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T1077

Sigma-Aldrich

Tissue Inhibitor of Metalloproteinase-2 human

recombinant, expressed in CHO cells, >95% (SDS-PAGE), lyophilized powder

Synonym(s):

TIMP-2

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in CHO cells

assay

>95% (SDS-PAGE)

form

lyophilized powder

mol wt

apparent mol wt ~20 kDa

technique(s)

activity assay: suitable
inhibition assay: suitable

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... TIMP2(7077)

General description

Tissue inhibitor of metalloproteinase-2 (TIMP-2) is an extracellular inhibitor of matrix metalloproteinases (MMPs). There are six conserved cysteine residues forming disulfide loops in its amino- and carboxy-terminal domains. The gene encoding this protein is localized on human chromosome 17q25.[1]

Biochem/physiol Actions

TIMP-2 has a greater binding efficiency to MMP-2 than the other MMPs. Although TIMP-2 is an inhibitor of MMP-2, it is also required at low concentrations for the activation of MMP-2.
Tissue inhibitor of metalloproteinase-2 (TIMP-2), like other protease inhibitors, functions as a key modulator of extracellular matrix degradation during tissue development and remodeling.[2] TIMP-2 can also act through a matrix metalloproteinase (MMP)-independent mechanism inhibiting endothelial cell proliferation in vitro.[3] It demonstrates anti-angiogenic activities in vivo. TIMP-2 is a target gene of the microRNA-miR-22.[4]

Physical form

Lyophilized from a 0.2 μm filtered solution in 25 mM Tris, and 150 mM sodium chloride, pH 7.5.

Analysis Note

The biological activity is measured by the ability to inhibit human MMP-2 hydrolysis of a fluorogenic MMP substrate.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves


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Genetics of Moyamoya disease.
Roder C
Journal of Human Genetics, 55(11), 711-716 (2010)
Matrix MetalloProteinases (MMPs) andTissue Inhibitors of MetalloProteinases (TIMPs): positive and negative regulators intumor cell adhesion
Dimitra B
Seminars in Cancer Biology, 20(3), 161-168 (2010)
Promotion of astrocytoma cell invasion by micro RNA-22 targeting of tissue inhibitor of matrix metalloproteinase-2.
Ohnishi YI
Journal of Neurosurgery. Spine, 26(3), 396-403 (2017)
Growth-stimulatory activity of TIMP-2 is mediated through c-Src activation followed by activation of FAK, PI3-kinase/AKT, and ERK1/2 independent of MMP inhibition in lung adenocarcinoma cells.
Kim Hle
Oncotarget, 6(40), 42905-42922 (2015)
W G Stetler-Stevenson et al.
The Journal of biological chemistry, 265(23), 13933-13938 (1990-08-15)
Human tissue inhibitor of metalloproteinase-2 (TIMP-2) was cloned and sequenced from an A2058 human melanoma cell cDNA library. When the sequence was compared with that of human TIMP-1 at both the nucleotide and deduced amino acid levels, the homology appeared

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