ABD38929.1
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
73,882 Da
NCBI Official Full Name
MMP2
NCBI Official Synonym Full Names
matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
NCBI Official Synonym Symbols
CLG4; MONA; CLG4A; TBE-1; MMP-II [Similar Products]
NCBI Protein Information
72 kDa type IV collagenase; MMP-2; gelatinase A; 72 kDa gelatinase; collagenase type IV-A; neutrophil gelatinase; matrix metalloproteinase-2; matrix metalloproteinase-II
UniProt Protein Name
72 kDa type IV collagenase
UniProt Synonym Protein Names
72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1
UniProt Synonym Gene Names
UniProt Entry Name
MMP2_HUMAN
NCBI Summary for MMP2
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. This gene 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 this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
UniProt Comments for MMP2
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: Motility/polarity/chemotaxis; Secreted, signal peptide; Cell development/differentiation; Secreted; EC 3.4.24.24; Protease; Apoptosis
Chromosomal Location of Human Ortholog: 16q12.2
Cellular Component: proteinaceous extracellular matrix; extracellular space; sarcomere; mitochondrion; extracellular region; plasma membrane; nucleus
Molecular Function: protein binding; zinc ion binding; metalloendopeptidase activity; serine-type endopeptidase activity
Biological Process: axon guidance; intramembranous ossification; extracellular matrix organization and biogenesis; proteolysis; blood vessel maturation; extracellular matrix disassembly; collagen catabolic process; cellular protein metabolic process; positive regulation of innate immune response; response to hypoxia; ephrin receptor signaling pathway; angiogenesis; embryo implantation
Disease: Multicentric Osteolysis, Nodulosis, And Arthropathy
Product References and Citations for anti-MMP2 antibody
1. Nagase, H.; Barrett, A. J.; Woessner, J. F., Jr. : Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1: 421-424, 1992. 2. Collier, I. E.; Bruns, G. A. P.; Goldberg, G. I.; Gerhard, D. S. : On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes. Genomics 9: 429-434, 1991. 3. Huhtala, P.; Chow, L. T.; Tryggvason, K. : Structure of the human type IV collagenase gene. J. Biol. Chem. 265: 11077-11082, 1990. 4. Irwin, J. C.; Kirk, D.; Gwatkin, R. B. L.; Navre, M.; Cannon, P.; Giudice, L. C. : Human endometrial matrix metalloproteinase-2, a putative menstrual proteinase: hormonal regulation in cultured stromal cells and messenger RNA expression during the menstrual cycle. J. Clin. Invest. 97: 438-447, 1996
Research Articles on MMP2
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Products associated with anti-MMP2 antibody
Pathways associated with anti-MMP2 antibody
Diseases associated with anti-MMP2 antibody
Organs/Tissues associated with anti-MMP2 antibody
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