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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

Sinónimos:

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

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About This Item

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.32

recombinante

expressed in NSO cells

Nivel de calidad

Análisis

>95% (SDS-PAGE)

formulario

buffered aqueous glycerol solution

mol peso

apparent mol wt ~72 kDa

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

Información sobre el gen

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

Descripción general

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.

Especificidad

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

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Forma física

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.

Nota de análisis

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

Información legal

Brij is a registered trademark of Croda International PLC

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

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


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

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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