Recombinant human MMP9 protein fragment (around aa 22-166) (exact sequence is proprietary)
Alternative Synonym:
82kDa matrix metalloproteinase-9, 92kDa gelatinase, 92kDa type IV collagenase, CLG 4B, CLG4B, Collagenase Type 4 beta, Collagenase type IV 92KD, Gelatinase 92KD, Gelatinase B, Gelatinase beta, GelatinaseB, GELB, Macrophage gelatinase, MANDP2, Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase), Matrix Metalloproteinase 9, MMP9, Type V collagenase
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
