Matrix metalloproteinase-2 (MMP-2) also known as gelatinase or type IV collagenase is a 72kDa protein. MMP-2 is a member of matrix metalloproteinase (MMP) family of enzymes. Basic structure of MMP2 contains signal peptide domain that targets the enzyme for secretion, the pro-peptide domain, which is removed when the enzyme is activated and the catalytic site containing gelatin-binding domain.
MMP-2 specifically cleaves type IV collagen, a major structural component of basement membranes.
Matrix metalloproteinase-2 (MMP2) human has been used:
- As a standard in zymography to measure gelatinolytic activity of MMP2.
- In enzymatic method for dissociation of brain tissue to single cells.
Matrix metalloproteinase-2 (MMP-2) cleaves gelatin, type IV, V, VII, X, and XI collagens, fibronectin, elastin, laminin, proteoglycans, and a range of non extracellular matrix (ECM ) components. MMP-2 cleaves native type I collagen to N-terminal ¾ and C-terminal ¼ fragments identical to those generated by interstitial collagenases. MMP2 and MMP9 play an essential role in matrix degradation and they are implicated in the maintenance of neovascularization. MMP-2 activity is associated with human ovarian follicular development. MMP2 expression is elevated in human myocardial infarction and dilated cardiomyopathy. Wound fluid from chronic leg ulcers show elevated expression of MMP2. Overexpression of active MMP2 affects wound healing in chronic leg ulcers. MMP2 activity is inhibited by tissue inhibitor of metalloproteinase-2 (TIMP-2). Human follicular fluid MMP-2 level acts as a potential biomarker of oocyte maturation in in vitro fertilization and intracytoplasmic sperm injection (ICSI) cycles.
MMP-2 degrades general matrix components and may have a role in processes such as host defense, cell proliferation, and protein turnover as well as tissue remodeling.
Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 5 mM CaCl2, 150 mM NaCl, and 1 μM ZnCl2, pH 7.5.
It is recommended that 0.1 mL of buffer (100 mM Tris, 10 mM calcium chloride, 150 mM sodium chloride, and 0.05% Brij® L23, pH 8.0) be used to give a stock solution of the enzyme at 100 μg/mL.
The biological activity is measured by its ability to cleave a fluorogenic peptide substrate.
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