SRP0141
PRMT1 Active human
recombinant, expressed in baculovirus infected insect cells, ≥70% (SDS-PAGE)
别名:
ANM1, Arginine methyltransferase 1, HMT1 hnRNP methyltransferase-like 2, HRMT1L2, Interferon receptor 1-bound protein 4 (IR1B4)
生物来源
human
重组
expressed in baculovirus infected insect cells
方案
≥70% (SDS-PAGE)
表单
aqueous solution
分子量
68 kDa
包装
pkg of 20 μg
储存条件
avoid repeated freeze/thaw cycles
浓度
>0.02 mg/mL
NCBI登记号
UniProt登记号
运输
dry ice
储存温度
−70°C
基因信息
human ... PRMT1(3276)
一般描述
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.
应用
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
外形
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 30% glycerol and 3 mM DTT.
制备说明
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.
其他说明
One unit is defined as the amount of enzyme required to methylate 1 pmol of substrate/min at 37°C.
法规信息
新产品
此项目有
历史批次信息供参考:
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
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
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
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