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Merck

M9445

Sigma-Aldrich

Matrix Metalloproteinase-2 from mouse

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

Synonim(y):

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

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About This Item

Numer MDL:
Kod UNSPSC:
12352202
NACRES:
NA.32

rekombinowane

expressed in NSO cells

Poziom jakości

Próba

>95% (SDS-PAGE)

Formularz

buffered aqueous glycerol solution

masa cząsteczkowa

apparent mol wt ~72 kDa

numer dostępu UniProt

Warunki transportu

wet ice

temp. przechowywania

−20°C

informacje o genach

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

Opis ogólny

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.

Specyficzność

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

Zastosowanie

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

Działania biochem./fizjol.

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. 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.

Postać fizyczna

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.

Komentarz do analizy

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

Informacje prawne

Brij is a registered trademark of Croda International PLC
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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 2

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

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


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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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