SRP0392
PRMT7 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)
Synonym(s):
Histone-arginine N-methyltransferase7, protein arginine N-methyltransferase 7
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
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)
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.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Physical form
Formulated in 80 ug/mL FLAG peptide, 20% glycerol, and 3 mM DTT.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
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
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
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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