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Key Documents

SRP6445

Sigma-Aldrich

TIMP1 human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Sinónimos:

CLGI, EPA, EPO, FLJ90373, HCI, TIMP, TIMP metallopeptidase inhibitor 1, TIMP-1

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in HEK 293 cells

tag

6-His tagged (C-terminus)

assay

≥95% (SDS-PAGE)

form

lyophilized

mol wt

calculated mol wt 24 kDa
observed mol wt 28-32 kDa by SDS-PAGE (DTT-reduced.)

packaging

pkg of 10 μg

impurities

<1 EU/μg endotoxin (LAL test)

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... TIMP1(7076)

General description

TIMP1 (tissue inhibitor of metalloproteinase 1) is a glycoprotein and is a member of TIMP family of endogenous MMP (matrix metalloproteinase) inhibitors. Humans contain four TIMPs. All TIMPs contain an N-terminal of 125 residues, a 65-residue C-terminal, and both these domains contain three disulfide bonds. The N-terminal domain inhibits MMPs by folding into a separate unit. TIMP1 is encoded by the gene mapped to human chromosome Xp11.23.

Biochem/physiol Actions

TIMP1 functions as a poor inhibitor of MT1 (membrane type 1)-MMP, MT3-MMP, MT5-MMP and MMP-19. It inhibits ADAM10 (a disintegrin and metalloproteinase domain-containing protein 10) protein. In human umbilical vein endothelial cells (HUVECs), the down-regulation of TIMP1 and up-regulation of MMP-3 results in aberrant endothelium-dependent vasodilation, EC (endothelial cell) death, and endothelial interruption in a FOXO3 (forkhead box O3)-mediated manner. In patients with CAD (coronary artery disease) and acute coronary syndrome (ACS), the urine levels of this protein are elevated. This protein interacts with Bcl-2 (B cell lymphoma) protein, and induces apoptosis in lung adenocarcinoma cells. The plasma levels of this protein are increased in patients with obesity and obesity-related disorders, such as steatosis, where it participates in pathogenesis of diet-induced hepatic steatosis and glucose intolerance.

Physical form

Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Barbara Grünwald et al.
Gastroenterology, 151(5), 1011-1024 (2016-08-11)
Pancreatic ductal adenocarcinoma (PDAC) metastasizes to liver at early stages, making this disease highly lethal. Tissue inhibitor of metalloproteinases-1 (TIMP1) creates a metastasis-susceptible environment in the liver. We investigated the role of TIMP1 and its receptor CD63 in metastasis of
T Y Ho et al.
Domestic animal endocrinology, 59, 1-10 (2016-11-21)
Nursing for 2 d from birth supports neonatal porcine uterine and cervical development. However, it is not clear how timing or duration of lactocrine signaling from birth (postnatal day = PND 0) affects development of neonatal female reproductive tract tissues. Therefore
M Okamoto et al.
International endodontic journal, 52(7), 1051-1062 (2019-02-15)
To evaluate the dentinogenetic effects of tissue inhibitor of metalloprotease (TIMP1) on human pulp cells in vitro and rat pulp tissue in vivo. The effect of TIMP1 on pulp cell functions related to hard tissue formation as part of the wound healing
Pierre Kunz et al.
BMC cancer, 16, 223-223 (2016-03-17)
Matrix metalloproteinases (MMPs) are crucially involved in the regulation of multiple stages of cancer progression. Elevated MMP levels have been associated with the development of metastases and poor prognosis in several types of cancer. However, the role of MMPs in
Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.
Benjamin MM1 and Khalil RA.
EXS, 103, 209-279 (2012)

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