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Dokumenty

567540

Sigma-Aldrich

Sodium Orthovanadate

A broad spectrum potent inhibitor of protein tyrosine phosphatases.

Synonim(y):

Sodium Orthovanadate, PTP Inhibitor X

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About This Item

Wzór empiryczny (zapis Hilla):
Na3O4V
Numer CAS:
Masa cząsteczkowa:
183.91
Numer MDL:
Kod UNSPSC:
12352202
NACRES:
NA.77

Poziom jakości

Postać

solid

producent / nazwa handlowa

Calbiochem®

warunki przechowywania

OK to freeze

kolor

white to off-white

rozpuszczalność

water: 10 mg/mL

Warunki transportu

ambient

temp. przechowywania

10-30°C

InChI

1S/3Na.4O.V/q3*+1;;3*-1;

Klucz InChI

IHIXIJGXTJIKRB-UHFFFAOYSA-N

Opis ogólny

A broad spectrum potent inhibitor of protein tyrosine phosphatases. Also known to inhibit Na+,K+-ATPase, acid and alkaline phosphatases, phosphofructokinase, and adenylate kinase. Also inhibits the ATPase activity of the reconstituted binding protein-dependent ATP-Binding Cassette (ABC) transporter for maltose (MalFGK2) of Salmonella typhimurium in the micromolar range. Can be converted to pervanadate by hydrogen peroxide.
A broad spectrum potent inhibitor of protein tyrosine phosphatases. Also known to inhibit Na+/K+ ATPase, acid and alkaline phosphatases, phosphofructokinase, and adenylate kinase. Most recently shown to inhibit ATPase activity of the reconstituted binding protein-dependent ATP-Binding Cassette (ABC) transporter for maltose (MalFGK2) of Salmonella typhimurium in the micromolar range. Can be converted to pervanadate by hydrogen peroxide.

Działania biochem./fizjol.

Cell permeable: no
Primary Target
Na+,K+-ATPase, acid , alkaline phosphatases, phosphofructokinase, and adenylate kinase
Product does not compete with ATP.
Reversible: no

Ostrzeżenie

Toxicity: Harmful (C)

Rekonstytucja

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Inne uwagi

Huyer, G., et al. 1997. J. Biol. Chem. 272, 843.
Hunke, S., et al. 1995. Biochem. Biophys. Res. Commun.216, 589.
Levchuck, S.G., et al. 1994. Pediatric Res.37, 382A.
Fohr, K.J., et al. 1989. Biochem. J.262, 83.
Swarup, G., et al. 1982. Biochem. Biophys. Res. Commun.107, 1104.
Seargeant, L.E. and Stinson, R.A. 1979. Biochem. J.181, 247.

Informacje prawne

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
This page may contain text that has been machine translated.

Piktogramy

Exclamation mark

Hasło ostrzegawcze

Warning

Zwroty wskazujące rodzaj zagrożenia

Klasyfikacja zagrożeń

Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Eye Irrit. 2 - Skin Irrit. 2

Kod klasy składowania

13 - Non Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Seungkirl Ahn et al.
The Journal of biological chemistry, 277(29), 26642-26651 (2002-05-16)
Endocytosis of ligand-activated receptors requires dynamin-mediated GTP hydrolysis, which is regulated by dynamin self-assembly. Here, we demonstrate that phosphorylation of dynamin I by c-Src induces its self-assembly and increases its GTPase activity. Electron microscopic analyses reveal that tyrosine-phosphorylated dynamin I
Fan Xia et al.
Redox biology, 52, 102284-102284 (2022-03-30)
Autophagy is an evolutionarily conserved self-protecting mechanism implicated in cellular homeostasis. ATG4B plays a vital role in autophagy process via undertaking priming and delipidation of LC3. Chemical inhibitors and regulative modifications such as oxidation of ATG4B have been demonstrated to
Tina Branscombe Miranda et al.
FEBS letters, 577(1-2), 181-186 (2004-11-06)
It has been reported that S-adenosylmethionine-dependent protein methylation in rat kidney extracts can be greatly stimulated by tyrphostin A25, a tyrosine kinase inhibitor. We have investigated the nature of this stimulation. We find that addition of tyrphostin A25, in combination
Dinesh Kumar Verma et al.
eNeuro, 7(5) (2020-09-06)
Small ubiquitin-like modifier (SUMO) is a widespread regulatory mechanism of post-translational modification (PTM) that induces rapid and reversible changes in protein function and stability. Using SUMO conjugase Ubc9-overexpressing or knock-down cells in Parkinson's disease (PD) models, we demonstrate that SUMOylation

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