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Key Documents

SRP3173

Sigma-Aldrich

TIMP-1 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture

Sinonimo/i:

Erythroid-Potentiating activity, Fibroblast collagenase inhibitor, Tissue inhibitor of metalloproteinase

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in E. coli

Saggio

≥95% (HPLC)
≥95% (SDS-PAGE)

Forma fisica

lyophilized

Potenza

0.5 μg/mL

PM

20.6 kDa

Confezionamento

pkg of 10 μg

tecniche

cell culture | mammalian: suitable

Impurezze

<0.1 EU/μg endotoxin, tested

Colore

white

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... TIMP1(7076)

Descrizione generale

TIMP1 (tissue inhibitor of metalloproteinase 1) is a glycoprotein and belongs to the 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 containing three disulfide bonds. The N-terminal domain inhibits MMPs by folding into a separate unit. Recombinant human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.

Azioni biochim/fisiol

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 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.

Sequenza

CTCVPPHPQT AFCNSDLVIR AKFVGTPEVN QTTLYQRYEI KMTKMYKGFQ ALGDAADIRF VYTPAMESVC GYFHRSHNRS EEFLIAGKLQ DGLLHITTCS FVAPWNSLSL AQRRGFTKTY TVGCEECTVF PCLSIPCKLQ SGTHCLWTDQ LLQGSEKGFQ SRHLACLPRE PGLCTWQSLR SQIA

Stato fisico

Lyophilized from 10 mM Sodium Phosphate, pH 7.5.

Ricostituzione

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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D E Gomez et al.
European journal of cell biology, 74(2), 111-122 (1997-11-14)
Four members of the tissue inhibitor of metalloproteinases (TIMP) family have been characterized so far, designated as TIMP-1, TIMP-2, TIMP-3, and TIMP-4. TIMP-1 and TIMP-2 are capable of inhibiting the activities of all known matrix metalloproteinases (MMPs) and as such
Gary J Litherland et al.
Arthritis & rheumatology (Hoboken, N.J.), 66(8), 2175-2187 (2014-04-24)
To assess the role of glycogen synthase kinase 3 (GSK-3) as a regulator of cartilage destruction in human tissue and a murine model of osteoarthritis (OA). Surgical destabilization of the medial meniscus (DMM) was performed to induce experimental murine OA
Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.
Benjamin MM1 and Khalil RA.
EXS, 103, 209-279 (2012)
TIMP-1 Inhibits Apoptosis in Lung Adenocarcinoma Cells via Interaction with Bcl-2.
Nalluri S, et al.
PLoS ONE, 10(9) (2015)
Jiayin Peng et al.
Theriogenology, 84(9), 1636-1643 (2015-10-06)
Tissue inhibitors of metalloproteinases (TIMPs) are associated with several reproductive processes, such as mammalian follicular growth, ovulation, CL formation, and embryonic development. However, the expression and function of TIMPs in goat oviducts remain unclear. This work aimed to identify TIMP1

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