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AMI-1 free acid Sale

(Synonyms: 猩红酸) 目录号 : GC39840

AMI-1 is a potent and specific Histone Methyltransferase (HMT) inhibitor with IC50 of 3.0 μM and 8.8 μM for yeast Hmt1p and human PRMT1, respectively.

AMI-1 free acid Chemical Structure

Cas No.:134-47-4

规格 价格 库存 购买数量
10mM (in 1mL DMSO)
¥299.00
现货
5mg
¥270.00
现货
10mg
¥270.00
现货
25mg
¥450.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

AMI-1 is a potent and specific Histone Methyltransferase (HMT) inhibitor with IC50 of 3.0 μM and 8.8 μM for yeast Hmt1p and human PRMT1, respectively.

[1] Donghang Cheng, et al. J Biol Chem . 2004 Jun 4;279(23):23892-9.

Chemical Properties

Cas No. 134-47-4 SDF
别名 猩红酸
Canonical SMILES O=C(NC1=CC2=CC(S(=O)(O)=O)=CC(O)=C2C=C1)NC3=CC4=CC(S(=O)(O)=O)=CC(O)=C4C=C3
分子式 C21H16N2O9S2 分子量 504.49
溶解度 DMSO: 83.33 mg/mL (165.18 mM) 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 1.9822 mL 9.911 mL 19.822 mL
5 mM 0.3964 mL 1.9822 mL 3.9644 mL
10 mM 0.1982 mL 0.9911 mL 1.9822 mL
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Research Update

An inhibitor of protein arginine methyltransferases, 7,7'-carbonylbis(azanediyl)bis(4-hydroxynaphthalene-2-sulfonic acid (AMI-1), is a potent scavenger of NADPH-oxidase-derived superoxide

Mol Pharmacol 2010 Feb;77(2):280-7.PMID:19903831DOI:10.1124/mol.109.061077.

The methylation of proteins is an important post-translational mechanism that has been established to influence the activity of nuclear and nucleic acid binding proteins. Much less is known about the importance of protein methylation in the regulation of cytosolic proteins. Increased methylation of proteins is observed in cardiovascular disease and occurs in conjunction with elevated production of reactive oxygen species. However, the nature of the relationship between reactive oxygen species and protein methylation is poorly understood. Therefore, the goal of the current study was to determine whether protein methylation influences the catalytic activity of the NADPH oxidases (Nox), which are a family of enzymes responsible for the generation of superoxide. We found that the selective inhibitor of protein arginine methyltransferases 7,7'-carbonylbis(azanediyl)bis(4-hydroxynaphthalene-2-sulfonic acid (AMI-1) was a potent antagonist of Nox-derived superoxide production. However, structurally and mechanistically dissimilar inhibitors of protein methylation and coexpression of protein arginine methyltransferase 1 did not influence Nox activity. Rather, the effect of AMI-1 was rapidly reversible and could be demonstrated in an assay using chemically synthesized superoxide. We conclude that protein methylation does not regulate the activity of NADPH-oxidases and that AMI-1 is a potent antioxidant with a greater potency than 4,5-dihydroxy-1,3-benzenedisulfonic acid (Tiron) and 4-hydroxy-2,2,6,6-tetramethylpiperydine-1-oxyl (Tempol).