Recombinant Human MMP-2 (ELISA Std.)

Pricing & Availability
Other Names
Matrix metallopeptidase 2, Gelatinase A, MMP-2, GelA, Clg4a, CLG4, MONA, TBE-1, MMP-II, MMP2
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Human_MMP-2_RECOM_040918
  • Human_MMP-2_RECOM_040918
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763301 4 pack 80 CHF
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Description

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
Technical Data Sheet (pdf)

Product Details

Source
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.
Purity
> 95%, as determined by Coomassie stained SDS-PAGE.
Formulation
Lyophilized in sterile-filtered PBS, pH 7.2, containing 1% BSA, 0.09% sodium azide, and protease inhibitors.
Concentration
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.
Application

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.

Application References

(PubMed link indicates BioLegend citation)
  1. Nagase H, Woessner JF. 1999. J. Biol. Chem. 274:21491-4.
  2. Martignetti JA, et al. 2001. Nat. Genet. 28:261-5.
  3. Itoh T, et al. 1997. J. Biol. Chem. 272:22389-92.
  4. Passlick B, et al. 2000. Clin. Cancer Res. 6:3944-8.
  5. Qian Q, et al. 2010. Cancer Invest. 28:661-9.
  6. Hoikkala S, et al. 2006. Cancer Lett. 236:125-32.
  7. Yamamura T, et al. 2002. Lung Cancer 35:249-55.

Antigen Details

Structure
Monomer
Distribution

MMP-2 is expressed by fibroblasts, endothelial cells, alveolar epithelial cells, and macrophages.

Function
Degradation of ECM and connective tissue proteins, angiogenesis, tissue remodeling, cancer metastasis and MMP-2 secretion is elevated in several types of cancers.
Ligand/Receptor
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
UniProt
View information about MMP-2 on UniProt.org

Related FAQs

There are no FAQs for this product.
Go To Top Version: 1    Revision Date: 04.10.2018

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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