MMP-16 (T583) 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-13 (also designated collagenase-3) is produced by breast carcinomas and degrades collagen types I, II and III. MMP-13 has wide substrate specificity, and its physiologic expression is limited to situations in which rapid and effective remodeling of collagenous ECM takes place, such as fetal bone development and adult bone remodeling.

Matrix metalloproteinase-16; MMP-16; MMP-X2; Membrane-type matrix metalloproteinase 3; MT-MMP 3; MTMMP3; Membrane-type-3 matrix metalloproteinase; MT3-MMP; MT3MMP; MMP16; MMPX2

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 MMP-16 (T583) polyclonal antibody at 1:500 dilution Lane1:SK-OVCAR3 whole cell lysate (40ug) Lane2:HT102 whole cell lysate (40ug) Lane3:H9C2 whole cell lysate (40ug) Lane4:CT26 whole cell lysate (40ug)