Cleaved-MMP-15 (Y132) polyclonal antibody

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 downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Matrix metalloproteinase-15; MMP-15; Membrane-type matrix metalloproteinase 2; MT-MMP 2; MTMMP2; Membrane-type-2 matrix metalloproteinase; MT2-MMP; MT2MMP; SMCP-2; MMP15

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of Cleaved-MMP-15 (Y132) pAb at 1:500 dilution Lane1:MCF-7 whole cell lysate (40ug) Lane2:SGC7901 whole cell lysate (40ug) Lane3:HCT116 whole cell lysate (40ug) Lane4:HEK293T whole cell lysate (40ug)