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Merck
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Documenti fondamentali

P0083

Sigma-Aldrich

PRMT1 from rat

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

Sinonimo/i:

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

Codice UNSPSC:
51111800
NACRES:
NA.32

Ricombinante

expressed in E. coli

Livello qualitativo

Saggio

≥90% (SDS-PAGE)

Stato

buffered aqueous solution

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

Informazioni sul gene

Azioni biochim/fisiol

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.

Definizione di unità

The specific activity is ≥ 0.1 nmol/mgP/min. measured by 3H-AdoMet incorporation into histone for 30 minues at 30 °C.

Stato fisico

Solution of 50 mM Tris, pH 7.6, 5 mM DTT, 0.2% IGEPAL® CA-630, 150 mM NaCl, and 30% glycerol (w/v).

Risultati analitici

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).

Note legali

IGEPAL is a registered trademark of Solvay

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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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