Human MMP-2 Protein (pro form) 3489

Additional Information:
accession P08253|express systemHEK293|product tagN-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundMatrix metalloproteinase (MMP)-2 cleaves a broad spectrum of substrates, including extracellular matrix components (responsible for normal tissue remodeling) and cytokines (modulators of the inflammatory response to physiological insults such as tissue damage). MMP-2 expression is elevated in many cardiovascular pathologies (e.g., myocardial infarction, hypertensive heart disease) where tissue remodeling and inflammatory responses are perturbed.|molecular weightThe protein has a predicted MW of 71.6 kDa. Due to glycosylation, the protein migrates to 72-75 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per ug by the LAL method.|Human MMP-2 Protein (pro form) 3489proteinSize and concentration100, 500g and liquidFormLiquidStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped with dry ice.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceMatrix metalloproteinase (MMP)-2 cleaves a broad spectrum of substrates, including extracellular matrix components (responsible for normal tissue remodeling) and cytokines (modulators of the inflammatory response to physiological insults such as tissue damage). MMP-2 expression is elevated in many cardiovascular pathologies (e.g., myocardial infarction, hypertensive heart disease) where tissue remodeling and inflammatory responses are perturbed.Protein names72 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 namesMMP2,MMP2 CLG4AProtein familyPeptidase M10A familyMass9606DaFunctionUbiquitinous 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 activityBINDING 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.TissuesProduced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.StructureInteracts (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 modificationPhosphorylation 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.DomainThTarget Relevance information above includes information from UniProt accession: P08253The UniProt Consortium|