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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.

FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: PRMT Inhibitor I

Primary Target: Protein arginine N-methyltransferases (PRMTs)
539209
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Aperçu

Replacement Information

Tableau de caractéristiques principal

Empirical Formula
C₂₁H₁₂N₂Na₄O₉S₂

Products

RéférenceConditionnement Qté
539209-5MG Ampoule plast. 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
Référence GTIN
539209-5MG 04055977269604

Documentation

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

Titre

Fiche de données de sécurité des matériaux (FDS) 

Protein Arginine N-Methyltransferase Inhibitor, AMI-1 - Calbiochem Certificats d'analyse

TitreNuméro de lot
539209

Références bibliographiques

Aperçu de la référence bibliographique
Cheng, D., et al. 2004. J. Biol. Chem. 279, 23892.
Skillman, A.G., et al. 2002. Bioorg. Chem. 30, 443.
Fiche technique

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.