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M9445

Sigma-Aldrich

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

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About This Item

MDL number:
MFCD01324322
UNSPSC Code:
12352202
NACRES:
NA.32

recombinant

expressed in NSO cells

Quality Level

200

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

Gene Information

mouse ... Mmp2(17390)
rat ... Mmp2(81686)

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.

Specificity

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

Application

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

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. In mice, deletion or inhibition of MMP2 protects against myocardial rupture.
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.

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.

Analysis Note

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

Legal Information

Brij is a registered trademark of Croda International PLC

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Murphy, G. et al.
Handbook of Proteolytic Enzymes, 497-503 (2004)
INHIBITION OF GELATINASE ACTIVITY OF
MMP-2 AND MMP-9 BY EXTRACTS OF Bauhinia
ungulata L. Kamilla.
Bioscience Journal, 31, 584-590 (2015)
Inhibition of Gelatinases by Vegetable Extracts
of the Species Tapirira guianensis
(Stick Pigeon).
Longatti T R
British Journal of Pharmaceutical Research, 1(4), 133-140 (2011)
Immunohistochemical expression of MMP-14 and MMP-2, and MMP-2 activity during human ovarian follicular development.
Vos MC
Reproductive Biology and Endocrinology, 12:12 (2014)
P Reponen et al.
The Journal of biological chemistry, 267(11), 7856-7862 (1992-04-15)
We report the isolation of a cDNA clone providing the first and complete sequence of mouse 72-kDa type IV collagenase. The clone contains 2800 nucleotides with a 1986-nucleotide open reading frame coding for 662 amino acids. The amino acid sequence
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