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Anti-MMP2 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P08253 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for 72 kDa type IV collagenase(MMP2) detection. Tested with WB, ELISA in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 4313 |
|---|---|
| Other Names | 72 kDa type IV collagenase, 3.4.24.24, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, PEX, MMP2, CLG4A |
| Calculated MW | 73882 MW KDa |
| Application Details | ELISA , 0.1-0.5 µg/ml, Human, - Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat |
| Subcellular Localization | Isoform 1: 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. |
| Tissue Specificity | Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. . |
| Protein Name | 72 kDa type IV collagenase |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | E. coli-derived human MMP2 recombinant protein (Position: K429-C660). Human MMP2 shares 95.7% and 95.3% amino acid (aa) sequence identity with mouse and rat MMP2, respectively. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Name | MMP2 |
|---|---|
| Synonyms | CLG4A |
| 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. Involved in the formation of the fibrovascular tissues in association with MMP14. [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial- nuclear stress signaling with activation of the pro-inflammatory NF- kappaB, NFAT and IRF transcriptional pathways. |
| Cellular Location | [Isoform 1]: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus Note=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 |
| Tissue Location | Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Matrix metalloproteinase-2 (MMP2) is a Type IV collagenase, 72-kD, which is also known as gelatinase and is a member of a group of secreted zinc metalloproteases. The MMP2 gene is 17 kb long with 13 exons varying in size from 110 to 901 bp and 12 introns ranging from 175 to 4,350 bp, located within a region of human chromosome 16q13. In addition, the extra exons encode the amino acids of the fibronectin-like domain which has so far been found in only the 72- and 92-kDa type IV collagenase. MMP2, which has a critical role in the binding of progelatinase A and TIMP4 via the C-terminal hemopexin-like domain (C domain), is functionally associated on the surface of angiogenic blood vessels. Not only is a likely effector of endometrial menstrual breakdown, MMP2 is also effector and regulator of the inflammatory response. Moreover, MMP2 could be helpful in diagnosing Takayasu arteritis.
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