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MilliporeSigma™ anti-MMP-2 (Ab-7), Polyclonal
Rabbit Polyclonal Antibody
Supplier: MilliporeSigma™ PC342100UG
Description
Specifically detects MMP-2 (Ab-7) Clone: in Human, Mouse samples, and it is validated for Immunoprecipitation
Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an∽10kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis. MMP-2 (Gelatinase A, 72kDa gelatinase, type IV collagenase, TBE-1) is synthesized as a 631 amino acid proenzyme (72kDa zymogen) which is proteolytically processed at the first 80 amino acids to the 66kDa active form. MMP-2, along with its most closely related member of the MMP family, MMP-9, show substrate specificity toward type IV and V collagens, gelatin and elastin. Numerous studies have shown a correlation between collagenase expression and metastatic potential and suggest that MMP-2 may be a useful marker for the diagnosis or prognosis of cancer.Specifications
MMP-2 (Ab-7) | |
Polyclonal | |
In 1X PBS, 0.2% BSA. | |
recombinant, human pro-MMP-2 | |
RUO | |
Recognizes the ∽72kDa latent form of the MMP-2 protein. Cross-reacts with recombinant MMP-9 at high concentrations but does not cross-react with native MMP-9. | |
2°C to 8°C | |
IgG |
Immunoprecipitation | |
Unconjugated | |
Rabbit | |
100 μg | |
Primary | |
Human, Mouse | |
Purified |
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