产品名称
EIF2AK3 (563-1115), active, GST tagged human, PRECISIO® Kinase, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
recombinant
expressed in E. coli
product line
PRECISIO® Kinase
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
15-21 nmol/min·mg
mol wt
~115 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... EIF2AK3(9451)
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Carsten Carlberg
Nutrigenomics null
Julie A Moreno et al.
Science translational medicine, 5(206), 206ra138-206ra138 (2013-10-11)
During prion disease, an increase in misfolded prion protein (PrP) generated by prion replication leads to sustained overactivation of the branch of the unfolded protein response (UPR) that controls the initiation of protein synthesis. This results in persistent repression of
H P Harding et al.
Molecular cell, 5(5), 897-904 (2000-07-06)
Malfolded proteins in the endoplasmic reticulum (ER) inhibit translation initiation. This response is believed to be mediated by increased phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha) and is hypothesized to reduce the work load imposed on the folding machinery during
Josef Neu
Gastroenterology and Nutrition null
Jaime D Blais et al.
Molecular and cellular biology, 24(17), 7469-7482 (2004-08-18)
Hypoxic stress results in a rapid and sustained inhibition of protein synthesis that is at least partially mediated by eukaryotic initiation factor 2alpha (eIF2alpha) phosphorylation by the endoplasmic reticulum (ER) kinase PERK. Here we show through microarray analysis of polysome-bound
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