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M9070

Sigma-Aldrich

Matrix Metalloproteinase-2 human

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

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

recombinant

expressed in NSO cells

Quality Level

Assay

>90% (SDS-PAGE)

form

lyophilized powder

mol wt

apparent mol wt ~69 kDa

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... MMP2(4313)

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SRP3118M9195SAE0078
Sigma-Aldrich

Sigma-Aldrich

SRP3118

MMP-2 human

assay

>90% (SDS-PAGE)

assay

≥98% (HPLC), ≥98% (SDS-PAGE)

assay

>95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

form

lyophilized powder

form

lyophilized

form

buffered aqueous solution

form

liquid

mol wt

apparent mol wt ~69 kDa

mol wt

62.0 kDa

mol wt

apparent mol wt 52-55 kDa

mol wt

calculated mol wt 66 kDa, observed mol wt 82 kDa by SDS-PAGE (The protein migrates as a 82 kDa protein on SDS-PAGE due to glycosylation)

UniProt accession no.

P08253

UniProt accession no.

P08253

UniProt accession no.

P03956

UniProt accession no.

P14780

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

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

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.

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. 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.

Physical form

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.

Analysis Note

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

Legal Information

Brij is a registered trademark of Croda International PLC

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

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

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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