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M9445

Sigma-Aldrich

Matrix Metalloproteinase-2

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

Sinonimo/i:

72 kD Gelatinase, 72 kD Type IV Collagenase, Gelatinase A, MMP-2

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About This Item

Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.32

Ricombinante

expressed in NSO cells

Livello qualitativo

Saggio

>95% (SDS-PAGE)

Forma fisica

buffered aqueous glycerol solution

PM

apparent mol wt ~72 kDa

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Informazioni sul gene

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

Descrizione generale

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.

Specificità

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

Applicazioni

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

Azioni biochim/fisiol

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.

Stato fisico

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.

Risultati analitici

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

Note legali

Brij is a registered trademark of Croda International PLC

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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


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Gelatinase A
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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