Mouse Betacellulin is a single type I membrane protein which belongs to the EGF family of cytokines. EGF family has many members including EGF, TGF-a, Amphiregulin, HB-EGF, Epiregulin, Tomoregulin and the Neuregulins. Betacellulin is characterised by a six-cysteine consensus motif that forms three intra-molecular disulfide bonds crucial for binding the ErbB receptor family. Betacellulin is expressed in several tissues and tumor cells including kidney, uterus, liver, pancreas and small intestine. Betacellulin binds and activates ErbB-1 and ErbB-4 homodimers. Betacellulin is thought to play a role in the differentiation of pancreatic beta cells.Human and mouse mature BTC protein are 80% identical at the amino acid sequence level. Betacellulin is involved in many biological processes such as stimulating gastrointestinal growth. It is proteolytically processed from a larger membrane-anchored precursor and is a potent mitogen for a wide variety of cell types.
Betacellulin(Betacellulin/BTC) is a member of the epidermal growth factor (EGF) family. These soluble proteins are ligands for one or more of the four receptor tyrosine kinases encoded by the ErbB gene family (ErbB-1/epidermal growth factor receptor (EGFR), neu/ErbB-2/HER2, ErbB-3/HER3 and ErbB-4/HER4). Betacellulin is a 32-kilodalton glycoprotein that appears to be processed from a larger transmembrane precursor by proteolytic cleavage. This protein is a ligand for the EGF receptor. Betacellulin/BTC is a polymer of about 62-111 amino acid residues. Secondary Structure: 6% helical (1 helices, 3 residues)36% beta sheet (5 strands, 18 residues). Betacellulin/BTC was originally identified as a growth-promoting factor in mouse pancreatic β-cell carcinoma cell line and has since been identified in humans. It plays a role in the growth and development of the neonate and/or mammary gland function. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.
FGF basic is one of 22 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. The 17 kDa mouse sequence has 98% aa identity with rat, and 95% identity with human, bovine, and sheep FGF basic. Binding of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis is reminiscent of a variety of pathological conditions.
Basic fibroblast growth factor (bFGF), also known as FGF2, is a member of the fibroblast growth factor (FGF) family. It is a highly specific chemotactic and mitogenic factor for many cell types, appears to be involved in remodeling damaged tissue, such as ulcer healing, vascular repair, traumatic brain injury (TBI). bFGF is a critical component of human embryonic stem cell culture medium. In addition, bFGF protein is a heparin-binding cationic protein involved in a variety of pathological conditions including angiogenesis and solid tumour growth. Thus, bFGF is regarded as a target for cancers chemopreventive and therapeutic strategies. bFGF/FGF2 Protein & Antibody Products
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