|Reactivity||Human, Mouse, Rat|
|Calculated MW||73882 Da|
|Other Names||72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, PEX, MMP2, CLG4A|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human MMP-2 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP-2 Antibody (propeptide) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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. Involved in the formation of the fibrovascular tissues in association with MMP14. 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.|
|Cellular 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|
|Tissue Location||Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.|
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Provided below are standard protocols that you may find useful for product applications.
The matrix metalloproteinases (MMPs) are a family of closely related proteolytic enzymes which are involved in the degradation of different components of the extracellular matrix. There is increasing evidence to indicate that individual MMPs have an important role in tumor invasion and tumour spread. MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme (1). MMP2 is regulated differently from other MMPs, suggesting that it may play a unique role in cell-matrix interactions, including cell invasion. The conversion from the 72 kDa progelatinase A to the active 62 kDa species may be a key event in the acquisition of invasive potential(2)
1. Murray GI, et al. J Pathol, 185(3):256-61
2. Yu, AE, et al. Biochem Cell Biol, 74(6):823-31, 1996.
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