Immunohistochemistry (IHC) : Human sarcoma stained with anti-MMP-2 antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of some tumor cells..

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

SKU: 6259parent Category: antibody Tags: anatomy, General & Epithelial Markers, MMP-2

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

antibody
Database link: human P08253
Tested applications IHC
Recommended dilutions Concentrated 1:50
Applicaiton Notes Positive control: Placenta, bladder, breast, and ovarian carcinoma
Immunogen A synthetic peptide derived from near N-terminal of human MMP-2 protein
Size and concentration 7 mL prediluted or 0.1, 0.5, 1.0 mL and concentrated
Form liquid
Storage Instructions 2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Purity affinity purified
Clonality monoclonal
Isotype IgG1
Compatible secondaries goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486 goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854 goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706 goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721
Isotype control Mouse monoclonal IgG1 - Isotype Control

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.