- Regulatory Status
- Other Names
- Matrix metallopeptidase 2, Gelatinase A, MMP-2, GelA, Clg4a, CLG4, MONA, TBE-1, MMP-II, MMP2
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- Product Citations
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MMP-2, also known as gelatinase A, is a member the of matrix metalloproteinase family of proteins (MMPs). MMPs are structurally-related calcium-dependent, zinc-containing enzymes that degrade extracellular matrix and connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling. MMPs are also active in disease processes such as arthritis and metastasis.
MMP-2 consists of a pro-domain (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 domain. The activated form of MMP-2 is produced by a 2-step proteolytic processing. First, a complex comprised of membrane type 1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase 2 (TIMP-2) recruits pro-MMP-2 from the extracellular milieu to the cell surface. The second step requires an active molecule of MT1-MMP, which itself activates MMP-2, leading to subsequent autocatalytic cleavage. Substrates of activated MMP-2 include several components of the articular cartilaginous matrix including: type IV collagen, aggrecan, link protein, decorin, fibronectin, and type X and XI collagens.
Elevated MMP-2 secretion is associated with poor prognosis in several types of human cancers. Mutations in the gene encoding 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 glands.Product Details
- Human MMP-2, amino acids (Ala30-Cys660) (Accession# NP_004521.1) with a C-terminal His tag and a linker sequence, was expressed in 293E cells.
- Molecular Mass
- This 652 amino acid recombinant protein has a predicted molecular mass of approximately 73.2 kD. The protein migrates at about 73 kD in DTT-reducing conditions and about 73 kD in non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Ala.
- > 95%, as determined by Coomassie stained SDS-PAGE.
- Lyophilized in sterile-filtered PBS, pH 7.2, containing 1% BSA, 0.09% sodium azide, and protease inhibitors.
- Lot-specific (please contact technical support for mass/vial, or use our Lookup tool if you have a lot number.)
- Storage & Handling
- Upon receiving, store unopened vials between 2°C and 8°C immediately and use within 12 months from date of receipt. Prior to use, reconstitute the lyophilized powder with 0.2 ml of PBS containing a carrier protein (e.g., 1% BSA, protease free), pH 7.4. Re-cap vial, vortex. Allow the reconstituted standard to sit at room temperature for 15 minutes, vortex again to mix completely. The reconstituted standard stock solution can be aliquoted into polypropylene vials and stored at -70°C for up to one month. Do not re-use diluted standards. Use a manual defrost freezer and avoid repeated freeze thaw cycles.
ELISA - Quality tested
- Recommended Usage
Each lot of this protein is quality control tested by ELISA assay. For use as an ELISA standard, a standard curve comprised of doubling dilutions from 0.156 ng/ml to 10 ng/ml is suggested. It is recommended that the reagent be titrated for optimal performance for each application.
- Application Notes
This MMP-2 protein is useful as a standard for a human MMP-2 sandwich ELISA, using unlabeled M6303D01 antibody (Cat. No. 679902) for capture and biotinylated M6310C11 antibody (Cat. No. 532001) for detection.
(PubMed link indicates BioLegend citation)
- Nagase H, Woessner JF. 1999. J. Biol. Chem. 274:21491-4.
- Martignetti JA, et al. 2001. Nat. Genet. 28:261-5.
- Itoh T, et al. 1997. J. Biol. Chem. 272:22389-92.
- Passlick B, et al. 2000. Clin. Cancer Res. 6:3944-8.
- Qian Q, et al. 2010. Cancer Invest. 28:661-9.
- Hoikkala S, et al. 2006. Cancer Lett. 236:125-32.
- Yamamura T, et al. 2002. Lung Cancer 35:249-55.
MMP-2 is expressed by fibroblasts, endothelial cells, alveolar epithelial cells, and macrophages.
- Degradation of ECM and connective tissue proteins, angiogenesis, tissue remodeling, cancer metastasis and MMP-2 secretion is elevated in several types of cancers.
- TIMPs, CCL7, thrombospondin 1
- Biology Area
- Angiogenesis, Cell Adhesion, Cell Biology, Neuroinflammation, Neuroscience
- Molecular Family
- Enzymes and Regulators
- Gene ID
- 4313 View all products for this Gene ID
- View information about MMP-2 on UniProt.org