The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
N-TERMINAL---Human BMP-2 (Met 1 – Arg 282) Human BMP-7 (Ser 293 – Arg 431)---C-TERMINAL. The DNA sequence encoding the human BMP-2 signal peptide and propeptide (1~282 amino acid) fused to the human rhBMP-7 mature chain (293~431 amino acid) was expressed in a Chinese hamster ovary cell line. The mature recombinant BMP-7 generated by the proteolytic removal of the signal peptide and propetide contains 139 amino acid residues. The glycosylation of BMP-7 increases the molecular mass and the glycosylated proteins migrate as 25 ~ 40 kDa in SDS-PAGE under non-reducing conditions.
BMP-7 is purified by proprietary chromatographic techniques.
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