Human BMP‑6 Biotinylated Antibody

Human BMP-6 is one of at least 15 structurally and functionally related BMPs, which are members of the transforming growth factor beta (TGF-beta ) superfamily. BMPs were originally identified as protein regulators of cartilage and bone formation. However, they have since been shown to be involved in embryogenesis and morphogenesis of various tissues and organs. BMPs have also been shown to regulate the growth, differentiation, chemotaxis and apoptosis of various cell types, including mesenchymal cells, epithelial cells, hematopoietic cells and neuronal cells. Similarly to other TGF-beta family proteins, BMPs are highly conserved across animal species. At the amino acid sequence level, mature human and mouse BMP-6 shares 96% amino acid sequence identity. BMP-6 is synthesized as a large precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxy-terminal domain. Biologically active BMP-6 is a disulfide-linked homodimer of the carboxy-terminal 132 amino acid residues that contains the characteristic seven conserved cysteine residues involved in the formation of the cysteine knot and the single interchain disulfide bond. Cellular responses to BMP-6 have been shown to be mediated by the formation of hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Based on amino acid sequence similarity, BMP-5, -6, -7 and -8 are in the same subgroup.