BMP-13 is expressed in hypertrophic chondrocytes during embryonic development of long bones. Continued postnatal expression of BMP-13 in articular cartilage suggests that it plays a regulatory role in the growth and maintenance of articular cartilage. Adenovirus-mediated BMP-13 gene transfer to rabbit bone marrow stem cells have been reported to augment periosteal repair of osteochondral defects. The functional form of BMP-13/CDMP-2 is a disulfide-linked homodimer of two 120 amino acid polypeptide chains. This 27.5 kDa protein is obtained by proteolytic processing of a biologically inactive precursor protein of 97.7 kDa. Recombinant Human BMP-13/CDMP-2 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.
Bone Morphogenetic Protein-13, GDF-6, Cartilage-Derived Morphogenetic Protein-2 (CDMP-2)
AA Sequence (monomer):
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR
Greater than 95% by SDS-PAGE gel and HPLC analyses.
The ED50 was determined by its ability to induce alkaline phosphatase production by ATDC-5 chondrogenic cells in the range of 2.0-3.0 µg/ml.