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SRP0392

Sigma-Aldrich

PRMT7 human

recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)

Sinônimo(s):

Histone-arginine N-methyltransferase7, protein arginine N-methyltransferase 7

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About This Item

Código UNSPSC:
12352200
NACRES:
NA.32

fonte biológica

human

recombinante

expressed in baculovirus infected Sf9 cells

Ensaio

≥80% (SDS-PAGE)

forma

aqueous solution

peso molecular

79 kDa

embalagem

pkg of 20 μg

nº de adesão NCBI

NM_019023

nº de adesão UniProt

Q9NVM4

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... PRMT7(54496)

Descrição geral

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.

Aplicação

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

forma física

Formulated in 80 ug/mL FLAG peptide, 20% glycerol, and 3 mM DTT.

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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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
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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