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MMP2/MMP-2/CLG4A  Protein, Antibody, ELISA Kit, cDNA Clone

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Expression host: Human Cells  
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Expression host: Human Cells  
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20 µg 
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MMP2/MMP-2/CLG4A Related Area

MMP2/MMP-2/CLG4A Related Pathways

    MMP2/MMP-2/CLG4A Related Protein, Antibody, cDNA Gene, and ELISA Kits

    MMP2/MMP-2/CLG4A Related Protein, Antibody, cDNA Gene, and ELISA Kits

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    MMP2/MMP-2/CLG4A Summary & Protein Information

    MMP2/MMP-2/CLG4A Background

    Gene Summary: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP2 encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in MMP2 have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for MMP2.
    General information above from NCBI
    Catalytic activity: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
    Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; ; Note=Binds 4 Ca(2+) ions per subunit.;; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; ; Note=Binds 2 Zn(2+) ions per subunit.;
    Enzyme regulation: ENZYME REGULATION: Inhibited by histatin-3 1/24 (histatin-5). {ECO:0000269|PubMed:11179305}.
    Subunit 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. {ECO:0000269|PubMed:11320090, ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:11751392, ECO:0000269|PubMed:11928808, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:12147339, ECO:0000269|PubMed:1655733, ECO:0000269|PubMed:19493954}.
    Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
    Subcellular 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.
    Tissue specificity: Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. {ECO:0000269|PubMed:11751392}.
    Induction: Aspirin appears to inhibit expression. {ECO:0000269|PubMed:18971601}.
    Post-translational: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro. {ECO:0000269|PubMed:17435175}.; 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. {ECO:0000269|PubMed:12879005, ECO:0000269|PubMed:9119036}.
    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. {ECO:0000269|PubMed:11431697, ECO:0000269|PubMed:15691365, ECO:0000269|PubMed:16542393}. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the peptidase M10A family. {ECO:0000305}.; Contains 3 fibronectin type-II domains. {ECO:0000255|PROSITE-ProRule:PRU00479}.; Contains 4 hemopexin repeats. {ECO:0000305}.
    General information above from UniProt

    Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN), Her2/neu, growth factors, cytokines, and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to favorable prognosis in patients with a hormone receptor-negative tumor, usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity, MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems, including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment.

    MMP2/MMP-2/CLG4A Alternative Name

    MMP2/MMP-2/CLG4A Related Studies

  • Thompson EW, et al. (1994) Collagen induced MMP-2 activation in human breast cancer. Breast Cancer Res Treat. 31(2-3): 357-70.
  • Jezierska A, et al. (2009) Matrix metalloproteinase-2 involvement in breast cancer progression: a mini-review. Med Sci Monit. 15(2): RA32-40.
  • Fredrich M, et al. (2010) MMP-2 is involved in synaptic remodeling after cochlear lesion. Neuroreport. 21(5): 324-7.