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Merck
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SRP3173

Sigma-Aldrich

TIMP-1 human

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

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352200
NACRES:
NA.32

biológiai forrás

human

rekombináns

expressed in E. coli

Teszt

≥95% (HPLC)
≥95% (SDS-PAGE)

Forma

lyophilized

hatékonyság

0.5 μg/mL

molekulatömeg

20.6 kDa

kiszerelés

pkg of 10 μg

technika/technikák

cell culture | mammalian: suitable

szennyeződések

<0.1 EU/μg endotoxin, tested

szín

white

alkalmasság

suitable for molecular biology

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

Géninformáció

human ... TIMP1(7076)

Általános leírás

Research area: Cell SignalingTIMP1 (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 with 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.

Alkalmazás

TIMP-1 human has been used for inhibition assays in enzymatic activity assays of Mmp1-CD and Mmp2-CD. It has also been used in interaction immunoassay.

Biokémiai/fiziológiai hatások

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.

Szekvencia

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

Fizikai forma

Lyophilized from 10 mM Sodium Phosphate, pH 7.5.

Feloldás

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.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Tissue Inhibitor Of Matrix Metalloproteinase-1 Is Required for High-Fat Diet-Induced Glucose Intolerance and Hepatic Steatosis in Mice.
Fj?re E, et al.
PLoS ONE, 10(7) (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
TIMP-1 Inhibits Apoptosis in Lung Adenocarcinoma Cells via Interaction with Bcl-2.
Nalluri S, et al.
PLoS ONE, 10(9) (2015)
Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.
Benjamin MM1 and Khalil RA.
EXS, 103, 209-279 (2012)
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

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