differentiation Factor-5 (GDF-5; also called BMP-14 and CDMP-1) is a member of the BMP family of TGF-beta superfamily proteins. Mature mouse GDF-5 shares 99% aa sequence identity with both mature human and rat GDF-5. Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis.   Product Properties Synonyms CDMP-1, GDF5, OS5, radotermin, SYNS2 Accession P43027 GeneID 14563 Source E.coli-derived mouse GDF-5/BMP-14 protein, Ala376-Arg495. Molecular Weight Approximately 27.2 kDa. AA Sequence APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. At the amino acid level, mature human GDF-7 shares 85% and 88% aa sequence identity with mature GDF-7 in mouse and rat. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-7 is involved in tendon and ligament formation and repair. GDF-7 also regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance in the central nervous system.   Product Properties Synonyms BMP12, GDF7, growth differentiation factor 7 Accession P43029 GeneID 238057 Source E.coli-derived mouse GDF-7/BMP-12 protein, Thr316-Arg461. Molecular Weight Approximately 29.8 kDa. AA Sequence TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Heparin-binding epidermal growth factor (HB-EGF)-like growth factor (EGF) is found in cerebral neurons. Human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF. Its expression is increased after hypoxic or ischemic injury, which also stimulates neurogenesis. HB-EGF has been implicated as a participant in a variety of normal physiological processes such as blastocyst implantation and wound healing, and in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. The protein is an 86 amino acid mitogenic and chemotactic glycoprotein containing an EGF-like domain with six conserved cysteine residues.   Product Properties Synonyms HBEGF, DT-R Accession Q06186 GeneID 15200 Source E.coli-derived mouse HB-EGF protein, Asp63-Leu148. Molecular Weight Approximately 9.8 kDa. AA Sequence DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using mouse Balb/c 3T3 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PBS, 500 mM NaCl, pH7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interferon-gamma (IFN-γ), also known as Type II interferon or immune interferon, is a pleiotropic cytokine which is now recognised as an important modulator of the immune response. Mature human IFN-γ exists as a non-covalently linked homodimer of 20-25 kDa variably glycosylated subunits.    Product Properties Synonyms Interferon-gamma, IFN-γ, IFG, IFI, IFNG, IFNgamma, IFN-gamma. Accession P01580 GeneID 15978 Source E.coli-derived mouse IFN-γ protein, His23-Cys155. Molecular Weight Approximately 15.5 kDa. AA Sequence HGTVIESLES LNNYFNSSGI DVEEKSLFLD IWRNWQKDGD MKILQSQIIS FYLRLFEVLK DNQAISNNIS VIESHLITTF FSNSKAKKDA FMSIAKFEVN NPQVQRQAFN ELIRVVHQLL PESSLRKRKR SRC Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE  analyses. Biological Activity The ED50 as determined by an anti-viral assay using murine L929 cells infected with encephalomyocarditis (EMC) virus is less than 0.8 ng/ml, corresponding to a specific activity of > 1.3×106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-1 beta (IL-1β) is a pro inflammatory cytokine, which is secreted by immune cells to trigger inflammation and this has been found profoundly in the lesions caused by Leishmania pathogens. IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2), which are the products of distinct genes. IL-1 alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both IL-1α and IL-1β binds to the same receptor and has similar but not identical biological properties; The mature human IL1β shares 96% amino acid sequence identity with rhesus and 67% -78% with canine, mouse and rat IL-1β.IL-1β, are known to modulate effects of neurotoxic neurotransmitters discharged during excitation or inflammation in the central nervous system (CNS).   Product Properties Synonyms Interleukin-1 beta, IL-1β, IL-1, IL1B, IL-1b, IL1-BETA, IL-1F2, IL1F2IL-1 beta, interleukin-1 beta, preinterleukin 1 beta, pro-interleukin-1-beta. Accession P10749 GeneID 16176 Source E.coli-derived human IL-1β protein, Vla118-Ser269. Molecular Weight Approximately 17.5 kDa. AA Sequence VPIRQLHYRL RDEQQKSLVL SDPYELKALH LNGQNINQQV IFSMSFVQGE PSNDKIPVAL GLKGKNLYLS CVMKDGTPTL QLESVDPKQY PKKKMEKRFV FNKIEVKSKV EFESAEFPNW YISTSQAEHK PVFLGNNSGQ DIIDFTMESV SS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 2 pg/mL, corresponding to a specific activity of > 5.0 × 108 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4, with 5% trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-10 (IL-10), also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of α-helical cytokines that also includes IL-19, IL-20, IL-22, IL-24, and IL-26/AK155. IL-10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. Mature human IL- 10 shares 72%- 86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL- 10. IL-10, a cytokine produced by CD4+ T lymphocytes belonging to the Th-2 subset, has previously been shown to inhibit the synthesis of IFN-gamma by both T cells and NK cells.The anti-inflammatory actions of IL-10 may be therapeutically useful either directly or through modulation of HO-1 activity.   Product Properties Synonyms Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, IL10A, TGIF, CSIF Accession P18893 GeneID 16153 Source E.coli-derived mouse IL-10 protein, Ser19-Ser178. Molecular Weight Approximately 18.7 kDa. AA Sequence SRGQYSREDN NCTHFPVGQS HMLLELRTAF SQVKTFFQTK DQLDNILLTD SLMQDFKGYL GCQALSEMIQ FYLVEVMPQA EKHGPEIKEH LNSLGEKLKT LRMRLRRCHR FLPCENKSKA VEQVKSDFNK LQDQGVYKAM NEFDIFINCI EAYMMIKMKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine MC/9-2 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-11 is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin.The mouse IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. It is found in the plasma mainly during inflammation, and is considered to be primarily anti- inflammatory. It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine. It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone absorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis. IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6. IL-11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL-11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.   Product Properties Synonyms AGIF Accession P47873 GeneID 16156 Source E.coli-derived Mouse IL-11, Pro22-Leut199, with an N-terminal Met. Molecular Weight Approximately 19.1 kDa. AA Sequence MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine T11 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-13 (IL-13) was first recognized for its effects on B cells and monocytes, where it upregulated class II expression, promoted IgE class switching and inhibited inflammatory cytokine production. IL-13 is a monomeric 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergy, cancer, and tissue fibrosis. Mature human IL-13 shares approximately 58% amino acid sequence identity with mouse and rat IL-13. It has become evident that IL-13 is a key mediator in the pathogenesis of allergic inflammation, and IL-13 is key proinflammatory cytokines in asthma. The cytokines interleukin IL-13 have pleiotropic effects on a variety of cell types and impact both pathologic changes and tissue remodeling.   Product Properties Synonyms BHR1interleukin-13, IL13, interleukin 13, MGC116786, NC30, P600 Accession P20109 GeneID 16163 Source E.coli-derived Mouse IL-13, Pro22-Phe131, with an N-terminal Met. Molecular Weight Approximately 12.3 kDa. AA Sequence MPVPRSVSLP LTLKELIEEL SNITQDQTPL CNGSMVWSVD LAAGGFCVAL DSLTNISNCN AIYRTQRILH GLCNRKAPTT VSSLPDTKIE VAHFITKLLS YTKQLFRHGP F Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 4 ng/mL, corresponding to a specific activity of > 2.5 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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