P0083
PRMT1 from rat
recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous solution
别名:
HMT1-like 2, HRMT1L2, Heterogenious nuclear ribonucleoprotein methyltransferase 1-like 2, IR1B4, Interferon receptor 1-bound protein 4, Protein arginine N-methyl transferase 1
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About This Item
重組細胞
expressed in E. coli
品質等級
化驗
≥90% (SDS-PAGE)
形狀
buffered aqueous solution
UniProt登錄號
運輸包裝
dry ice
儲存溫度
−20°C
基因資訊
rat ... Prmt1(60421)
生化/生理作用
Methyl transferases catalyze the addition of methyl groups to nitrogen, carbon, sulfur, and oxygen atoms of small molecules, lipids, proteins, and nucleic acids. Eight mammalian protein arginine methyltransferases (PRMT) have been identified. PRMT1 is the predominant member of the methyl transferases, which catalyzes the protein arginine N-methylation reactions. PRMT1 is implicated in various cellular processes including: transcription, RNA processing, and signal transduction.
單位定義
The specific activity is ≥ 0.1 nmol/mgP/min. measured by 3H-AdoMet incorporation into histone for 30 minues at 30 °C.
外觀
Solution of 50 mM Tris, pH 7.6, 5 mM DTT, 0.2% IGEPAL® CA-630, 150 mM NaCl, and 30% glycerol (w/v).
分析報告
The N-methyltransferase activity is determined by detecting the level of radiolabel transfer from 3H-AdoMet (Methyl donor) to histone (Cat. No. H4380), which is arginine rich (methyl acceptor).
法律資訊
IGEPAL is a registered trademark of Solvay
相關產品
产品编号
说明
价格
儲存類別代碼
10 - Combustible liquids
水污染物質分類(WGK)
WGK 1
閃點(°F)
Not applicable
閃點(°C)
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
The Journal of clinical investigation, 125(12), 4529-4543 (2015-11-17)
Posttranslational modifications to the intracellular domain of the EGFR are known to regulate EGFR functions; however, modifications to the extracellular domain and their effects remain relatively unexplored. Here, we determined that methylation at R198 and R200 of the EGFR extracellular
Oncotarget, 6(34), 35173-35182 (2015-10-16)
Inner centromere protein (INCENP) is a part of a protein complex known as the chromosomal passenger complex (CPC) that is essential for correcting non-bipolar chromosome attachments and for cytokinesis. We here demonstrate that a protein arginine methyltransferase PRMT1, which are
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