Product Catalog


MMP-2 / CLG4A Protein (Native)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 10082-HNAH |
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YES |
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Matrix Metalloproteinase-2 ( MMP-2 / CLG4A ) Protein
MMP-2 / CLG4A Protein Price Inquiry ( Available Sizes )
- 200μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
MMP-2 / CLG4A Protein Product Information
| Synonym : |
CLG4, CLG4A, MMP-II, MONA, TBE-1, MMP2 |
| Protein Construction: |
A DNA sequence encoding the native human MMP2 ( NP_004521.1 ) ( Met 1 - Cys 660 ) was expressed and purified |
| Source: | Human |
| Expression Host: | Human Cells |
MMP-2 / CLG4A Protein QC Testing
| Purity: | > 95 % as determined by SDS-PAGE | SDS-PAGE:![]() MMP2 protein |
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Bio-activity: |
1. Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2 (R&D Systems, Catalog # ES001). The specific activity is > 1,000 pmoles/min/µg. 2. Measured by its binding ability in a functional ELISA. 3. Immobilized human MMP2 at 10 μg/mL (100 μl/well) can bind human TIMP2/Fc (Cat: 10396-H01H). The EC50 of human TIMP2/Fc is 0.02 μg/mL. |
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| Endotoxin: | < 1.0 EU per μg of the protein as determined by the LAL method. | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: | Ala 30 | |
| Molecular Mass: |
The recombinant human MMP2 consisting of 631 amino acids and migrates as an 72 kDa band as predicted in SDS-PAGE under reducing conditions. |
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| Formulation: | Lyophilized from sterile PBS , pH 7.4
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MMP-2 / CLG4A Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
MMP-2 / CLG4A Protein Related Products & Topics
Related Areas:
Enzyme>>Protease & Regulator>>Metalloprotease & Regulator>>Matrix Metalloproteinase>>MMP-2/MMP2
Cancer>>Angiogenesis>>Matrix Metalloproteinase>>MMP-2/MMP2
Cancer>>Cancer Biomarkers>>MMP-2/MMP2
Proteins:
Antibodies:
| Human MMP-2/MMP2 |
WB, ELISA | MMP-2/MMP2 Antibody, Rabbit PAb | 10082-RP01 |
| Human MMP-2/MMP2 |
WB, ELISA | MMP-2/MMP2 Antibody, Rabbit PAb (Antigen Affinity Purified) | 10082-RP02 |
MMP-2 / CLG4A Protein Description
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. 72 kDa type IV collagenase, also known as Matrix metalloproteinase-2, Gelatinase A, MMP-2, and CLG4A, is a secreted protein which belongs to thepeptidase M10A family. MMP-2/MMP2 contains threefibronectin type-II domains and four hemopexin-like domains. MMP-2/MMP2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2/MMP2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2/MMP2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways. MMP-2/MMP2 contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Defects in MMP-2/MMP2 are the cause of Torg-Winchester syndrome (TWS), also known as multicentric osteolysis nodulosis and arthropathy (MONA). TWS is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia.
References
- Brooks P.C. et al., 1998, Cell 92:391-400.
- Fernandez-Patron C. et al., 1999, Circ. Res. 85:906-11.
- Fernandez-Patron C. et al., 2000, Circ. Res. 87:670-6.
- Bello L., et al., 2001, Cancer Res. 61:8730-6.
- Kandasamy A.D. et al., 2009, Cardiovasc. Res. 83:698-706.
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