567540
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:
Molecular Weight:
183.91
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77
Quality Level
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
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.
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
Signal Word
Warning
Hazard Statements
Precautionary Statements
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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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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