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567540

Sigma-Aldrich

Sodium Orthovanadate

A broad spectrum potent inhibitor of protein tyrosine phosphatases.

Synonyme(s) :

Sodium Orthovanadate, PTP Inhibitor X

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About This Item

Formule empirique (notation de Hill):
Na3O4V
Numéro CAS:
Poids moléculaire :
183.91
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Niveau de qualité

Forme

solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Couleur

white to off-white

Solubilité

water: 10 mg/mL

Conditions d'expédition

ambient

Température de stockage

10-30°C

InChI

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

Clé InChI

IHIXIJGXTJIKRB-UHFFFAOYSA-N

Description générale

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.

Actions biochimiques/physiologiques

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

Avertissement

Toxicity: Harmful (C)

Reconstitution

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

Autres remarques

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.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Classification des risques

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

Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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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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