SRP0392
PRMT7 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)
别名:
Histone-arginine N-methyltransferase7, protein arginine N-methyltransferase 7
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关于此项目
NACRES:
NA.32
UNSPSC Code:
12352200
Assay:
≥80% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
产品名称
PRMT7 human, recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
79 kDa
packaging
pkg of 20 μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRMT7(54496)
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
General description
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.
Physical form
Formulated in 80 ug/mL FLAG peptide, 20% glycerol, and 3 mM DTT.
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Tiago R Ferreira et al.
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
Mamta Verma et al.
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
Jin-Hyung Lee et al.
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
Tina Branscombe Miranda et al.
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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