Human BMP-2 Recombinant (AF)

Bone Morphogenetic Proteins (BMPs) are part of the TGF-? superfamily, a group of structurally related signaling proteins. Among them, BMP-2 stands out as a potent osteoinductive cytokine, capable of prompting bone and cartilage formation when coupled with osteoconductive carriers like collagen and synthetic hydroxyapatite. Besides its role in osteogenesis, BMP-2 contributes significantly to cardiac morphogenesis and is expressed in various tissues such as the lung, spleen, brain, liver, prostate, ovary, and small intestine. The active form of BMP-2 is a 26 kDa protein made up of two identical 114 amino acid polypeptide chains connected by a single disulfide bond. Each BMP-2 monomer is part of a precursor polypeptide, featuring a 23 amino acid signal sequence for secretion and a 259 amino acid propeptide. Upon precursor dimerization, a furin-type protease cleaves the covalent bonds between the propeptide (also a disulfide-linked homodimer) and the mature BMP-2 ligand. Recombinant Human/Murine/Rat BMP-2 is a 26.0 kDa homodimeric protein composed of two 115 amino acid polypeptide chains.