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Phenazine methylsulfate Sale

(Synonyms: 吩嗪硫酸甲酯; 5-Methylphenazinium methylsulfate) 目录号 : GC61179

A free radical generator

Phenazine methylsulfate Chemical Structure

Cas No.:299-11-6

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产品描述

Phenazine is a free radical generator.1 It has been used as an electron transfer reactant in cell viability assays.2 Phenazine (10 ?M) induces ssDNA break formation in the presence of the reducing agent NADPH in a cell-free plasmid cleavage assay when used at a concentration of 10 ?M. It induces oxidative DNA damage in an alkaline comet assay and apoptosis in A375 melanoma cells when used at a concentration of 10 ?M. Phenazine (20 nM) oxidizes cysteine-containing proteins in HepG2 cells.1

1.Lin, C.-Y., Hu, C.-T., Cheng, C.-C., et al.Oxidation of heat shock protein 60 and protein disulfide isomerase activates ERK and migration of human hepatocellular carcinoma HepG2Oncotarget7(10)11067-11082(2016) 2.Hua, A.B., Justiniano, R., Perer, J., et al.Repurposing the electron transfer reactant phenazine methosulfate (PMS) for the apoptotic elimination of malignant melanoma cells through induction of lethal oxidative and mitochondriotoxic stressCancers (Basel)11(5)E590(2019)

Chemical Properties

Cas No. 299-11-6 SDF
别名 吩嗪硫酸甲酯; 5-Methylphenazinium methylsulfate
Canonical SMILES C[N+]1=C2C=CC=CC2=NC3=C1C=CC=C3.O=S(OC)([O-])=O
分子式 C14H14N2O4S 分子量 306.34
溶解度 DMSO: 62.5 mg/mL (204.02 mM) 储存条件 4°C, protect from light
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1 mg 5 mg 10 mg
1 mM 3.2643 mL 16.3217 mL 32.6435 mL
5 mM 0.6529 mL 3.2643 mL 6.5287 mL
10 mM 0.3264 mL 1.6322 mL 3.2643 mL
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Research Update

Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii

J Biol Chem 2005 Jan 7;280(1):564-70.PMID:15507457DOI:10.1074/jbc.M406367200.

The apicomplexan parasite Toxoplasma gondii is highly susceptible to oxidative stress caused by tert-butyl-hydroperoxide, juglone, and Phenazine methylsulfate with IC(50) in the nanomolar range. Using dichlorofluorescein diacetate, a detector of endogenous oxidative stress, it was shown that juglone and Phenazine methylsulfate are potentially toxic to the parasites without affecting the host cells. These results demonstrate that T. gondii is vulnerable to oxidative challenge that results from disruption of its redox balance and so this could be an effective approach to therapeutic intervention. This study has characterized redox active and antioxidant peroxidases belonging to the class of 1-Cys and 2-Cys peroxiredoxins that play crucial roles in maintaining redox balance. The tachyzoite stages of T. gondii express thioredoxin (TgTrx), 1-Cys peroxiredoxin (TgTrx-Px2), and a 2-Cys peroxiredoxin (TgTrx-Px1) and immunofluorescent studies revealed that all three proteins are located in the cytosol of the parasite confirming previous studies on TgTrx-Px1 (Kwok, L.Y., Schluter, D., Clayton, C., and Soldati, D. (2004) Mol. Microbiol. 51, 47-61). TgTrx-Px1 showed K(m) values for H(2)O(2) and tert-butyl hydroperoxide in the nanomolar range, emphasizing the great affinity of the protein for theses substrates. Moreover, the catalytic efficiency of TgTrx-Px1 for these substrates at 10(6)-10(7) M(-1) s(-1) is unusually high, which qualifies the enzyme as an extremely potent antioxidant. Kinetic analyses revealed that TgTrx-Px1 is inhibited by tert-butyl hydroperoxide, and apparent inhibition constants were determined to be between 33 and 35.6 microm depending on the concentration of the non-inhibitory substrate thioredoxin. TgTrx-Px2 protected glutamine synthetase from inactivation by Fe(3+)/DTT, showing that it is an active peroxiredoxin.

[Comparative study of the effect of phenazine methosulfate and vitamin K3 on human erythrocytes by hemolysis curves]

Biofizika 1991 Nov-Dec;36(6):1048-50.PMID:1809383doi

Hemolysis curves were used for comparative study of Phenazine methylsulfate (PMS) and vitamin K3 action on human erythrocytes. Some differences in PMS and vitamin K3 action were revealed while the concentration of studied compounds and incubation time with them were changed. It is considered that the observed differences in PMS and vitamin K3 action are caused by different degree of oxidation of intracellular hemoglobin.