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(Synonyms: Arginine N-Methyltransferase Inhibitor-1) 目录号 : GC42784

A cell permeable inhibitor of PRMTs

AMI-1 (sodium salt) Chemical Structure

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5mg
¥1,284.00
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25mg
¥5,396.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Protein arginine methyltransferases (PRMTs) post-translationally modify proteins, including histones, and in this way regulate gene expression, signal transduction, and protein-protein interactions. AMI-1 is a cell permeable inhibitor of PRMTs. It inhibits both yeast Type I arginine methyltransferase Hmt1p and human PRMT1 (IC50 = 3.0 and 8.8 μM, respectively). AMI-1 also effectively blocks the activity of PRMTs 3, 4, and 6 but not that of either SET (Sub39H1, Suv39H2, SET7) or non-SET (DOT1) lysine methyltransferases. The mechanism of inhibition of PRMTs by AMI-1 involves blocking peptide-substrate binding. AMI-1 also inhibits HIV-1 reverse transcriptase (IC50 = 5.0 μM).

Chemical Properties

Cas No. SDF
别名 Arginine N-Methyltransferase Inhibitor-1
Canonical SMILES O=C(NC1=CC(C=C(S(=O)([O-])=O)C=C2[O-])=C2C=C1)NC3=CC4=C(C([O-])=CC(S(=O)([O-])=O)=C4)C=C3.[Na+].[Na+].[Na+].[Na+]
分子式 C21H12N2O9S2•4Na 分子量 592.4
溶解度 Water: 10 mg/ml 储存条件 Store at -20°C
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储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.688 mL 8.4402 mL 16.8805 mL
5 mM 0.3376 mL 1.688 mL 3.3761 mL
10 mM 0.1688 mL 0.844 mL 1.688 mL
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Research Update

Protein arginine methylation modulates light-harvesting antenna translation in Chlamydomonas reinhardtii

Plant J 2011 Jan;65(1):119-130.PMID:21175895DOI:10.1111/j.1365-313X.2010.04406.x

Methylation of protein arginines represents an important post-translational modification mechanism, which has so far primarily been characterized in mammalian cells. In this work, we successfully identified and characterized arginine methylation as a crucial type of post-translational modification in the activity regulation of the cytosolic translation repressor protein NAB1 in the plant model organism Chlamydomonas reinhardtii. NAB1 represses the cytosolic translation of light-harvesting protein encoding mRNAs by sequestration into translationally silent messenger ribonucleoprotein complexes (mRNPs). Protein arginine methylation of NAB1 could be demonstrated by PRMT1 catalyzed methylation of recombinant NAB1 in vitro, and by immunodetection of methylated NAB1 arginines in vivo. Mass spectrometric analyses of NAB1 purified from C. reinhardtii revealed the asymmetric dimethylation of Arg90 and Arg92 within GAR motif I. Inhibition of arginine methylation by either adenosine-2'-3'-dialdehyde (AdOx) or 7,7'-carbonylbis(azanediyl)bis(4-hydroxynaphthalene-2-sulfonic acid) sodium salt hydrate (AMI-1) caused a dark-green phenotype characterized by the increased accumulation of light-harvesting complex proteins, and indicating a reduced translation repressor activity of NAB1. The extent of NAB1 arginine methylation depends on the growth conditions, with phototrophic growth causing a high methylation state and heterotrophic growth resulting in lowered methylation of the protein. In addition, we could show that NAB1 activity regulation by arginine methylation operates independently from cysteine-based redox control, which has previously been shown to control the activity of NAB1.