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Each lot of this antibody is quality control tested by Western blotting. For Western blotting, suggested working dilution(s): Use 4 µg/ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Application References:
1. Murray G et al. 1998. Gut. 43:791.
Western blot analysis of recombinant human MMP-3 protein using anti-MMP-3, clone F36P1B4.
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that degrade substances withinthe extracellular matrix. The MMP family includes six different groups of enzymes: collagenases, gelatinases, stromelysins, transmembrane MMPs, matrilysins and others. MMPs are secreted as proenzymes that have to be cleaved in order to be activated. Other MMPs, plasmins as well as other factors activate MMPs. MMPs are thought to play an important role in tissue remodeling associated with various physiological and pathological processes. MMP1 cleaves collagens of types I, II, III, VII and X.MMP1 is thought to play an important role in rheumatoid and osteo-arthritis pathogenesis as mediators of cartilage and bone destruction. Clone F15P3B6 has been shown to be useful for western blotting and immunohistochemistry of human MMP1.
Other Names:
Progelatinase, STR1, Transin, Stromelysin I, MMP-3 < Transin-1, STMY1>
Structure:
Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains, predicted molecular weight approximately 54 kD.
Distribution:
Extracellular
Function:
MMP3 degrades fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. MMP-3 is thought to play a prominent role in the pathogenesis of rheumatoid arthritis.
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Purified anti-MMP3
Western blot analysis of recombinant human MMP-3 protein using anti-MMP-3, clone F36P1B4.
