MMP2 Protein (AA 30-660, C-Term)
Quick Overview for MMP2 Protein (AA 30-660, C-Term) (ABIN2666503)
Target
See all MMP2 ProteinsProtein Type
Biological Activity
Origin
Source
Application
Purity
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Protein Characteristics
- AA 30-660, C-Term
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Sterility
- 0.22 μm filtered
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Endotoxin Level
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Less than 1.0 EU per μg of protein as determine by the LAL method
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Application Notes
- Optimal working dilution should be determined by the investigator.
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Comment
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Biological activity: Human MMP-2 cleaves the modified fluorogenic peptide Mca-PLGL-Dpa-AR-NH2 with an activity above 1100 pmol/min/μg.
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Restrictions
- For Research Use only
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Format
- Liquid
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Reconstitution
- For maximum results, quick spin vial prior to opening.
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Buffer
- 0.22 μm filtered protein solution is in TCN (25 mM TRIS, 5 mM CaCl2, 150 mM NaCl, pH 7.5).
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Handling Advice
- Avoid repeated freeze/thaw cycles.
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Storage
- -20 °C
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Storage Comment
- Unopened vial can be stored at -70°C for six months.
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- MMP2 (Matrix Metalloproteinase 2 (MMP2))
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Alternative Name
- MMP-2
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Background
- MMP-2, also named gelatinase A, is a member of matrix metalloproteinase family proteins (MMPs). MMPs are structurally related, zinc-containing enzymes that degrade the extracellular matrix and connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling as well as in disease processes such as arthritis and metastasis. MMP-2 consists of a prodomain, which is cleaved upon activation, a catalytic domain containing the zinc binding site, a fibronectin-like domain (that plays a role in the substrate targeting), and a carboxyl-terminal (hemopexin-like repeats) domain. Activation of MMP-2 requires proteolytic processing: first, a complex of membrane type 1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase 2 recruits pro-MMP-2 from the extracellular milieu to the cell surface, second, MMP-2 is activated by active MT1-MMP and subsequent autocatalytic cleavage. Substrates of MMP-2 include type IV collagen, aggrecan, link protein, decorin, fibronectin, and type X and XI collagens, all of which are components of the articular cartilaginous matrix. Importantly, MMP-2 secretion is elevated in several types of human cancers and its elevated expression has been associated with a poor prognosis. Mutations in the MMP-2 gene are associated with Torg-Winchester syndrome, multicentric osteolysis, arthritis syndrome, and possibly keloids. MMP-2 deficient mice exhibit slightly delayed growth, reduced neovascularization, retarded tumor progression, an exaggerated asthma response to allergens, and impaired branching morphogenesis of the mammary gland.
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Molecular Weight
- This 652 amino acid recombinant protein has a predicted molecular mass of approximately 73.2 kDa. The protein migrates at about 73 kDa in DTT-reducing conditions and about 73 kDa in non-reducing conditions by SDS-PAGE.The predicted N-terminal amino acid i
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Pathways
- Activation of Innate immune Response
Target
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