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Key Documents

SRP0141

Sigma-Aldrich

PRMT1 Active human

recombinant, expressed in baculovirus infected insect cells, ≥70% (SDS-PAGE)

Sinonimo/i:

ANM1, Arginine methyltransferase 1, HMT1 hnRNP methyltransferase-like 2, HRMT1L2, Interferon receptor 1-bound protein 4 (IR1B4)

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in baculovirus infected insect cells

Saggio

≥70% (SDS-PAGE)

Forma fisica

aqueous solution

PM

68 kDa

Confezionamento

pkg of 20 μg

Condizioni di stoccaggio

avoid repeated freeze/thaw cycles

Concentrazione

>0.02 mg/mL

N° accesso NCBI

NM_001536

N° accesso UniProt

Q99873

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... PRMT1(3276)

Descrizione generale

Human PRMT1, GenBank Accession No. NM_001536, amino acids 2-end, with N-terminal GST tag, MW = 68 kDa, expressed in a Baculovirus infected Sf9 cell expression system.

Applicazioni

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Definizione di unità

One unit is defined as the amount of enzyme required to methylate 1 pmol of substrate/min at 37°C.

Stato fisico

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 30% glycerol and 3 mM DTT.

Nota sulla preparazione

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

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Qingfei Zheng et al.
Nature communications, 11(1), 3241-3241 (2020-06-28)
Protein arginine deiminase 4 (PAD4) facilitates the post-translational citrullination of the core histones H3 and H4. While the precise epigenetic function of this modification has not been resolved, it has been shown to associate with general chromatin decompaction and compete
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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