M9445

Matrix Metalloproteinase-2 from mouse

recombinant, expressed in NSO cells, >95% (SDS-PAGE), buffered aqueous glycerol solution

• Synonym(s): Collagenase Type IV 72 kDa, Gelatinase 72 kDa, Gelatinase A, MMP-2
• UNSPSC Code: 12352202
• NACRES: NA.32
• MDL number: MFCD01324322

Properties

• Product Name: Matrix Metalloproteinase-2 from mouse, recombinant, expressed in NSO cells, >95% (SDS-PAGE), buffered aqueous glycerol solution
• recombinant: expressed in NSO cells
• assay: >95% (SDS-PAGE)
• form: buffered aqueous glycerol solution
• mol wt: apparent mol wt ~72 kDa
• UniProt accession no.: P33434; P33436
• shipped in: wet ice
• storage temp.: −20°C
• Quality Level: 200
• Gene Information: mouse ... Mmp2(17390) ; rat ... Mmp2(81686)

Description

Analysis Note

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

Application

Matrix metalloproteinase-2 (MMP2) human has been used as a standard in zymography to measure proteolytic activity of MMP-2.[1][2]

Biochem/physiol Actions

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.

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.[3] MMP-2 cleaves native type I collagen to N-terminal ¾ and C-terminal ¼ fragments identical to those generated by interstitial collagenases.[4] MMP2 and MMP9 play an essential role in matrix degradation and they are implicated in the maintenance of neovascularization.[5] In mice, deletion or inhibition of MMP2 protects against myocardial rupture.[6]

The amino acid sequences 1-662[7] of the proenzymes of MMP-2 are identical between mouse and rat.

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.[4] 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.[6]

Physical form

Supplied as a 0.2 μm filtered solution of 25 mM Tris, pH 7.5, 5 mM calcium chloride, 75 mM sodium chloride, 0.025% Brij^® 35 and 50% glycerol.

Legal Information

Brij is a registered trademark of Croda International PLC

Safety Information

• Storage Class: 12 - Non Combustible Liquids
• wgk: WGK 2
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)