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Products:Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
Overview
Product name
MMP2 protein (Human)
See all MMP2 products (11) ...
Protein description
Full length Human MMP2 protein (purified from human fibroblast cell culture media).
Properties
Purification notes
Purified from human fibroblasts, free of its endogenous inhibitor, TIMP-2, and other matrix metalloproteinases. The enzyme is supplied as a mixture of the zymogen and processed enzyme.
Biological activity
Degrades denatured Collagen (gelatin), and a range of extracellular matrix components in-vivo.
Form
Liquid
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage buffer
Preservative: None
Constituents: 50% Glycerol, PBS, 250mM Sodium chloride, pH 7.4
Concentration
Concentration information loading...
Research areas
Cancer >> Cancer Metabolism >> Response to hypoxia
Cancer >> Tumor biomarkers >> Enzymes >> MMPs
Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> MMPs
Cancer >> Invasion/microenvironment >> ECM >> Extracellular matrix >> MMPs
Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
Applications
Show applications key
Our Abpromise guarantee covers the use of ab39302 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: Use at an assay dependent dilution. Predicted molecular weight: 74 kDa.
SDS-PAGE: Use at an assay dependent dilution.
Protein info
Function
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-
-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro.
PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.
Tissue specificity
Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.
Involvement in disease
Defects in MMP2 are the cause of Torg-Winchester syndrome (TWS) [MIM:259600]; also known as multicentric osteolysis nodulosis and arthropathy (MONA). TWS is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Torg-Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes.
Sequence similarities
Belongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin-like domains.
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Post-translational
modifications
Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.
The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.
Cellular localization
Secreted > extracellular space > extracellular matrix. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.
Target information above from: UniProt accessionP08253
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
References for MMP2 protein (Human) (ab39302)
ab39302 has not yet been referenced specifically in any publications.
Publishing research using ab39302? Please let us know so that we can cite the reference in this datasheet
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"