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Mouse Anti-EIF2AK3 (AA 530-850) Recombinant Antibody (CBFYE-0647) (CBMAB-E1059-FY)

This product is mouse antibody that recognizes EIF2AK3. The antibody CBFYE-0647 can be used for immunoassay techniques such as: WB.
See all EIF2AK3 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYE-0647
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
This EIF2AK3 antibody is generated from a mouse immunized with a recombinant protein conjugated synthetic peptide between 530-850 amino acids from human EIF2AK3
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 530-850

Target

Full Name
Eukaryotic Translation Initiation Factor 2 Alpha Kinase 3
Introduction
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.
Entrez Gene ID
Human9451
Mouse13666
Rat29702
UniProt ID
HumanQ9NZJ5
MouseQ9Z2B5
RatQ9Z1Z1
Alternative Names
Eukaryotic Translation Initiation Factor 2 Alpha Kinase 3; PRKR-Like Endoplasmic Reticulum Kinase; Pancreatic EIF2-Alpha Kinase; EC 2.7.11.1; PERK; PEK; Eukaryotic Translation Initiation Factor 2-Alpha Kinase 3; HsPEK; WRS
Research Area
Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions. Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as unfolded protein response (UPR) and low amino acid availability (By similarity).

EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming (PubMed:33384352).

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).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Angiogenesis Source: ParkinsonsUK-UCL
Bone mineralization Source: UniProtKB
Calcium-mediated signaling Source: UniProtKB
Cellular response to amino acid starvation Source: UniProtKB
Cellular response to cold Source: UniProtKB
Cellular response to glucose starvation Source: ParkinsonsUK-UCL
Chondrocyte development Source: UniProtKB
EiF2alpha phosphorylation in response to endoplasmic reticulum stress Source: UniProtKB
Endocrine pancreas development Source: UniProtKB
Endoplasmic reticulum organization Source: UniProtKB
Endoplasmic reticulum unfolded protein response Source: UniProtKB
ER overload response Source: UniProtKB
Insulin-like growth factor receptor signaling pathway Source: UniProtKB
Negative regulation of myelination Source: UniProtKB
Negative regulation of translation Source: UniProtKB
Negative regulation of translational initiation in response to stress Source: UniProtKB
Ossification Source: UniProtKB
Peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
Positive regulation of gene expression Source: ParkinsonsUK-UCL
Positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
Positive regulation of transcription by RNA polymerase I Source: ParkinsonsUK-UCL
Positive regulation of vascular endothelial growth factor production Source: ParkinsonsUK-UCL
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Source: UniProtKB
Regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Regulation of translational initiation by eIF2 alpha phosphorylation Source: ParkinsonsUK-UCL
Response to endoplasmic reticulum stress Source: BHF-UCL
Response to manganese-induced endoplasmic reticulum stress Source: Ensembl
Skeletal system development Source: UniProtKB
Cellular Location
Endoplasmic reticulum membrane
Involvement in disease
Wolcott-Rallison syndrome (WRS):
A rare autosomal recessive disorder, characterized by permanent neonatal or early infancy insulin-dependent diabetes and, at a later age, epiphyseal dysplasia, osteoporosis, growth retardation and other multisystem manifestations, such as hepatic and renal dysfunctions, mental retardation and cardiovascular abnormalities.
Topology
Lumenal: 30-514
Helical: 515-535
Cytoplasmic: 536-1116
PTM
Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-982 on the kinase activation loop (By similarity). Autophosphorylated. Phosphorylated at Tyr-619 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity.
N-glycosylated.
ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

Saptarshi, N., Porter, L. F., & Paraoan, L. (2022). PERK/EIF2AK3 integrates endoplasmic reticulum stress-induced apoptosis, oxidative stress and autophagy responses in immortalised retinal pigment epithelial cells. Scientific Reports, 12(1), 1-13.

Gupta, A., Reddy, C., Saini, L., Yadav, J., Kumar, R., Houghton, J., ... & Dayal, D. (2021). Lissencephaly-pachygyria spectrum in a North Indian boy with Wolcott-Rallison syndrome due to homozygous deletion of exon 1 in the EIF2AK3 gene. Pediatric Endocrinology Diabetes and Metabolism, 27(1).

Rong, K., Li, X., Jiang, W., Wu, X., Xia, Q., Chen, J., & Yin, X. (2021). Alendronate alleviated femoral head necrosis and upregulated BMP2/EIF2AK3/EIF2A/ATF4 pathway in liquid nitrogen treated rats. Drug Design, Development and Therapy, 15, 1717.

Zhang, H. J., Wang, S. B., Guo, X. F., Weng, B., Lin, L., & Hao, Y. (2019). A case report of EIF2AK3-related Wolcott-Rallison syndrome and literature review. Zhongguo Dang dai er ke za zhi= Chinese Journal of Contemporary Pediatrics, 21(2), 176-179.

Fatani, T. H. (2019). EIF2AK3 novel mutation in a child with early-onset diabetes mellitus, a case report. BMC pediatrics, 19(1), 1-4.

Chaurasia, M., Gupta, S., Das, A., Dwarakanath, B. S., Simonsen, A., & Sharma, K. (2019). Radiation induces EIF2AK3/PERK and ERN1/IRE1 mediated pro-survival autophagy. Autophagy, 15(8), 1391-1406.

Wong, T. H., van der Lee, S. J., van Rooij, J. G., Meeter, L. H., Frick, P., Melhem, S., ... & van Swieten, J. C. (2019). EIF2AK3 variants in Dutch patients with Alzheimer's disease. Neurobiology of aging, 73, 229-e11.

Sanyoura, M., Letourneau, L. R., Dickens, L., Ladsaria, S. S., Greeley, S. A. W., Naylor, R. N., ... & Philipson, L. H. (2018). Case 9: EIF2AK3: Wolcott-Rallison Syndrome. In Atypical Diabetes: Pathophysiology, Clinical Presentations, and Treatment Options. American Diabetes Association.

Wang, J., Li, Y., Duan, J., Yang, M., Yu, Y., Feng, L., ... & Sun, Z. (2018). Silica nanoparticles induce autophagosome accumulation via activation of the EIF2AK3 and ATF6 UPR pathways in hepatocytes. Autophagy, 14(7), 1185-1200.

Sowers, C. R., Wang, R., Bourne, R. A., McGrath, B. C., Hu, J., Bevilacqua, S. C., ... & Cavener, D. R. (2018). The protein kinase PERK/EIF2AK3 regulates proinsulin processing not via protein synthesis but by controlling endoplasmic reticulum chaperones. Journal of Biological Chemistry, 293(14), 5134-5149.

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For research use only. Not intended for any clinical use.

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