M9070

Matrix Metalloproteinase-2 human

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

• Synonym(s): 72 Kd Gelatinase, 72 Kd Type IV Collagenase, Gelatinase A, MMP-2
• MDL number: MFCD01324322
• UNSPSC Code: 12352204
• NACRES: NA.32

Properties

• recombinant: expressed in NSO cells
• Quality Level: 200
• Assay: >90% (SDS-PAGE)
• form: lyophilized powder
• mol wt: apparent mol wt ~69 kDa
• UniProt accession no.: P08253
• storage temp.: −20°C
• Gene Information: human ... MMP2(4313)

Description

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.[1] 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.[2]

Specificity

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

Application

Matrix metalloproteinase-2 (MMP2) human has been used:

• As a standard in zymography to measure gelatinolytic activity of MMP2.[3]
• In enzymatic method for dissociation of brain tissue to single cells.[4]

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.[5] MMP-2 cleaves native type I collagen to N-terminal ¾ and C-terminal ¼ fragments identical to those generated by interstitial collagenases.[1] MMP2 and MMP9 play an essential role in matrix degradation and they are implicated in the maintenance of neovascularization.[6] MMP-2 activity is associated with human ovarian follicular development.[7] MMP2 expression is elevated in human myocardial infarction and dilated cardiomyopathy.[2][8] Wound fluid from chronic leg ulcers show elevated expression of MMP2. Overexpression of active MMP2 affects wound healing in chronic leg ulcers.[8] 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.[3]

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.

Analysis Note

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

Legal Information

Brij is a registered trademark of Croda International PLC

Safety Information

• Storage Class Code: 10 - Combustible liquids
• WGK: WGK 3
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable
• Personal Protective Equipment: dust mask type N95 (US), Eyeshields, Gloves