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Safety Information

SRP5024

Sigma-Aldrich

EIF2AK3 (563-1115), active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

DKFZp781H1925, HRI, PEK, PERK, WRS

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.77

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

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Josef Neu
Gastroenterology and Nutrition null
Carsten Carlberg
Nutrigenomics 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
Identification of common variants influencing risk of the tauopathy Progressive Supranuclear Palsy
Gunter U
Nature Genetics (2011)
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

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