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M9445

Sigma-Aldrich

Matrix Metalloproteinase-2 from mouse

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

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Synonym(s):
Collagenase Type IV 72 kDa, Gelatinase 72 kDa, Gelatinase A, MMP-2
MDL number:
NACRES:
NA.32

recombinant

expressed in NSO cells

Quality Level

Assay

>95% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

apparent mol wt ~72 kDa

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

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

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This Item
M9070M9195M8945
assay

>95% (SDS-PAGE)

assay

>90% (SDS-PAGE)

assay

>95% (SDS-PAGE)

assay

>90% (SDS-PAGE)

form

buffered aqueous glycerol solution

form

lyophilized powder

form

buffered aqueous solution

form

buffered aqueous solution

mol wt

apparent mol wt ~72 kDa

mol wt

apparent mol wt ~69 kDa

mol wt

apparent mol wt 52-55 kDa

mol wt

apparent mol wt ~93 kDa

UniProt accession no.

P33434, P33436

UniProt accession no.

P08253

UniProt accession no.

P03956

UniProt accession no.

P14780

shipped in

wet ice

shipped in

-

shipped in

dry ice

shipped in

dry ice

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Customers Also Viewed

Slide 1 of 7

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INHIBITION OF GELATINASE ACTIVITY OF
MMP-2 AND MMP-9 BY EXTRACTS OF Bauhinia
ungulata L. Kamilla.
Bioscience Journal, 31, 584-590 (2015)
Gelatinase A
Murphy, G. et al.
Handbook of Proteolytic Enzymes, 497-503 (2004)
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)
Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor.
Rodriguez-Manzaneque JC
Proceedings of the National Academy of Sciences of the USA, 98(22), 12485-12490 (2001)

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