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. Membrane-type matrix metalloproteinases, including MT-MMP-1 (also designated MMP-14), MT-MMP-2 (also designated MMP-15), MT-MMP-3 (also designated MMP-16) and MT-MMP-4 (also designated MMP-17) are type I membrane proteins that function to activate other MMPs. MT-MMP activation appears to be mediated by members of the proprotein convertase family, suggesting that a proprotein convertase/MT-MMP/MMP cascade may be involved in the regulation of ECM turnover.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200
Application Notes:
MMP-14 (P509) polyclonal antibody detects endogenous levels of MMP-14 protein.
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