Millipore Sigma Vibrant Logo
Attention: We have moved. Merck Millipore products are no longer available for purchase on MerckMillipore.com.Learn More

539209 Protein Arginine N-Methyltransferase Inhibitor, AMI-1 - Calbiochem

The Protein Arginine N-Methyltransferase Inhibitor, AMI-1 controls the biological activity of Protein Arginine N-Methyltransferase. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: PRMT Inhibitor I

Primary Target: Protein arginine N-methyltransferases (PRMTs)
539209
Purchase on Sigma-Aldrich

Overview

Replacement Information

Key Spec Table

Empirical Formula
C₂₁H₁₂N₂Na₄O₉S₂

Products

Catalogue NumberPackaging Qty/Pack
539209-5MGCN Plastic ampoule 5 mg
Description
OverviewA cell-permeable, symmetrical sulfonated urea compound that acts as a potent, specific and non-AdoMet (S-adenosyl-L-methionine, SAM)-competitive inhibitor of protein arginine N-methyltransferases (PRMTs; IC50 = 8.81 µM for PRMT1 and 3.03 for yeast-RMT1p) with minimal effect on lysine methyltransferases. Inhibits nuclear receptor reporter gene activation in MCF-7 cells, and HIV-1 RT polymerase (IC50 = 5 µM).
Catalogue Number539209
Brand Family Calbiochem®
SynonymsPRMT Inhibitor I
References
ReferencesCheng, D., et al. 2004. J. Biol. Chem. 279, 23892.
Skillman, A.G., et al. 2002. Bioorg. Chem. 30, 443.
Product Information
ATP CompetitiveN
FormSolid
Hill FormulaC₂₁H₁₂N₂Na₄O₉S₂
Chemical formulaC₂₁H₁₂N₂Na₄O₉S₂
Hygroscopic Hygroscopic
ReversibleN
Structure formula ImageStructure formula Image
Quality LevelMQ100
Applications
Biological Information
Primary TargetProtein arginine N-methyltransferases (PRMTs)
Primary Target IC<sub>50</sub>8.81 µM for PRMT1 and 3.03 for yeast-RMT1p
Purity≥95% by HPLC
Physicochemical Information
Cell permeableY
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Protect from Light Protect from light
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Packaging Information
Packaged under inert gas Packaged under inert gas
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
539209-5MGCN 04055977269604

Documentation

Protein Arginine N-Methyltransferase Inhibitor, AMI-1 - Calbiochem SDS

Title

Safety Data Sheet (SDS) 

Protein Arginine N-Methyltransferase Inhibitor, AMI-1 - Calbiochem Certificates of Analysis

TitleLot Number
539209

References

Reference overview
Cheng, D., et al. 2004. J. Biol. Chem. 279, 23892.
Skillman, A.G., et al. 2002. Bioorg. Chem. 30, 443.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision10-March-2008 JSW
SynonymsPRMT Inhibitor I
DescriptionA cell-permeable, potent, specific, and non-AdoMet (S-adenosyl-L-methionine, SAM)-competitive inhibitor of protein arginine N-methyltransferases (PRMTs; IC50 = 8.81 µM for PRMT1 and 3.03 µM for yeast-RMT1p) with minimal effect on lysine methyltransferases. Inhibits nuclear receptor reporter gene activation in MCF-7 cells, and HIV-1 RT polymerase (IC50 = 5 µM).
FormSolid
Intert gas (Yes/No) Packaged under inert gas
Chemical formulaC₂₁H₁₂N₂Na₄O₉S₂
Structure formulaStructure formula
Purity≥95% by HPLC
SolubilityH₂O (50 mg/ml)
Storage Protect from light
-20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity Standard Handling
ReferencesCheng, D., et al. 2004. J. Biol. Chem. 279, 23892.
Skillman, A.G., et al. 2002. Bioorg. Chem. 30, 443.