EIF2AK3, Blocking Peptide

Eukaryotic translation initiation factor 2-alpha kinase 3; PRKR-like endoplasmic reticulum kinase; Pancreatic eIF2-alpha kinase; HsPEK; EIF2AK3; PEK; PERK

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

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Small volumes of EIF2AK3 blocking peptide 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.

Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function (By similarity).

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

Chromosomal Location of Human Ortholog: 2p12

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

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

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

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

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