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 taphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-3, MMP-10 and MMP-11 (also designated stromelysin- 1, -2 and -3) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and it is expressed at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
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 IF: 1:50~1:200
Application Notes:
MMP-11 (G88) polyclonal antibody detects endogenous levels of MMP-11 protein.
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