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生化/生理作用
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.
特点和优势
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警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Cingulate protein arginine methyltransferases 1 regulates peripheral hypersensitivity via fragile X messenger ribonucleoprotein.
Wu, et al.
Frontiers in Molecular Neuroscience, 16, 1153870-1153870 (2023)
Kirti Lathoria et al.
Autophagy, 19(7), 1997-2014 (2023-01-18)
Mutations in the Krebs cycle enzyme IDH1 (isocitrate dehydrogenase (NADP(+)) 1) are associated with better prognosis in gliomas. Though IDH1 mutant (IDH1R132H) tumors are characterized by their antiproliferative signatures maintained through hypermethylation of DNA and chromatin, mechanisms affecting cell death
Wenya Hou et al.
Developmental cell, 45(2), 262-275 (2018-04-25)
The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitations, coimmunoprecipitations, cellular reconstitutions, and in vitro
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