HUMAN BMP-2

BMP-2 human has been used to study the biological role of BMP-2 on adult renal progenitor cells under in vitro and in vivo conditions.

The functional form of BMP-2 (bone morphogenetic protein 2) is a 26kDa protein composed of two identical 114 amino-acid polypeptide chains (monomers) linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino-acid signal sequence for secretion, and a 259 amino-acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant human BMP-2 is a 26kDa homodimeric disulfide-linked protein consisting of two identical 115 amino acid chains.

BMP-2 (bone morphogenetic protein 2) is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with an osteoconductive carrier such as collagen and synthetic hydroxyapatite. During bone repair, it controls the expression of Runt-related transcription factor 2 (Runx2) and Osterix (Osx), thereby enhancing migration, proliferation and osteogenic differentiation of mesenchymal stem cells. In addition to its osteogenic activity, BMP-2 appears to play an important role in cardiac morphogenesis, and is expressed in a variety of other tissues including lung, liver, spleen, prostate, ovary, and small intestine.