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Biochem/physiol Actions
AMI-1 inhibits arginine, but not lysine, methyltransferase activity in vitro, while not interacting with S-adenosyl methionine (AdoMet), unlike most methyltransferase inhibitors which compete for the AdoMet binding site.
Protein arginine N-methyltransferases (PRMTs) are involved in post-translational modification implicated in protein trafficking, signal transduction, and transcriptional regulation. AMI-1 does not inhibit lysine methyltransferase activity and does not interact with S-adenosylmethionine (AdoMet), unlike most methyltransferase inhibitors which compete for the AdoMet binding site. AMI-1 can modulate nuclear receptor-regulated transcription from estrogen and androgen response elements; and is a HIV-1 reverse transcriptase inhibitor. AMI-1 is a potent antagonist of NADPH-oxidase-derived superoxide production, but acts as a direct antioxidant rather than indirectly through methyltransferase inhibition.
Features and Benefits
This compound is a featured product for Gene Regulation research. Click here to discover more featured Gene Regulation products. Learn more about bioactive small molecules for other areas of research at sigma.com/discover-bsm.
| assay | ≥98% (HPLC) |
| form | powder |
| storage condition | desiccated,protect from light |
| color | purple |
| solubility | H2O: >10 mg/mL |
| storage temp. | 2-8°C |
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