P0083
PRMT1 from rat
recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous solution
동의어(들):
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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모든 사진(1)
About This Item
UNSPSC 코드:
51111800
NACRES:
NA.32
재조합
expressed in E. coli
Quality Level
분석
≥90% (SDS-PAGE)
양식
buffered aqueous solution
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−20°C
유전자 정보
rat ... Prmt1(60421)
생화학적/생리학적 작용
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.
단위 정의
The specific activity is ≥ 0.1 nmol/mgP/min. measured by 3H-AdoMet incorporation into histone for 30 minues at 30 °C.
물리적 형태
Solution of 50 mM Tris, pH 7.6, 5 mM DTT, 0.2% IGEPAL® CA-630, 150 mM NaCl, and 30% glycerol (w/v).
분석 메모
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).
법적 정보
IGEPAL is a registered trademark of Solvay
관련 제품
제품 번호
설명
가격
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
가장 최신 버전 중 하나를 선택하세요:
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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