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P0083

Sigma-Aldrich

PRMT1 from rat

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

Synonym(s):

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

UNSPSC Code:
51111800
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

Assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

UniProt accession no.

Q63009

shipped in

dry ice

storage temp.

−20°C

Gene Information

rat ... Prmt1(60421)

Biochem/physiol Actions

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.

Unit Definition

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

Physical form

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

Analysis Note

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).

Legal Information

IGEPAL is a registered trademark of Solvay

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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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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