Cellular responses to BMP-6 are mediated by the formation of hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Mature human and murine BMP-6 demonstrates 96% homology.
BMP6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (375-513) and having a molecular mass of 18kDa.
BMP6 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules, which can induce ectopic bone growth. Various BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were initially identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based upon its expression early in embryogenesis, BMP6 has a suggested role in early development. Moreover, the fact that the BMP6 is closely related to BMP5 and BMP7 leads to an assumption of possible bone inductive activity.
