The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 0.5 - 2 µg/ml. Detects a band of approximately 72 kDa (predicted molecular weight: 72 kDa).
Use a concentration of 2 - 4 µg/ml.
Use at an assay dependent concentration.
Use at an assay dependent concentration. PubMed: 20181831
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.
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.
Belongs to the peptidase M10A family. Contains 3 fibronectin type-II domains. Contains 4 hemopexin-like domains.
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.
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.
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.
Detection of MMP2 in a frozen injured rat nerve tissue section stained using ab37150 at 2µg/ml. No antigen retrieval was carried out.
Immunocytochemistry/ Immunofluorescence - Anti-MMP2 antibody (ab37150)This image is courtesy of an anonymous Abreview
ab37150 staining MMP2 in Rat fibroblast cells by Immunocytochemistry/ Immunofluorescence. The cells were paraformaldehyde fixed and then blocked using 1% BSA for 1 hour at 25°C. Samples were then incubated with primary antibody at 1/200 for 16 hours at 4°C. The secondary antibody used was a goat anti-rabbit IgG conjugated to Alexa Fluor® 488 (green) (ab150077) used at a 1/1000 dilution.Cells were stimulated with PDBu.