Pro-MMP-2 Protein | MMP2 protein

Pro-MMP-2, mouse

Cat. Num. AAA844081

• Gene Names: Mmp2; GelA; Clg4a; MMP-2
• Applications: SDS-Page
• Purity: >=90%
• Synonyms: Pro-MMP-2; mouse; 72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2) [Cleaved into: PEX]; Matrix metalloproteinase-2; MMP; MMP recombinant; MMP protein; MMP inhibitor; MMP2 protein

• Host: mouse fibroblasts
• Purity/Purification: >=90%
• Form/Format: In 50 mM Tris-HCl, pH 7; 200 mM NaCl; 5 mM CaCl?; 1 muM ZnCl?; 0.05% Brij 35; 0,05% NaN?; Appearance: Liquid
• Concentration: 50 mug/ ml; >40 mU/mg (Masui substrate), >40 mU/mg (Knight substrate) - APMA activation, 1 hour/37 degree C (varies by lot)
• Sequence Length: 662

• Applicable Applications for MMP2 protein: SDS-PAGE; HPLC
• Handling: Centrifuge the vial prior to opening.
• Preparation and Storage: At -80 degree C; Shelf Life: 12 months

Testing Data

Related Product Information for MMP2 protein

Background: The progelatinase A, a member of the matrix metalloproteinase (MMP) family, has been isolated from macrophages and fibroblasts. Gelatinase A hydrolyses several components of the extracellular matrix, e.g. the collagen types IV, V and XI and gelatin. Progelatinase A complexed via their C-terminal domain with TIMP-2 was isolated from culture media of different cell types. This complex shows both properties of its constituents: Like TIMP-2 it inhibits active matrix metalloproteinases and like gelatinase it shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate). However, its proteolytic activity is less than 10% of that of gelatinase A not complexed with TIMP-2. In contrast to the other MMPs the progelatinase A cannot be activated by the serine proteinase trypsin. Until quite recently a potential natural activator that can transform latent progelatinase A into the active form was unknown. It was shown that the catalytic domain of the membrane type 2-matrix metalloproteinase activates progelatinase A as well as the progelatinase A / TIMP-2 complex, by cleaving the 72 kDa progelatinase A to yield 67 kDa gelatinase A, which is than transformed into 62 kDa gelatinase A. The 62 kDa form is about twice as active as the 67 kDa form towards the Dnp-pepitde (Masui et al.). No significant difference in activity was found between free and complexed gelatinase A forms.

Product Categories/Family for MMP2 protein

Proteins and Enzymes; Proteases; MMPsProteins and Enzymes; Animal-Free Origin (AOF) Recombinant Proteins & Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 6678902
• NCBI GeneID: 17390
• NCBI Accession #: NP_032636.1
• NCBI GenBank Nucleotide #: NM_008610.2
• UniProt Accession #: Q3UG07; P33434
• Molecular Weight: 40/42 kDa
• NCBI Official Full Name: 72 kDa type IV collagenase
• NCBI Official Synonym Full Names: matrix metallopeptidase 2
• NCBI Official Symbol: Mmp2
• NCBI Official Synonym Symbols: GelA; Clg4a; MMP-2
• NCBI Protein Information: 72 kDa type IV collagenase
• UniProt Protein Name: Matrix metallopeptidase 2
• Protein Family: Matrix metalloproteinase
• UniProt Gene Name: Mmp2
• UniProt Entry Name: Q3UG07_MOUSE

Uniprot Description

MMP2: 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. 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. Aspirin appears to inhibit expression. Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. Inhibited by histatin-3 1/24 (histatin-5). Belongs to the peptidase M10A family.

Protein type: Apoptosis; Motility/polarity/chemotaxis; Protease; Secreted; EC 3.4.24.24; Secreted, signal peptide; Cell development/differentiation

Cellular Component: extracellular matrix; proteinaceous extracellular matrix; extracellular space; sarcomere; mitochondrion; membrane; cytoplasm; extracellular region; plasma membrane; nucleus

Molecular Function: peptidase activity; hydrolase activity; zinc ion binding; metallopeptidase activity; metalloendopeptidase activity; metal ion binding; fibronectin binding

Biological Process: response to drug; cell migration; intramembranous ossification; positive regulation of apoptosis; tissue remodeling; negative regulation of cell adhesion; proteolysis; axon regeneration in the peripheral nervous system; blood vessel maturation; negative regulation of vasoconstriction; collagen catabolic process; response to hydrogen peroxide; ovarian follicle development; response to estrogen stimulus; skeletal morphogenesis; response to mechanical stimulus; positive regulation of innate immune response; response to hypoxia; angiogenesis; response to oxidative stress; embryo implantation; positive regulation of cell migration