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MilliporeSigma™ anti-MMP-2 Clone: 42-5D11,
Mouse Monoclonal Antibody
Supplier: MilliporeSigma™ IM33100UG
Description
Specifically detects MMP-2 Clone: 42-5D11 in Bovine, Human, Mouse, Rat samples, and it is validated for Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immuno Blotting
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 approximately 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 secreted as a 72kDa zymogen which is proteolytically processed 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 it may be a useful marker for the diagnosis or prognosis of cancer.
Specifications
MMP-2 | |
Monoclonal | |
Unconjugated | |
Mouse | |
100 μg | |
Primary | |
Bovine, Human, Mouse, Rat | |
Purified |
Immunoblot, Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin) | |
42-5D11 | |
In 100mM sodium phosphate buffer, 0.1% BSA, pH 7.0 | |
a synthetic peptide (VTPRDKPMGPLLVATF) corresponding to amino acids 468-483 of human MMP-2 | |
RUO | |
Recognizes the ∽72kDa latent and the ∽66kDa active forms of the MMP-2. | |
−20°C | |
IgG1 |
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