Cytokines

Human Complement 5a (C5a) is an enzymatically generated glycoprotein that belongs to a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 74 amino acid (aa) peptide that is created by the activity of C5a convertase on the C5 alpha -chain. Human C5a has four alpha -helices plus three intrachain disulfide bonds that create a triple loop structure. In serum, proteolytic processing removes the Cterminal arginine, creating a low activity C5adesArg74 molecule. Human C5a is 60% and 54% aa identical to mouse and rat C5a, respectively. C5a binds to a signaling G-protein coupled receptor (C5aR/CD88) and a nonsignaling GPCR termed C5L2. Activation of Cd88 results in neutrophil chemotaxis and endothelial cell activation. It also triggers an oxidative burst in macrophages and neutrophils, and induces release of histamine in basophils and mast cells. Product Properties Synonyms CPAMD4 Accession P01031 GeneID 727 Source E.coli-derived Human C5a, Thr678-Arg751. Molecular Weight Approximately 8.3 kDa. AA Sequence TLQKKIEEIA AKYKHSVVKK CCYDGACVNN DETCEQRAAR ISLGPRCIKA FTECCVVASQ LRANISHKDM QLGR 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 its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 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 ℃ 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 Avoid repeated freeze-thaw cycles. For your safety and health, please wear lab coats and disposable gloves for operation. For research use only!

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Apolipoprotein A1 (ApoA1) is a 28 kDa glycoprotein that is the major protein component of high density lipoprotein (HDL) particles. HDL particles play a central role in the reverse transport of cholesterol from peripheral tissues to the liver. HDL is known as “good cholesterol” due to its ability to facilitate the removal of cholesterol from macrophage foam cells in atherosclerotic plaques and thereby retard the progression of disease. ApoA1 is secreted from hepatocytes with variable amounts of lipidation. Product Properties Synonyms Alp-1，Brp-14; Ltw-1 Accession P02647 GeneID 335 Source Recombinant Human ApoA-I Protein is expressed from Yeast Cells with His tag at the C-terminal. It contains Asp25-Gln267 Molecular Weight Approximately 28.9 kDa. AA Sequence DEPPQSPWDR VKDLATVYVD VLKDSGRDYV SQFEGSALGK QLNLKLLDNW DSVTSTFSKL REQLGPVTQE FWDNLEKETE GLRQEMSKDL EEVKAKVQPY LDDFQKKWQE EMELYRQKVE PLRAELQEGA RQKLHELQEK LSPLGEEMRD RARAHVDALR THLAPYSDEL RQRLAARLEA LKENGGARLA EYHAKATEHL STLSEKAKPA LEDLRQGLLP VLESFKVSFL SALEEYTKKL NTQ Purity > 95% by SDS-PAGE. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation The 0.2 μm filtered concentrated solution in PBS, pH 7.4. 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 mediated 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 Accession Q07817 GeneID 598 Source E.coli-derived Human Bcl-2, Ser2-Arg212. Molecular Weight Approximately 23.7 kDa. AA Sequence SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEGT ESEMETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIAAWMA TYLNDHLEPW IQENGGWDTF VELYGNNAAA 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 rHuBcl-xL as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 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℃ 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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Botulinum and tetanus neurotoxins (BoNTs and TeNT) are zinc metalloproteases that hydrolyze and inactivate proteins necessary for neurotransmission. The protease domain is located in the light chain of the neurotoxin. Among the known substrates of BoNTs and TeNT are synaptosomal protein-25 (SNAP25) and vesicle-associated membrane protein (VAMP). This substrate incorporates a green fluorescent protein (GFPuv) and portions of human SNAP25B and VAMP2 that contain the cleavage sites of all the known BoNTs and TeNT. The light chains of BoNTs -A, -C, and -E cleave the SNAP25B sequence, while BoNTs -B, -D, -F, -G, and TeNT cleave within the VAMP2 sequence. The substrate can be used in a SDSPAGE gel-shift assay to detect cleavage by the neurotoxin proteases. Alternatively, the substrate can be coupled to maleimide-activated microwell plates through the C-terminal cysteine residue to generate a high throughput assay format. A similar substrate and assay format has been used to screen for inhibitors of these neurotoxin proteases.   Product Properties Synonyms Green Fluorecence Protein,GFP/SNAP25B/VAMP-2 Accession P42212 GeneID 7011691 Source E.coli-derived eGFP, with an N-terminal Met. Molecular Weight Approximately 26.9 kDa. AA Sequence MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. 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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TAFA2 also named FAM19A2, is a secreted, 11 kDa member of the FAM19/TAFA family of chemokine-like proteins. It is synthesized as a 131 amino acid (aa) precursor that contains a 30 aa signal sequence and a 101 aa mature chain. Like other members of the FAM19/TAFA family, with the exception of TAFA5, mature TAFA1 contains 10 regularly spaced cysteine residues that follow the pattern CX7CCX13CXCX14CX11CX4CX5CX10C, where C represents a conserved cysteine residue and X represents any noncysteine amino acid. Human TAFA2 is 97% aa identical to mouse TAFA2. The biological functions of TAFA family members remain to be determined, but there are a few tentative hypotheses. First, TAFAs may modulate immune responses in the CNS by functioning as brain-specific chemokines, and may act with other chemokines to optimize the recruitment and activity of immune cells in the CNS. Second, TAFAs may represent a novel class of neurokines that act as regulators of immune nervous cells. Finally, TAFAs may control axonal sprouting following brain injury.   Product Properties Synonyms Chemokine-like protein TAFA-2, FAM19A2, MGC42403, TAFA2 Accession Q8N3H0 GeneID 338811 Source E.coli-derived human TAFA-2 protein, Ala31-His131. Molecular Weight Approximately 11.2 kDa. AA Sequence ANHHKAHHVK TGTCEVVALH RCCNKNKIEE RSQTVKCSCF PGQVAGTTRA APSCVDASIV EQKWWCHMQP CLEGEECKVL PDRKGWSCSS GNKVKTTRVT H Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity is determined by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. recombinant human TAFA-2, immobilized at 6-24 μg/mL on a 96 well plate, is able to significantly enhance neurite outgrowth. 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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Amphiregulin is an EGF related growth factor that signals through the EGF/TGF-α receptor, and stimulates growth of keratinocytes, epithelial cells and some fibroblasts. Amphiregulin also inhibits the growth of certain carcinoma cell lines. Synthesized as a transmembrane protein, Amphiregulin’s extracellular domain is proteolytically processed to release the mature protein. There are 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds essential for biological activity. Recombinant Human Amphiregulin is an 11.3 kDa glycoprotein consisting of 98 amino acid residues.   Product Properties Synonyms AR, AREG, Colorectum Cell-derived Growth Factor, CRDGF Accession P15514 GeneID 374 Source E.coli-derived Human Amphiregulin protein,Val60-Leu108. Molecular Weight Approximately 11.3 kDa. AA Sequence SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK 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 a cell proliferation assay using murine Balb/c 3T3 cells is between 5-10 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2μm 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 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 BD-3 Protein, DEFB-3 Protein, DEFB103 Protein, DEFB3 Protein, BD-3 Protein, BD3 Protein, BP-3 Protein, BP3 Protein Accession P81534 GeneID 55894 Source E.coli-derived human Beta-defensin 3 protein, Gly23-Lys67 Molecular Weight Approximately 5.2 kDa. AA Sequence GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK 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 anti-microbial activity against E.coli. is less than 30 μg/ml, corresponding to a specific activity of > 33.3 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 20 mM PB, pH 7.4, 130 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 °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 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 beta2, Beta-defensin 2, Defensin, beta 2, BD-2 Accession O15263 GeneID 1673 Source E.coli-derived human Beta-defensin 2 protein, Gly24-Pro64 Molecular Weight Approximately 4.3 kDa. AA Sequence GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P 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 immature human dendritic cells is in a concentration range 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 20 mM PB, pH 7.4, 130 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 °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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R-Spondin 1 (RSPO1, Roof plate-specific Spondin 1), also known as cysteine-rich and single thrombospondin domain containing protein 3, is a 27 kDa secreted protein that shares ~40% aa identity with three other R-Spondin family members . All R-Spondins regulate Wnt/ beta-Catenin signaling but have distinct expression patterns. In humans, rare disruptions of the R-Spondin 1 gene are associated with tendencies for XX sex reversal (phenotypic male) or hermaphroditism, indicating a role for R-Spondin 1 in gender- Injection of recombinant R-Spondin 1 in mice causes activation of beta-catenin and proliferation of intestinal crypt epithelial cells, and ameliorates experimental colitis. Interest in R-Spondin 1 as a cell culture supplement has grown with the expansion of the organoid field. R-Spondin 1 is widely used in organoid cell culture workflows as a vital component that promotes both growth and survival of 3D organoids . Product Properties Synonyms R-Spondin 1 ；Roof Plate-specific Spondin 1 Accession Q2MKA7 Source CHO Stable Cells-derived human RSPO1 protein, Met1-Ala 263. Molecular Weight Approximately 26.8 kDa. As a result of glycosylation, the apparent molecular mass of it is approximately 40 and 31 kDa in SDS-PAGE under reducing conditions. AA Sequence MRLGLCVVAL VLSWTHLTIS SRGIKGKRQR RISAEGSQAC AKGCELCSEV NGCLKCSPKL FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE HCEACFSHNF CTKCKEGLYL HKGRCYPACP EGSSAANGTM ECSSPAQCEM SEWSPWGPCS KKQQLCGFRR GSEERTRRVL HAPVGDHAAC SDTKETRRCT VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR RRKGQQQQQQ QGTVGPLTSA GPA     Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE. Biological Activity Measured by its ability to induce activation of ßcatenin response in a Topflash Luciferase assay using HEK293T human embryonic kidney cells. The ED50 for this effect is typically 20-120 ng/mL in the presence of 5 ng/mL recombinant mouse wnt3a. 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℃ 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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Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane SCF is required for normal hematopoietic function. SCF plays an important role in hematopoiesis, spermatogenesis and melanogenesis and it promotes mast cell adhesion, migration, proliferation, and survival. Soluble canine SCF shares 88 %, 93 %, 86 %, 83 %, 76 %, 76 %, 86 % and 88 % a.a. sequence identity with porcine, feline, bovine, human, mouse, rat, goat and equine SCF, respectively. Cells known to express SCF include endothelial cells, fibroblasts and keratinocytes .   Product Properties Synonyms Clo Protein, Con Protein, Gb Protein, Kitlg Protein, Mgf Protein, SCF Protein, SF Protein, Sl Protein, SLF Protein Accession Q06220 GeneID 403507 Source E.coli-derived canine Stem Cell Factor, Lys26-Ala190 Molecular Weight Approximately 18.4 kDa. AA Sequence KGICGKRVTD DVKDVTKLVA NLPKDYKIAL KYVPGMDVLP SHCWISVMVE QLSVSLTDLL DKFSNISEGL SNYSIIDKLV KIVDDLVECT EGYSFENVKK APKSPELRLF TPEEFFRIFN RSIDAFKDLE TVASKSSECV VSSTLSPDKD SRVSVTKPFM LPPVA 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 human TF-1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 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 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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BDNF is a member of the neurotrophin family of growth factors that are required for the differentiation and survival of specific neuronal subpopulations in both the central as well as the peripheral nervous system. Product Properties Synonyms Brain Derived Neurotrophic Factor, Abrineurin Uniprot No. P23560 Source Recombinant Human BDNF Protein is expressed from CHO Cells Cells. It contains His129-Arg247. Molecular Weight 12~14 kDa, on SDS-PAGE under reducing conditions. Biological Activity ED50 < 4.0 μg/ml, measured in a bioassay using C6 cells. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.2 EU per 1μg of the protein by the LAL method. Formulation Lyophilized after extensive dialysis against PBS. Reconstitution It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH2O or PBS up to 100 μg/ml. Shipping and Storage The product should be stored at -85~-65℃ for 6 months from date of receipt. Upon reconstitution, the product should be stable for up to 1 week at 4°C or up to 3 months at -20°C. For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. 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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Cardiotrophin-1 (CT-1) 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). It was originally isolated based on its ability to induce cardiac myocyte hypertrophy in vitro. CT-1 has since been shown to be a pleiotrophic cytokine with overlapping actions with other IL-6 family members on a variety of cell types. Human CT-1 encodes a 201 aa residue protein that lacks a hydrophobic signal peptide. The mechanism of CT-1 release from cells is currently not understood. Human and mouse CT-1 share 80% aa sequence identity and exhibit cross-species activity. CT-1 is highly expressed in heart, skeletal muscle, liver, lung and kidney. Lower levels of CT-1 expression is also seen in testis and brain. CT-1 initiates downstream signaling pathways through the heterodimerization of gp130 and the LIF receptor beta subunit.   Product Properties Synonyms cardiophin 1; Cardiotrophin1; Cardiotrophin-1; CT1; CTF1 Accession Q16619 GeneID 1489 Source E.coli-derived Human CT-1, Met 1-Ala201 Molecular Weight Approximately 21.2 kDa. AA Sequence MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A 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 1.0 ng/ml, corresponding to a specific activity of > 1.0× 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 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°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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Bone morphogenetic protein-4 (BMP-4) is one of nine structurally related BMPs belonging to the transforming growth factor-beta (TGF-beta) superfamily of secreted proteins. The human BMP-4 shares 98 % sequence indentity with mouse BMP-4. Mature BMP-4 is a dimer that binds to a multimeric transmembrane receptor with serine/threonine kinase activity. BMP-4, a stimulator of chondrogenesis, both in vitro and in vivo, is a potential therapeutic agent for cartilage regeneration.   Product Properties   Synonyms BMP2B, BMP-2B, BMP2B1, BMP2BMCOPS6, BMP4,DVR4, MCOPS6, OFC11, ZYME Accession P12644 Source E.coli-derived human BMP-4 protein, Ser293-Arg408, E399D. Molecular Weight The recombinant Human BMP4 predicts a molecular mass of 13.25 kDa. Tag None Purity > 95% by SDS-PAGE Biological Activity Measured by its ability to induce alkaline phosphatase production by MC3T3-E1 mouse osteoblastic cells. The ED50 for this effect is typically 0.08-0.4ug/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from sterile 30% Acetonitrile, 1/1000 TFA. 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 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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FGF basic is a member of the FGF family, currently comprised of seven related mitogenic proteins which show 35 - 55% amino acid conservation. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF basic in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. FGF basic is chemotactic and mitogenic for endothelial cells in vitro. FGF basic induces neuron differentiation, survival and regeneration. FGF basic has also been shown to be crucial in modulating embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Product Properties Synonyms FGF-2, HBGF-2 Accession P03969 GeneID 281161 Source E.coli-derived Bovine bFGF, Pro10-Ser155, with an N-terminal Met. Molecular Weight Approximately 16.5 kDa. AA Sequence MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS 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 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°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 Avoid repeated freeze-thaw cycles. For your safety and health, please wear lab coats and disposable gloves for operation. For research use only!

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IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.   Product Properties Synonyms Interferon gamma；IFN-gamma； Accession P42160 GeneID 100034181 Source E.coli-derived equine Interferon-gamma protein,Gln24-Gln166 Molecular Weight Approximately 16.7 kDa. AA Sequence QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ 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 ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg. Endotoxin < 0.1 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, 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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IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.   Product Properties Synonyms Interferon gamma; IFN-gamma Accession P42161 GeneID 403801 Source E.coli-derived canine Interferon-gamma protein, Gln24-Lys166 Molecular Weight Approximately 16.9 kDa. AA Sequence QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK 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 ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 25 mM Sodium Succinate, pH 5.0, 60 mM NaCl, with 0.1 % 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 °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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The homeostatic chemokine CXCL13 (also called B cell-attracting chemokine 1 [BCA-1] or B-lymphocyte chemoattractant [BLC]) is constitutively expressed in secondary lymphoid tissue and initiates lymphoid neogenesis when expressed aberrantly. Recombinant human CXCL13 is a single non-glycosylated polypeptide chain containing 87 amino acids and mature human BCA-1 shares 64% amino acid sequence similarity with the mouse protein and 23-34% amino acid sequence identity with other known CXC chemokines. CXCL13 is a homeostatic chemokine for lymphocyte homing and positioning within follicles of secondary lymphoid tissues, acting through its cognate receptor, CXCR5. Besides, CXCL13 is a potent chemokine, produced by mature and recently recruited macrophages to sites of inflammation, which has antimicrobial and anti-angiogenic properties.   Product Properties Synonyms Angie, B lymphocyte chemoattractant, BCA1, CXC chemokine BLC, Small-inducible cytokine B13,  SCYB13 Accession O43927 GeneID 10563 Source E.coli-derived Human BCA-1/CXCL13, Val23-Pro109. Molecular Weight Approximately 10.3 kDa. AA Sequence VLEVYYTSLR CRCVQESSVF IPRRFIDRIQ ILPRGNGCPR KEIIVWKKNK SIVCVDPQAE WIQRMMEVLR KRSSSTLPVP VFKRKIP 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 B cells 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, pH 7.4, 100 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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AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant Human soluble AITRL is a 14.4 kDa protein, containing 127 amino acid residues corresponding to the extracellular domain of AITRL.   Product Properties Synonyms Human Endostatin Accession Q9UNG2 GeneID 8995 Source E.coli-derived Human AITR Ligand protein,Glu74-Leu251. Molecular Weight Approximately 14.3 kDa. AA Sequence ETAKEPCMAK FGPLPSKWQM ASSEPPCVNK VSDWKLEILQ NGLYLIYGQV APNANYNDVA PFEVRLYKNK DMIQTLTNKS KIQNVGGTYE LHVGDTIDLI FNSEHQVLKN NTYWGIILLA NPQFIS 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 as determined by stimulation of IL-8 production using human PBMC is in a concentration range of 0.1-10 ng/mL. 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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4-1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4-1BBL binds to its receptor 4-1BB, and provides a co-stimulatory signal for T cell activation and expansion. The human 4-1BBL gene codes for a 254 amino acid type II transmembrane containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane protein domain, and a 205 amino acid extracellular domain. The soluble form of 4-1BBL contains the TNF-like portion of the extracellular domain of 4-1BBL. Recombinant Human 4-1BBL is a soluble 19.5 kDa protein consisting of 185 amino acid residues.   Product Properties Synonyms TNFSF9, CD137L Accession P41273 GeneID 8744 Source E.coli-derived Human 4-1BB Ligand/TNFSF9 protein,Arg71-Glu254. Molecular Weight Approximately 19.4 kDa. AA Sequence REGPELSPDD PAGLLDLRQG MFAQLVAQNV LLIDGPLSWY SDPGLAGVSL TGGLSYKEDT KELVVAKAGV YYVFFQLELR RVVAGEGSGS VSLALHLQPL RSAAGAAALA LTVDLPPASS EARNSAFGFQ GRLLHLSAGQ RLGVHLHTEA RARHAWQLTQ GATVLGLFRV TPEIPAGLPS PRSE 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 stimulation of IL-8 production using human PBMC is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 105 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 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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BAFF Receptor (BAFFR), a member of the TNFR superfamily, is highly expressed in the spleen, lymph nodes, and resting B cells, and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFFR is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B).  BAFFR/BAFF signaling plays a critical role in B cell survival and maturation.  Human and mouse BAFF R share 56% aa sequence identity. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, in resting CD4+ T cells, in thymus and peripheral blood leukocytes. BAFF knockout mice lack mature B cells. Similarly, A/WySnJ mice that are defective in BAFF-R intracellular signaling also lack mature B cells, suggesting that BAFF R is the critical receptor for BAFF during B lymphopoiesis. In contrast, BCMA- or TACI-deficient mice have no major defect in B-cell development. While the function of BCMA is not defined, TACI has been shown to control B-cell homeostasis and T-cell-independent immune responses.   Product Properties Synonyms BAFFR, TNFRSF13C Accession Q96RJ3 GeneID 115650 Source E.coli-derived Human B cell Activating Factor Rececptor protein,Met1-Gly76,with an N-terminal Met Molecular Weight Approximately 7.8 kDa AA Sequence MRRGPRSLRG RDAPAPTPCV PAECFDLLVR HCVACGLLRT PRPKPAGASS PAPRTALQPQ ESVGAGAGEA ALPLPG 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 its ability to block BAFF induced mouse splenocyte survival is 1.0-5.0 μg/ml in the presence of 1.0 μg/ml of rHuBAFF. Endotoxin < 1 EU/μg of protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 8.0, 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°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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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 27% amino acid (aa) identity in equine. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1 alpha and IL-1 beta are regulated independently, they bind to the same receptor and exert identical biological effects. IL-1 RI binds directly to IL-1 alpha or IL-1 beta and then associates with IL-1R accessory protein (IL-1 R3/IL-1 R AcP) to form a high-affinity receptor complex that is competent for signal transduction. IL-1RII has high affinity for IL-1 beta but functions as a decoy receptor and negative regulator of IL-1 beta activity. IL-1ra functions as a competitive antagonist by preventing IL-1 alpha and IL-1 beta from interacting with IL-1 RI. The equine IL-1 beta cDNA encodes a 268 aa precursor. A 115 aa propeptide is cleaved intracellularly by the cysteine protease IL-1 beta -converting enzyme (Caspase-1/ICE) to generate the active cytokine. An alternatively spliced form of equine IL-1 beta has a deletion which encompasses the Caspase-1 cleavage site and potentially results in a membrane-associated form. The 17 kDa mature equine IL-1 beta shares 65%-75% aa sequence identity with canine, cotton rat, feline, human, mouse, porcine, rat, and rhesus IL-1 beta.   Product Properties Synonyms IL-1 beta Accession Q28386 GeneID 100034237 Source E.coli-derived Equine IL-1β, Ala116-Ala268. Molecular Weight Approximately 17.3 kDa. AA Sequence AAMHSVNCRL RDIYHKSLVL SGACELQAVH LNGENTNQQV VFCMSFVQGE EETDKIPVAL GLKEKNLYLS CGMKDGKPTL QLETVDPNTY PKRKMEKRFV FNKMEIKGNV EFESAMYPNW YISTSQAEKS PVFLGNTRGG RDITDFIMEI TSA 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 murine D10S cells is less than 20 pg/mL, corresponding to a specific activity of > 5.0 × 107 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, 0.1 % 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°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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CCL20, also known as LARC (Liver and Activation-regulated Chemokine) or MIP3A(Macrophage Inflammatory Protein-3), is a small cytokine belonging to the CC chemokine family. CCL20 is Expressed predominantly in the liver, lymph nodes, appendix, peripheral blood lymphocytes, and fetal lung. The expression of CCL20 is strongly up-regulated by inflammatory signals and down-regulated by the anti-inflammatory cytokine IL-10. CCL20 has been shown to be chemotactic for lymphocytes. This chemokine may Inhibit proliferation of myeloid progenitors in colony formation assays and it may be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. Chemokine CCL2 was shown to play a role in colorectal cancer (CRC) pathogenesis. Product Properties Synonyms LARC, Beta-chemokine Exodus-1, Liver and Activation-regulated Chemokine Accession P78556 GeneID 6364 Source E.coli-derived Human MIP-3α/CCL20, Ala27-Met96. Molecular Weight Approximately 8.0 kDa. AA Sequence ASNFDCCLGY TDRILHPKFI VGFTRQLANE GCDINAIIFH TKKKLSVCAN PKQTWVKYIV RLLSKKVKNM 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 T-lymphocytes is in a concentration range of 10-50 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, pH 7.4, 100 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°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 Avoid repeated freeze-thaw cycles. For your safety and health, please wear lab coats and disposable gloves for operation. For research use only!

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Interleukin-1 alpha (IL1a) is also known as IL-1A, IL1,and is a cytokine of the interleukin-1 family. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human IL-1 has been found to be biologically active on murine cell lines. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. IL-1 is a major immunoregulatory/proinflammatory cytokine which also affects fibroblast proliferation and function and therefore it was of interest to investigate whether its constitutive expression influences the in vivo tumorigenic potential of transformed fibroblastoid cell lines.   Product Properties   Synonyms Interleukin-1 alpha, IL-1α, BAF, IL-1F1, LAF, LEM, preinterleukin 1 alpha, pro-interleukin-1-alpha. Source E.coli-derived human IL-1alpha protein, Ser113-Ala271. AA sequence SAPFSFLSNV KYNFMRIIKY EFILNDALNQ SIIRANDQYL TAAALHNLDE AVKFDMGAYK SSKDDAKITV ILRISKTQLY VTAQDEDQPV LLKEMPEIPK TITGSETNLL FFWETHGTKN YFTSVAHPNL FIATKQDYWV CLAGGPPSIT DFQILENQA Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is 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. Source E.coli-derived human IL-1β protein, Ala117-Ser269. AA sequence APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVALGLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The products are shipped with ice pack and can be stored at -20 ℃ 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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IL-1ra was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The naturally occurring, fully glycosylated form has an apparent molecular weight of about 25,000 Daltons. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha. It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptor (I and II) on human cells, but reportedly will not block binding to the type II receptor on murine pre-B cell lines. The recombinant, non-glycosylated form of IL-1ra blocks binding of IL-1 to its receptor equally as well as the naturally-occurring, glycosylated form. The IL-1ra has been shown to block the inflammatory responses induced by IL-1 both in vitro and in vivo. Currently, pre-clinical and clinical studies are underway to test possible therapeutic applications for IL-1ra in the treatment of sepsis, rheumatoid arthritis and chronic myelogenous leukemia.   Product Properties   Synonyms IL-1RN, IRAP Source E.coli-derived Human IL-1RA, Arg26-Glu177. AA sequence RPSGRKSSKM QAFRIWDVNQ KTFYLRNNQL VAGYLQGPNV NLEEKIDVVP IEPHALFLGI HGGKMCLSCV KSGDETRLQL EAVNITDLSE NRKQDKRFAF IRSDSGPTTS FESAACPGWF LCTAMEADQP VSLTNMPDEG VMVTKFYFQE DE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 96% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The products are shipped with ice pack and can be stored at -20 ℃ 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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The human IL-2 protein, also known as interleukin-2, is an important cytokine that plays a vital role in regulating the immune system. It is produced by activated T cells and stimulates the proliferation and activation of various immune cells, such as T cells, B cells, and natural killer cells. IL-2 also promotes the development of immune memory and enhances the effectiveness of the immune response against infections and cancers. In addition, IL-2 has been used therapeutically in the treatment of certain diseases, such as cancer and autoimmune disorders, to boost the immune system.   Product Properties   Synonyms Interleukin-2; T-Cell Growth Factor; TCGF; Aldesleukin Source HEK293 cells-derived human IL-2 protein, Ala21-Thr153, with N-terminal his tag. AA sequence RPSGRKSSKM QAFRIWDVNQ KTFYLRNNQL VAGYLQGPNV NLEEKIDVVP IEPHALFLGI HGGKMCLSCV KSGDETRLQL EAVNITDLSE NRKQDKRFAF IRSDSGPTTS FESAACPGWF LCTAMEADQP VSLTNMPDEG VMVTKFYFQE DE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 90% as determined by SDS-PAGE. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   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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Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation. At the amino acid sequence level, mature human and murine IL-3 share only 29% sequence identity. Consistent with this lack of homology, IL-3 activity is highly species-specific and human IL-3 does not show activity on murine cells. Cytokines are actively involved in the host-defense system to coordinate the functional activity and the generation of effector cells. Some of these molecules function as inflammatory mediators and hematopoietic growth factors at the same time such as IL-3. IL-3 (or multi-CSF) is known as a pleiotropic cytokine with a broad spectrum of target cells and functions. IL-3 regulates the proliferation and differentiation of normal hematopoietic progenitor cells in the early stages of hematopoiesis. And IL-3 inhibits apoptosis and promotes the autonomous growth of blast cells.   Product Properties   Synonyms Interleukin-3, IL-3, Hematopoietic growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor Source E.coli-derived human IL-1alpha protein, Ala20-Phe152. AA sequence APMTQTTSLK TSWVNCSNMI DEIITHLKQP PLPLLDFNNL NGEDQDILME NNLRRPNLEA FNRAVKSLQN ASAIESILKN LLPCLPLATA APTRHPIHIK DGDWNEFRRK LTFYLKTLEN AQAQQTTLSL AIF Endotoxin < 1.0 EU per μg by the LAL method. Purity > 96% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The product should be stored at -25~-15℃ for 1 year from date of receipt. 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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines. Unlike other family members, it is present as a covalently linked antiparallel dimer. The cDNA for human IL-5 encodes a signal peptide and a 115 amino acid (aa) mature protein. Mature human IL-5 shares 70%, 70%, 62%, 71%, 70% and 66%, aa sequence identity with mouse, rat, canine, equine, feline and porcine IL-5, respectively and shows cross-reactivity with mouse IL-5. IL-5 is primarily produced by CD4+ Th2 cells, but also by activated eosinophils, mast cells, EBV-transformed B cells, Reed-Sternberg cells in Hodgkin’s disease, and IL- 2-stimulated invariant natural killer T cells (iNKT). IL-5 increases production and mobilization of eosinophils and CD34+ progenitors from the bone marrow and causes maturation of eosinophil precursors outside the bone marrow. The receptor for human IL-5, mainly expressed by eosinophils, but also found on basophils and mast cells, consists of a unique ligand-binding subunit (IL-5 R alpha ) and a shared signal-transducing subunit, beta. IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor.   Product Properties   Synonyms B-cell differentiation factor I, Eosinophil differentiation factor, TRF Source E.coli-derived human IL-5 protein, Ile20-Ser134,with an N-terminal Met. AA sequence MIPTEIPTSA LVKETLALLS THRTLLIANE TLRIPVPVHK NHQLCTEEIF QGIGTLESQT VQGGTVERLF KNLSLIKKYI DGQKKKCGEE RRRVNQFLDY LQEFLGVMNT EWIIES Endotoxin < 1.0 EU per μg by the LAL method. Purity > 98% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20mM PB, pH 7.5, 3% trehalose, 0.1% Tween-80. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃. 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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IL-6 is similar to other interleukins in that it has a compact globular folding structure and is held in place by two disulfide bonds. The cysteine involved in forming these two disulfide bonds is highly conserved. IL-6, expressed by a variety of cells, regulates cell growth and differentiation in various tissues and is an important pro-inflammatory and immunomodulatory cytokine.   Product Properties   Synonyms Interleukin-6,BSF2,HSF,IFNB2 Source Recombinant Human IL-6 Protein is expressed from E.coli without tag. It contains Val30-Met212. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Normally 8% trehalose is added as protectant before lyophilization. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in distilled water.   Storage   The products are shipped with ice pack and can be stored at -20 ℃ for 1 year.  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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Interleukin 9, also known as IL-9, is a cytokine (cell signaling molecule) belonging to the group of interleukins. IL-9 is a cytokine that acts as a regulator of a variety of hematopoietic cells. This cytokine stimulates cell proliferation and prevents apoptosis. It functions through the interleukin 9 receptor (IL-9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.   Product Properties   Synonyms Cytokine P40, T-cell Growth Factor P40 Source E.coli-derived human IL-1alpha protein, Gln19-Ile144. AA sequence QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKI 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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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 Source E.coli-derived human IL-10 protein, Ser19-Asn178. AA sequence SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin 11 (IL-11), a member of the IL-6 family of cytokines, exerts pleiotropic activities by stimulating hemopoiesis and thrombopoiesis, regulating macrophage differentiation, and conferring mucosal protection in the intestine. These effects are mediated by a multimeric complex comprising the ligand-binding IL-11R± and the ubiquitously expressed gp130R-subunit, which together, trigger intracellular signaling and engagement of Stat3. Mature human IL-11 shares 88%, 88%, and 96% aa sequence identity with mouse, rat and canine IL-11, respectively. IL-11 is a pleotropic cytokine produced by lung stromal cells in response to respiratory viruses, cytokines, and histamine. The functions of IL-11 are that it directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation resulting in increased platelet production.   Product Properties   Synonyms Adipogenesis inhibitory factor, AGIF, IL-11, IL-11Oprelvekin, interleukin 11, interleukin-11, Oprelveki Source E.coli-derived human IL-11, Pro22-Leu199, with an N-terminal Met. AA sequence MPGPPPGPPR VSPDPRAELD STVLLTRSLL ADTRQLAAQL RDKFPADGDH NLDSLPTLAM SAGALGALQL PGVLTRLRAD LLSYLRHVQW LRRAGGSSLK TLEPELGTLQ ARLDRLLRRL QLLMSRLALP QPPPDPPAPP LAPPSSAWGG IRAAHAILGG LHLTLDWAVR GLLLLKTRL 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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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 Source E.coli-derived Human IL-13, Gly35-Asp146. AA sequence GPVPPSTALR ELIEELVNIT QNQKAPLCNG SMVWSINLTA GMYCAALESL INVSGCSAIE KTQRMLSGFC PHKVSAGQFS SLHVRDTKIE VAQFVKDLLL HLKKLFREGR FN Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4 with 5% trehalose. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with 20 mM HCl to a concentration of 0.1-1.0 mg/mL.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Human Interleukin-15 (IL-15) is a widely expressed 14 kDa cytokine that is plays an important role in many immunological diseases. It shares approximately 97% and 73% sequence identity with simian and murine IL-15, respectively. Both human and simian IL-15 are active on murine cells. IL-15 is secreted by mononuclear phagocytes (and some other cells), especially macrophages following infection by virus. IL-15 and IL-2 have similar biologic properties in vitro, consistent with their shared receptor (R) signaling components (IL-2/15Rβγc). A role for IL-15 during autoimmune processes such as rheumatoid arthritis and malignancies such as adult T-cell leukemia suggest that dysregulation of IL-15 may result in deleterious effects for the host.   Product Properties   Synonyms Interleukin-15, IL-15, MGC972 Source E.coli-derived human IL-15 protein, Asn49-Ser162. AA sequence NWVNVISDLK KIEDLIQSMH IDATLYTESD VHPSCKVTAM KCFLLELQVI SLESGDASIH DTVENLIILA NNSLSSNGNV TESGCKECEE LEEKNIKEFL QSFVHIVQMF INTS Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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IL17, also known as IL17a, is a cytokine that belongs to the IL-17 family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. The IL-17 family of cytokines includes six members, IL-17/IL-17A, IL-17B, IL-17C, IL-17D, IL-17E/IL-25, and IL-17F, which are produced by multiple cell types. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis, and multiple sclerosis.   Product Properties   Synonyms Cytotoxic T-lymphocyte-associated antigen 8, CLTA-8 , IL-17A Source E.coli-derived human IL-17 protein,Gly24-Ala155 AA sequence GITIPRNPGC PNSEDKNFPR TVMVNLNIHN RNTNTNPKRS SDYYNRSTSP WNLHRNEDPE RYPSVIWEAK CRHLGCINAD GNVDYHMNSV PIQQEILVLR REPPHCPNSF RLEKILVSVG CTCVTPIVHH VA 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in 4 mM HCl to a concentration of 0.1-1.0 mg/mL.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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The Interleukin 17B (IL-17) family proteins, comprising six members (IL-17, IL-17B through IL-17F), are secreted, structurally related proteins that share a conserved cystine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus (1, 2). With the exception of IL-17B, which exists as a non- covalently linked dimer, all IL-17 family members are disulfide-linked dimers (3). IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions (1, 2). Two receptors (IL- 17 R, and IL-17B R), which are activated by IL-17 family members, have been identified. In addition, at least three additional orphan type I transmembrane receptors with homology to IL-17 R, including IL-17 RL (IL-17 RC), IL-17 RD, and IL- 17 RE, have also been reported (1- 4). Human IL-17B cDNA encodes a 180 aa protein with a putative 20 aa signal peptide (5, 6). Human and mouse IL-17B share 88% amino acid sequence identity. Among IL-17 family members, IL-17B is most closely related to IL-17D, sharing 27% aa sequence homology. IL-17B is expressed highly in spinal cord, and at lower levels in brain, kidney, lung, small intestine, prostate, testes, pancreas, adrenal gland and trachea (5- 7). Expression of IL-17B has also been detected in chondrocytes in articular cartilage (2). IL-17B binds the IL-17B receptor but not IL-17 R and exhibits bioactivities distinct from those of IL-17 (5, 6).   Product Properties   Synonyms IL-17B Source E.coli-derived human IL-17B protein, Gln21-Phe180, with an N-terminal Met. AA sequence MQPRSPKSKR KGQGRPGPLA PGPHQVPLDLVSRMKPYARM EEYERNIEEM VAQLRNSSEL AQRKCEVNLQ LWMSNKRSLS PWGYSINHDP SRIPVDLPEA RCLCLGCVNP FTMQEDRSMV SVPVFSQVPV RRRLCPPPPR TGPCRQRAVM ETIAVGCTCI F 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 0.1% Tween-20 and 3% Trehalose. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA.   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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The Interleukin 17F (IL-17) family proteins, comprising six members (IL-17, IL-17B through IL-17F), are secreted, structurally related proteins that share a conserved cystine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non- covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Two receptors (IL- 17 R, and IL-17B R), which are activated by IL-17 family members, have been identified. In addition, at least three additional orphan type I transmembrane receptors with homology to IL-17 R, including IL-17 RL (IL-17 RC), IL-17 RD, and IL- 17 RE, have also been reported. Human IL-17B cDNA encodes a 180 aa protein with a putative 20 aa signal peptide. Human and mouse IL-17B share 88% amino acid sequence identity. Among IL-17 family members, IL-17B is most closely related to IL-17D, sharing 27% aa sequence homology. IL-17B is expressed highly in spinal cord, and at lower levels in brain, kidney, lung, small intestine, prostate, testes, pancreas, adrenal gland and trachea . Expression of IL-17B has also been detected in chondrocytes in articular cartilage. IL-17B binds the IL-17B receptor but not IL-17 R and exhibits bioactivities distinct from those of IL-17.   Product Properties   Synonyms ML-1, IL-24 Source E.coli-derived human IL-17F protein, Arg31-Gln163, with an N-terminal Met. AA sequence MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in 6 mM HCl to a concentration of 0.1 mg/ml.   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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IL-20 belongs to the IL-10 family. It is a cytokine structurally related to interleukin 10. Human IL-20 is synthesized as a 176 amino acid (aa) precursor with a 24 aa signal sequence and a 152 aa mature segment. IL-20 production has been found in skin, trachea, and other tissues. In particular, it is produced by activated keratinocytes and monocytes. It has been shown that IL-20 transduces its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. It may be involved in epidermal function and psoriasis. It also regulates the proliferation and differentiation of keratinocytes during inflammation, particularly inflammation associated with the skin. Also, it is reported to induce the proliferation of multipotential hematopoietic progenitor cells, direct the differentiation and expansion of keratinocytes, and promote the release of proinflammatory mediators in keratinocytes and other IL-20 receptor expressing cells.   Product Properties   Synonyms Cytokine Zcyto10 Source E.coli-derived Human IL-20, Leu25-Glu176, with an N-terminal Met. AA sequence MLKTLNLGSC VIATNLQEIR NGFSEIRGSV QAKDGNIDIR ILRRTESLQD TKPANRCCLL RHLLRLYLDR VFKNYQTPDH YTLRKISSLA NSFLTIKKDL RLCHAHMTCH CGEEAMKKYS QILSHFEKLE PQAAVVKALG ELDILLQWME ETE  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 7.2, with trehalose. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA.   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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Hunan IL-21 protein is a molecule that is found in the immune system of individuals. It is a type of interleukin, which is a protein that helps in the communication between immune cells. IL-21 plays a crucial role in regulating the body's immune response, specifically in the development, differentiation, and function of certain immune cells, such as T cells and natural killer cells.   Product Properties   Synonyms Interleukin-21, IL-21, Za11 Source HEK293 cells-derived human IL-21 protein, Gln30-Ser162, with N-terminal Flag tag. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   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.   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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Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Human IL-22 cDNA encodes a 179 amino acid (aa) residue protein with a putative 33 aa signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with mouse IL-22 and human IL-10, respectively. The human IL-22 gene is localized to chromosome 12q15. Although it exists as a single copy gene in human and in many mouse strains, the mouse IL-22 gene is duplicated in some mouse strains including C57B1/6, FVB and 129. The two mouse genes designated IL-TIF alpha and IL-TIF beta, share greater than 98% sequence homology in their coding region. IL-22 has been shown to activate STAT- 1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal T cells upon anti-CD3 stimulation in humans. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R beta (previously known as CRF2-4), belonging to the class II cytokine receptor family.   Product Properties   Synonyms Cytokine Zcyto 18, TIF Source E.coli-derived human IL-22 protein, Ala34-Ile179. AA sequence MAPISSHCRL DKSNFQQPYI TNRTFMLAKE ASLADNNTDV RLIGEKLFHG VSMSERCYLM KQVLNFTLEE VLFPQSDRFQ PYMQEVVPFL ARLSNRLSTC HIEGDDLHIQ RNVQKLKDTV KKLGESGEIK AIGELDLLFM SLRNACI  Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 5.0. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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IL-33, also known as interleukin-33, is a protein that belongs to the IL-1 superfamily. It is primarily produced by epithelial and endothelial cells and acts as an important cytokine involved in immune response and inflammation. IL-33 functions as an alarmin, which means it is released upon tissue damage and initiates an inflammatory response to recruit immune cells to the site of injury.   Product Properties   Synonyms IL33, DV27, C9ORF26, IL1F11, NFHEV, DKFZp586H0523, DVS27, NFEHEV, RP11-575C20.2 Source E.coli-derived human IL-33 protein, His109-Thr 270, with C-terminal His tag. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 90% by SDS-PAGE analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   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.   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 IL-36 alpha, previously called IL-1F6 and FIL1 epsilon (family of IL-1 member epsilon), is a member of the IL-1 family which includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18, and novel family members IL-36 Ra (IL-1F5), IL-36 beta (IL-1F8), IL-36 gamma (IL-1F9), IL-37 (IL-1F7) and IL- 38 (IL- 1F10) . All family members show a 12 beta -strand, beta -trefoil configuration, and are believed to have arisen from a common ancestral gene. IL-36 alpha is an 18- 22 kDa, 158 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential from N-linked glycosylation sites. It can be released in response to LPS and the cell ATP-induced activation of the P2X7 receptor. A 120 aa isoform missing aa 1- 38 has been reported. Human IL- 36 alpha (aa 6 - 158) shares 57- 68% aa sequence identity with mouse, rabbit, equine and bovine IL- 36 alpha and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid  tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes, B and T cells. The receptor for IL- 36 alpha is a combination of IL- 1 Rrp2 (also called IL1RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL-36 alpha, beta, and gamma all activate NF-kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL-8. IL-36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL-36 alpha is present in kidney tubule epithelia, and it is highly expressed in intubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. Product Properties   Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Source E.coli-derived human IL-36 alpha protein, Met1-Phe158. AA sequence MEKALKIDTP QQGSIQDINH RVWVLQDQTL IAVPRKDRMS PVTIALISCR HVETLEKDRG NPIYLGLNGL NLCLMCAKVG DQPTLQLKEK DIMDLYNQPE PVKSFLFYHS QSGRNSTFES VAFPGWFIAV SSEGGCPLIL TQELGKANTT DFGLTMLF 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 2 × PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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Human IL-36 alpha, previously called IL-1F6 and FIL1 epsilon (family of IL-1 member epsilon), is a member of the IL-1 family which includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18, and novel family members IL-36 Ra (IL-1F5), IL-36 beta (IL-1F8), IL-36 gamma (IL-1F9), IL-37 (IL-1F7) and IL- 38 (IL- 1F10) . All family members show a 12 beta -strand, beta -trefoil configuration, and are believed to have arisen from a common ancestral gene. IL-36 alpha is an 18- 22 kDa, 158 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential from N-linked glycosylation sites. It can be released in response to LPS and the cell ATP-induced activation of the P2X7 receptor. A 120 aa isoform missing aa 1- 38 has been reported. Human IL- 36 alpha (aa 6 - 158) shares 57- 68% aa sequence identity with mouse, rabbit, equine and bovine IL- 36 alpha and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid  tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes, B and T cells. The receptor for IL- 36 alpha is a combination of IL- 1 Rrp2 (also called IL1RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL-36 alpha, beta, and gamma all activate NF-kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL-8. IL-36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL-36 alpha is present in kidney tubule epithelia, and it is highly expressed in intubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. Product Properties   Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Source E.coli-derived human Interleukin-36 alpha protein, Lys6-Phe158. AA sequence KIDTPQQGSI QDINHRVWVL QDQTLIAVPR KDRMSPVTIA LISCRHVETL EKDRGNPIYL GLNGLNLCLM CAKVGDQPTL QLKEKDIMDL YNQPEPVKSF LFYHSQSGRN STFESVAFPG WFIAVSSEGG CPLILTQELG KANTTDFGLT MLF 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 20 mM Tris, 300 mM NaCl, pH 8.0, 0.1% Tween 80. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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Interleukin-36 Beta Human Recombinant Shipping: Synonyms Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882. Introduction Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner. Description IL36B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.7kDa. Product Properties   Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Source E.coli-derived human Interleukin-36 beta protein, Met1-Glu157, with an N-terminal Met. AA sequence MNPQREAAPK SYAIRDSRQM VWVLSGNSLI AAPLSRSIKP VTLHLIACRD TEFSDKEKGN MVYLGIKGKD LCLFCAEIQG KPTLQLKEKN IMDLYVEKKA QKPFLFFHNK EGSTSVFQSV SYPGWFIATS TTSGQPIFLT KERGITNNTN FYLDSVE 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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Interleukin-36 Beta Human Recombinant Shipping: Synonyms Interleukin 36 beta, interleukin 1 family member 8, Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily, IL1H2, MGC126880, MGC126882. Introduction Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Product Properties   Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Source E.coli-derived human Interleukin-36 beta protein, Arg5-Glu157. AA sequence REAAPKSYAI RDSRQMVWVL SGNSLIAAPL SRSIKPVTLH LIACRDTEFS DKEKGNMVYL GIKGKDLCLF CAEIQGKPTL QLKEKNIMDL YVEKKAQKPF LFFHNKEGST SVFQSVSYPG WFIATSTTSG QPIFLTKERG ITNNTNFYLD SVE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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IL-36 gamma [previously called IL-1F9, IL-1 epsilon (epsilon), and IL-1H1] is a member of the IL-1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, IL- 36 Ra (IL- 1F5), IL-36 alpha (IL- 1F6), IL- 36 beta (IL- 1F8), IL- 37 (IL- 1F7) and IL-1F10. All family members show a 12 beta -strand, beta -trefoil configuration, and are believed to have arisen from a common ancestral gene. IL- 36 gamma is an 18- 22 kDa, 169 amino acid intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL- 36 gamma (aa 18- 169) shares 58%, 59%, 68% and 69% aa sequence identity with mouse, rat, bovine and equine IL- 36 gamma, respectively, and 23- 57% aa sequence identity with other family members. 134 aa isoform missing aa 19- 53 has been reported. Highest levels of IL- 36 gamma are produced by Langerhans cells, keratinocytes, and stomach Chief cells and parietal cells; these cells contribute to first-line defense against pathogens in the skin, lungs and  digestive tract. Its expression is induced by LPS treatment of monocytes, and by IL- alpha / beta, IL- 17 or TNF- alpha treatment of keratinocytes and bronchial epithelia. Skin IL-36 gamma expression is increased in contact hypersensitivity and psoriasis. It is elevated in inflammatory disorders of the lung (such as asthma) and viral infections. Lung IL- 36 gamma and other IL- 36 proteins contribute to neutrophil influx. The receptor for IL-36 gamma is a combination of IL- 1 Rrp2, mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha,beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and IL- 36 gamma induces production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. Product Properties   Synonyms IL-1RP2, IL-1 epsilon, IL-1F9, IL-1H1 Source E.coli-derived human Interleukin-36 gamma protein, Met1-Asp169, with an N-terminal Met. AA sequence MRGTPGDADG GGRAVYQSMC KPITGTINDL NQQVWTLQGQ NLVAVPRSDS VTPVTVAVIT CKYPEALEQG RGDPIYLGIQ NPEMCLYCEK VGEQPTLQLK EQKIMDLYGQ PEPVKPFLFY RAKTGRTSTL ESVAFPDWFI ASSKRDQPII LTSELGKSYN TAFELNIND 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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IL-36 gamma [previously called IL-1F9, IL-1 epsilon (epsilon), and IL-1H1] is a member of the IL-1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, IL- 36 Ra (IL- 1F5), IL-36 alpha (IL- 1F6), IL- 36 beta (IL- 1F8), IL- 37 (IL- 1F7) and IL-1F10. All family members show a 12 beta -strand, beta -trefoil configuration, and are believed to have arisen from a common ancestral gene. IL- 36 gamma is an 18- 22 kDa, 169 amino acid intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL- 36 gamma (aa 18- 169) shares 58%, 59%, 68% and 69% aa sequence identity with mouse, rat, bovine and equine IL- 36 gamma, respectively, and 23- 57% aa sequence identity with other family members. 134 aa isoform missing aa 19- 53 has been reported. Highest levels of IL- 36 gamma are produced by Langerhans cells, keratinocytes, and stomach Chief cells and parietal cells; these cells contribute to first-line defense against pathogens in the skin, lungs and  digestive tract. Its expression is induced by LPS treatment of monocytes, and by IL- alpha / beta, IL- 17 or TNF- alpha treatment of keratinocytes and bronchial epithelia. Skin IL-36 gamma expression is increased in contact hypersensitivity and psoriasis. It is elevated in inflammatory disorders of the lung (such as asthma) and viral infections. Lung IL- 36 gamma and other IL- 36 proteins contribute to neutrophil influx. The receptor for IL-36 gamma is a combination of IL- 1 Rrp2, mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha,beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and IL- 36 gamma induces production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. Product Properties   Synonyms IL-1RP2, IL-1 epsilon, IL-1F9, IL-1H1 Source E.coli-derived human Interleukin-36 gamma protein, Ser18-Asp169. AA sequence SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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Human interleukin-36 receptor antagonist IL-36Ra; previously IL-1F5 and also named FIL-1δ (delta), IL- 1HY1, IL- 1H3, and IL-1L1 is a member of the IL- 1 family of proteins. IL- 1 family members include IL-1 beta, IL-1 alpha, IL-1ra, IL- 18 and IL-1F5-F10. All family members show a 12 beta -strand, beta -trefoil configuration, and all family members are believed to have arisen from a common ancestral gene that underwent multiple duplications . The human IL- 36Ra/IL- 1F5 gene is in closest proximity to the gene for IL-1ra and is likely a relatively recent duplication of the IL-1ra gene. IL-36Ra/IL-1F5 is synthesized as a 155 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site(s). Nevertheless, it appears to be secreted as a 17 kDa monomer. There is an alternate start site that potentially gives rise to an alternate splice form. The translated product, however, has a premature stop codon, resulting in a truncated 16 aa peptide. Human to mouse, full length IL-1F5 has 90% aa identity. Within the family, IL-36Ra/IL-1F5 is 50% aa identical to IL-1ra, and 32%, 31%, 35%, 37%, 32% and 42% aa identical to IL-1 beta, IL-36 alpha /IL- 1F6, IL- 37/IL- 1F7, IL- 36 beta /IL- 1F8, IL- 36 gamma /IL- 1F9 and IL- 1F10, respectively. Cells reported to expressIL- 36Ra/IL- 1F5 include monocytes, B cells, dendritic cells/Langerhans cells, keratinocytes, and gastric fundus Parietal and Chief cells. The receptor for IL-36Ra/IL-1F5 has not been positively identified. Indirect evidence suggests it is IL-1 Rrp2 and/or IL-1 RAcP. In either case, activity association with receptor binding is also unclear. It was initially reported to be an antagonist of IL- 36 gamma /IL- 1F9 activity. This would be consistent with its hypothesized relationship to IL- 1ra. Studies, however, find IL-36Ra/IL-1F5 antagonist activity difficult to demonstrate. Product Properties   Synonyms IL-1RP3, IL-1HY1, IL-1 delta, IL-1F5, IL-1ra homolog 1, IL-1L1 Source E.coli-derived human Interleukin-36 Receptor Antagonist protein, Val2-Asp155. AA sequence VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAGKVIKGEE ISVVPNRWLD ASLSPVILGV QGGSQCLSCG VGQEPTLTLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTVPEADQPV RLTQLPENGG WNAPITDFYF QQCD 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. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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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