BMP-13/CDMP-2

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.

GDF6; KFM; KFS; KFS1; KFSL; SGM1; BMP13; CDMP2; MCOP4; SCDO4; MCOPCB6

392255

P43028

NP_038554.1

NM_013526.1

8q22.1

Human

Mouse, Human

TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR

< 0.1 ng/µg of protein (< 1EU/µg)

>95% by SDS-PAGE & HPLC analysis

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.

120

Lyophilized

27.0 kDa

E. coli