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567540

Sigma-Aldrich

Sodium Orthovanadate

A broad spectrum potent inhibitor of protein tyrosine phosphatases.

Sinónimos:

Sodium Orthovanadate, PTP Inhibitor X

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About This Item

Fórmula empírica (notación de Hill):
Na3O4V
Número de CAS:
13721-39-6
Peso molecular:
183.91
Número MDL:
MFCD00003511
Código UNSPSC:
12352202
NACRES:
NA.77

Nivel de calidad

100

descripción

RTECS - YW1120000

Formulario

solid

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze

color

white to off-white

solubilidad

water: 10 mg/mL

Condiciones de envío

ambient

temp. de almacenamiento

10-30°C

cadena SMILES

[V](=O)([O-])([O-])[O-].[Na+].[Na+].[Na+]

InChI

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

Clave InChI

IHIXIJGXTJIKRB-UHFFFAOYSA-N

Descripción general

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.

Acciones bioquímicas o fisiológicas

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

Advertencia

Toxicity: Harmful (C)

Reconstitución

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

Otras notas

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.

Información legal

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

Pictogramas

Exclamation mark
GHS07

Palabra de señalización

Warning

Clasificaciones de peligro

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

Código de clase de almacenamiento

13 - Non Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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

Artículos

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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