|Description||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.|
|BiologicalActivity||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.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human BMP-13/CDMP-2 is for research use only and not for use in diagnostic or therapeutic procedures.|
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