SRP0140
PRMT1 human
recombinant, expressed in E. coli, ≥50% (SDS-PAGE)
Sinónimos:
ANM1, Arginine methyltransferase 1, HMT1 hnRNP methyltransferase-like 2, HRMT1L2, Interferon receptor 1-bound protein 4 (IR1B4)
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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Nombre del producto
PRMT1 human, recombinant, expressed in E. coli, ≥50% (SDS-PAGE)
biological source
human
recombinant
expressed in E. coli
assay
≥50% (SDS-PAGE)
form
aqueous solution
mol wt
68 kDa
packaging
pkg of 50 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
>0.02 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRMT1(3276)
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
General description
Human PRMT1, GenBank Accession No. NM_001536, amino acids 2- end, with N-terminal GST tag, MW = 68 kDa, expressed in E. coli expression system.
Other Notes
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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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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