Matrix, >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Stock Code: 3573482
Manufacturer Part No: M9070-10UG

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Descriptions

Analysis Note

The biological activity is measured by its ability to cleave a fluorogenic peptide substrate.

Application

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.

Biochem/physiol Actions

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.

General description

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.

Legal Information

Brij is a registered trademark of Croda International PLC

Physical form

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.

Reconstitution

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.

Specificity

MMP-2 specifically cleaves type IV collagen, a major structural component of basement membranes.