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SRP0392

Sigma-Aldrich

PRMT7 human

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

Sinonimo/i:

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

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About This Item

Codice UNSPSC:
12352200
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in baculovirus infected Sf9 cells

Saggio

≥80% (SDS-PAGE)

Forma fisica

aqueous solution

PM

79 kDa

Confezionamento

pkg of 20 μg

N° accesso NCBI

NM_019023

N° accesso UniProt

Q9NVM4

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... PRMT7(54496)

Descrizione generale

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.

Applicazioni

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

Stato fisico

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

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°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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