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567540

Sigma-Aldrich

Sodium Orthovanadate

A broad spectrum potent inhibitor of protein tyrosine phosphatases.

Synonym(s):

Sodium Orthovanadate, PTP Inhibitor X

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About This Item

Empirical Formula (Hill Notation):
Na3O4V
CAS Number:
13721-39-6
Molecular Weight:
183.91
MDL number:
MFCD00003511
UNSPSC Code:
12352200

Quality Level

100

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

color

white to off-white

solubility

water: 10 mg/mL

shipped in

ambient

storage temp.

10-30°C

InChI

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

InChI key

IHIXIJGXTJIKRB-UHFFFAOYSA-N

General description

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.

Biochem/physiol Actions

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

Warning

Toxicity: Harmful (C)

Reconstitution

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

Other Notes

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.

Legal Information

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

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Classifications

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

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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The Journal of biological chemistry, 277(29), 26642-26651 (2002-05-16)
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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
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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

Articles

Phosphoprotein Phosphatases (Tyrosine)

Protein tyrosine phosphatases (PTPs) and related enzymes (more than a hundred coded by the human genome) are more numerous than serine/threonine phosphatases. They belong to four families, three of which possess a conserved cysteine for catalysis and some conserved features of 3-dimensional structure. The catalytic mechanism of these PTPs involves the transient formation of a covalently phosphorylated enzyme.

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