生物来源
human
重组
expressed in baculovirus infected Sf9 cells
检测方案
≥80% (SDS-PAGE)
形式
aqueous solution
分子量
79 kDa
包装
pkg of 20 μg
NCBI登记号
UniProt登记号
运输
dry ice
储存温度
−70°C
基因信息
human ... PRMT7(54496)
一般描述
Human PRMT7 (protein arginine methyltransferase 7), (GenBank Accession No. NM_019023), amino acids 2-692 (end) with N-terminal FLAG-tag, MW=79 kDa, expressed in Sf9 cells using a Baculovirus expression system.
应用
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
外形
Formulated in 80 ug/mL FLAG peptide, 20% glycerol, and 3 mM DTT.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
Nucleic acids research, 48(10), 5511-5526 (2020-05-05)
RNA binding proteins (RBPs) are the primary gene regulators in kinetoplastids as transcriptional control is nearly absent, making Leishmania an exceptional model for investigating methylation of non-histone substrates. Arginine methylation is an evolutionarily conserved protein modification catalyzed by Protein aRginine
The Journal of biological chemistry, 280(5), 3656-3664 (2004-10-21)
The cDNA for PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned and expressed in Escherichia coli and mammalian cells. Immunopurified PRMT7 actively methylated histones, myelin basic protein, a fragment of human fibrillarin (GAR) and spliceosomal protein SmB. Amino
Journal of molecular biology, 429(15), 2278-2289 (2017-06-08)
Protein arginine methyltransferase 7 (PRMT7) catalyzes the introduction of monomethylation marks at the arginine residues of substrate proteins. PRMT7 plays important roles in the regulation of gene expression, splicing, DNA damage, paternal imprinting, cancer and metastasis. However, little is known
The Journal of biological chemistry, 279(22), 22902-22907 (2004-03-27)
We have identified a mammalian arginine N-methyltransferase, PRMT7, that can catalyze the formation of omega-NG-monomethylarginine in peptides. This protein is encoded by a gene on human chromosome 16q22.1 (human locus AK001502). We expressed a full-length human cDNA construct in Escherichia
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