Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG1 |
clonality | monoclonal |
concentration | concentrate, predilute |
applications | IHC |
reactivity | human |
available size | 0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted |
mouse anti-MMP-2 monoclonal antibody (CA-4001) 6259
$160.00 – $528.00
Antibody summary
- Mouse monoclonal to MMP-2
- Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
- Reacts with: Human
- Isotype:IgG1
- Control: Placenta, bladder, breast, and ovarian carcinoma
- Visualization: Cytoplasmic
- 0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted
mouse anti-MMP-2 monoclonal antibody CA-4001 6259
target relevance |
---|
Protein names 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) (TBE-1) [Cleaved into: PEX] |
Gene names MMP2,MMP2 CLG4A |
Protein family Peptidase M10A family |
Mass 9606Da |
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.; 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.; [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. |
Catalytic activity BINDING 102; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /note="in inhibited form"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD"; BINDING 134; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 168; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU"; BINDING 178; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 180; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 185; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 186; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 193; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 200; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU"; BINDING 202; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 204; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 206; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 208; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 209; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 211; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; BINDING 211; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; BINDING 403; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; BINDING 407; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; BINDING 413; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; BINDING 476; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; BINDING 521; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; BINDING 569; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; BINDING 618; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="4"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG" |
Subellular 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.; [Isoform 2]: Cytoplasm. Mitochondrion. |
Tissues Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. |
Structure Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B. |
Post-translational modification 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. |
Domain Th |
Involvement in disease DISEASE: Multicentric osteolysis, nodulosis, and arthropathy (MONA) [MIM:259600]: An autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. Note=The disease is caused by variants affecting the gene represented in this entry. |
Target Relevance information above includes information from UniProt accession: P08253 |
The UniProt Consortium |
Data
Human sarcoma stained with anti-MMP-2 antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of some tumor cells.. |
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
---|
Protocols
relevant to this product |
---|
IHC |
Documents
# | |||
---|---|---|---|
Please enter your product and batch number here to retrieve - product datasheet, SDS, and QC information. |
Only logged in customers who have purchased this product may leave a review.
Reviews
There are no reviews yet.