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Matrix Metalloproteinase-3 from Human, Recombinant


Cat No.
NATE-0861
Description
Matrix metalloproteinase-3 (MMP-3) also known as stromelysin-1 and transin (EC 3.4.24.17) cleaves a number of substrates including cartilage proteoglycan, collagen types II, III, IV, V and IX, fibronectin, laminin, and can activate MMP 1. MMP-3 is secreted as 57 and 59 kDa proenzymes and can be activated in vitro by organomercurials (e.g., 4 aminophenylmercuric acetate, APMA) and in vivo by proteases via intermediate forms to a 45 kDa active MMP 3 enzyme. Further autolysis to a 28 kDa form can also occur. MMP-3 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis and cancer cell invasion.
Abbr
MMP-3, Recombinant (Human)
Alias
MMP-3
Species
Human
Applications
Immunoblotting; Substrate Cleavage Assay; Zymography
Product Overview
Recombinant, human pro-MMP-3 purified from cell culture supernatant. May be used as a positive control or standard for zymographic analysis, or substrate assay. Requires activation for immunoblotting, prior to use. M.W. 57000/58000.
Form
Lyophilized from 100 mM NaCl, 50 mM HEPES, pH 7.3.
Enzyme Commission Number
EC 3.4.24.17
CAS No.
79955-99-0
Molecular Weight
57 kDa
Purity
>95% by SDS-PAGE
Storage
< -70°C; Avoid freeze/thaw
Synonyms
Stromelysin 1; EC 3.4.24.17; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein
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