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安全信息

SRP0392

Sigma-Aldrich

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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About This Item

UNSPSC代码:
12352200
NACRES:
NA.32

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

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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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