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Key Documents

M9070

Sigma-Aldrich

Matrix Metalloproteinase-2 human

>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Synonyme(s) :

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

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About This Item

Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in NSO cells

Niveau de qualité

Pureté

>90% (SDS-PAGE)

Forme

lyophilized powder

Poids mol.

apparent mol wt ~69 kDa

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

human ... MMP2(4313)

Description générale

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.

Spécificité

MMP-2 specifically cleaves type IV collagen, a major structural component of basement membranes.

Application

Matrix metalloproteinase-2 (MMP2) human has been used:
  • As a standard in zymography to measure gelatinolytic activity of MMP2.
  • In enzymatic method for dissociation of brain tissue to single cells.

Actions biochimiques/physiologiques

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. MMP-2 activity is associated with human ovarian follicular development. MMP2 expression is elevated in human myocardial infarction and dilated cardiomyopathy. Wound fluid from chronic leg ulcers show elevated expression of MMP2. Overexpression of active MMP2 affects wound healing in chronic leg ulcers. MMP2 activity is inhibited by tissue inhibitor of metalloproteinase-2 (TIMP-2). Human follicular fluid MMP-2 level acts as a potential biomarker of oocyte maturation in in vitro fertilization and intracytoplasmic sperm injection (ICSI) cycles.
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.

Forme physique

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 5 mM CaCl2, 150 mM NaCl, and 1 μM ZnCl2, pH 7.5.

Reconstitution

It is recommended that 0.1 mL of buffer (100 mM Tris, 10 mM calcium chloride, 150 mM sodium chloride, and 0.05% Brij® L23, pH 8.0) be used to give a stock solution of the enzyme at 100 μg/mL.

Remarque sur l'analyse

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

Informations légales

Brij is a registered trademark of Croda International PLC

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
Matrix metalloproteinase 2 level in human follicular fluid is a reliable marker of human oocyte maturation in in vitro fertilization and intracytoplasmic sperm injection cycles.
Yang WJ
Reproductive Biology and Endocrinology, 13:102 (2015)
A non-aggressive, highly efficient, enzymatic method for dissociation of human brain-tumors and brain-tissues to viable single-cells.
Volovitz I
BMC Neuroscience, 17(1):30 (2016)
Takashi Temma et al.
PloS one, 9(7), e102180-e102180 (2014-07-11)
Since matrix metalloproteinase-2 (MMP-2) is an important marker of tumor malignancy, we developed an original drug design strategy, MMP-2 activity dependent anchoring probes (MDAP), for use in MMP-2 activity imaging, and evaluated the usefulness of this probe in in vitro
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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