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SRP0141

Sigma-Aldrich

PRMT1 Active human

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

Synonym(s):

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

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected insect cells

Assay

≥70% (SDS-PAGE)

form

aqueous solution

mol wt

68 kDa

packaging

pkg of 20 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

>0.02 mg/mL

NCBI accession no.

NM_001536

UniProt accession no.

Q99873

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PRMT1(3276)

General description

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.

Application

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

Unit Definition

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

Physical form

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

Preparation Note

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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Certificates of Analysis (COA)

Lot/Batch Number
5104160901
51041091216
5104191216

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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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