Eukaryotic Translation Initiation Factor 2 Alpha Kinase 3, Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures.

Host: E Coli
Source: Prokaryotic expression

>90%

Supplied as lyophilized form in PBS, pH7.4, containing 5% trehalose, 0.01% sarcosyl.

Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. The loss of this protein is less than 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customer’s specifications, please inquire.

Small volumes of EIF2aK3 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

125,216 Da

eukaryotic translation initiation factor 2-alpha kinase 3

eukaryotic translation initiation factor 2-alpha kinase 3

Eukaryotic translation initiation factor 2-alpha kinase 3

PEK; PERK; HsPEK  [Similar Products]

E2AK3_HUMAN

The protein encoded by this gene phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2, leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. This protein is thought to modulate mitochondrial function. It is a type I membrane protein located in the endoplasmic reticulum (ER), where it is induced by ER stress caused by malfolded proteins. Mutations in this gene are associated with Wolcott-Rallison syndrome. [provided by RefSeq, Sep 2015]

PERK: a transmembrane protein kinase of the PEK family resident in the endoplasmic reticulum (ER) membrane and is linked to insulin processing. Couples ER stress to translation inhibition. Stress induces autophosphorylation of its kinase domain and increases its activity. Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. A critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin d1. Forms dimers with BiP in resting cells. Oligomerizes in ER-stressed cells. LOF mutations cause Wolcott-Rallison syndrome (WRS), characterized by insulin-dependent diabetes in early infancy and, later, multiple system abnormalities. Neuronal death in Alzheimer?s and Parkinson?s diseases is thought to be due to ER stress and has been weakly linked to PEK.

Protein type: Protein kinase, Other; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Membrane protein, integral; Translation; EC 2.7.11.1; Other group; PEK family; PEK subfamily

Chromosomal Location of Human Ortholog: 2p12

Cellular Component: endoplasmic reticulum membrane; membrane; endoplasmic reticulum; cytoplasm; integral to endoplasmic reticulum membrane

Molecular Function: protein serine/threonine kinase activity; identical protein binding; protein binding; enzyme binding; protein phosphatase binding; ATP binding; eukaryotic translation initiation factor 2alpha kinase activity; protein kinase activity

Biological Process: lactation; fat cell differentiation; translation; positive regulation of protein binding; protein amino acid autophosphorylation; protein amino acid phosphorylation; bone mineralization; positive regulation of transcription from RNA polymerase I promoter; cellular response to glucose starvation; regulation of fatty acid metabolic process; angiogenesis; skeletal development; protein homooligomerization; ER overload response; endoplasmic reticulum organization and biogenesis; caspase activation; ossification; negative regulation of myelination; unfolded protein response; calcium-mediated signaling; chondrocyte development; SREBP-mediated signaling pathway; endocrine pancreas development; peptidyl-serine phosphorylation; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; insulin-like growth factor receptor signaling pathway; insulin secretion; negative regulation of translation; negative regulation of translation initiation in response to stress; negative regulation of apoptosis

Disease: Epiphyseal Dysplasia, Multiple, With Early-onset Diabetes Mellitus

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