Inhibitor of thioredoxin reductase (TrxR) (IC50 = 20 nM; Ki = 4 nM for the NADPH-reduced form of human cytosolic TrxR). Thought to induce the mitochondrial permeability transition via inhibition of mitochondrial TrxR. Also exhibits anti-inflammatory and immunosuppressive activities; inhibits 5-lipoxygenase at high concentrations and stimulates LTA hydrolase at low concentrations.
|Storage||Store at RT|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
|Solvent||Max Conc. mg/mL||Max Conc. mM|
Preparing Stock Solutions
The following data is based on the product molecular weight 678.48. Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.
|Concentration / Solvent Volume / Mass||1 mg||5 mg||10 mg|
|1 mM||1.47 mL||7.37 mL||14.74 mL|
|5 mM||0.29 mL||1.47 mL||2.95 mL|
|10 mM||0.15 mL||0.74 mL||1.47 mL|
|50 mM||0.03 mL||0.15 mL||0.29 mL|
References are publications that support the biological activity of the product.
Kim et al (2007) Auranofin blocks interleukin-6 signalling by inhibiting phosphorylation of JAK1 and STAT3. Immunology 122 607 PMID: 17645497
Rigobello et al (2002) Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative. Br.J.Pharmacol. 136 1162 PMID: 12163349
Gromer et al (1998) Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J.Biol.Chem. 273 20096 PMID: 9685351
Betts et al (1990) Auranofin stimulates LTA hydrolase and inhibits 5-lipoxygenase/LTA synthase activity of isolated human neutrophils. Biochem.Pharmacol. 39 1233 PMID: 2157444
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1 Citation for Auranofin
Citations are publications that use Tocris products. Selected citations for Auranofin include:
Tsai et al (2015) Zeta Inhibitory Peptide Disrupts Electrostatic Interactions That Maintain Atypical Protein Kinase C in Its Active Conformation on the Scaffold p62. J Biol Chem 290 21845 PMID: 26187466
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