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Merck
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重要文件

P0083

Sigma-Aldrich

PRMT1 from rat

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous solution

同義詞:

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

分類程式碼代碼:
51111800
NACRES:
NA.32

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

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.
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

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)


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Hsin-Wei Liao et al.
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
Xiaolan Deng et al.
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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