Formalin-fixed, paraffin-embedded human spleen stained with MMP9 Mouse Recombinant Monoclonal Antibody (SPM425).
Known Applications & Suggested Dilutions
Host / Ig Isotype
Mol. Weight of Antigen
Specificity & Comments
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.