|Other Names||Eukaryotic translation initiation factor 2-alpha kinase 3, PRKR-like endoplasmic reticulum kinase, Pancreatic eIF2-alpha kinase, HsPEK, EIF2AK3, PEK, PERK|
|Format||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.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. 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.|
|Cellular Location||Endoplasmic reticulum membrane; Single-pass type I membrane protein|
|Tissue Location||Ubiquitous. A high level expression is seen in secretory tissues|
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The protein encoded by this gene phosphorylates the alphasubunit of eukaryotic translation-initiation factor 2 (EIF2),leading to its inactivation, and thus to a rapid reduction oftranslational initiation and repression of global proteinsynthesis. It is a type I membrane protein located in theendoplasmic reticulum (ER), where it is induced by ER stress causedby malfolded proteins. Mutations in this gene are associated withWolcott-Rallison syndrome.
Xu, H., et al. Toxicology 277 (1-3), 1-5 (2010) :Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Kim, K.W., et al. Oncogene 29(22):3241-3251(2010)Lee do, Y., et al. PLoS ONE 5 (5), E10489 (2010) :
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