Betacellulin (BTC) is a new member of the EGF family of cytokines that is comprised of at least ten proteins including EGF, TGF-alpha, amphiregulin, HB-EGF, and the various heregulins. All of these cytokines are synthesized as transmembrane precursors
and are characterized by the presence of one or more EGF structural units in their extracellular domain. The soluble forms of these cytokines are released by proteolytic cleavage. BTC, a heparin-binding protein, was originally isolated from the conditioned media of mouse pancreatic beta tumor cells as a 32 kDa glycoprotein composed of 80 amino acid residues. The cDNA encoding human BTC was cloned from a human breast adenocarcinoma cell line (MCF-7) cDNA library. Human and mouse cDNAs encode BTC precursor proteins of 178 and 177 amino acid residues, respectively. At the amino acid sequence level, human BTC precursor protein exhibits 79% identity with that of the mouse BTC precursor. In a mouse cell line transfected with human BTC cDNA, three forms of soluble human BTC have been detected: the glycosylated, intact BTC composed of 80 amino acid residues, a truncated molecule lacking 12 amino acid residues from the amino terminus, and a second truncated molecule lacking 30 amino acid residues from the amino terminus. The biological activities of these BTC forms were shown to be identical. BTC can bind to the EGF receptor and is a potent mitogen for Balb/c 3T3 fibroblasts, retinal pigment epithelial cells and vascular smooth muscle cells.
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.
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!
