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.
Function:
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 integrin alpha-v/beta-3 on the surface of blood vessels.
Subcellular Location:
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.
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Monoclonal Antibody for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
Protein for Bovine 72 kDa type IV collagenase
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
1.
"Molecular cloning and biological characterization of bovine matrix metalloprotease 2 (bMMP-2)." Yan L.
,
Zhang B.
,
Tsang P.
,
Fang J.
,
Yu Y.
,
Ingber D.E.
,
Moses M.A.
Submitted (2000-07) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA]