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Mouse Monoclonal PERK antibody [5G5] (STJ98319)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:10000
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
EIF2AK3 antibody, PEK antibody, PERK antibody,|DKFZp781H1925 antibody|E2AK3_HUMAN antibody|EC 126.96.36.199 antibody|Eif2ak3 antibody|Eukaryotic translation initiation factor 2 alpha kinase 3 antibody|Eukaryotic translation initiation factor 2-alpha kinase 3 antibody|Heme regulated EIF2 alpha kinase antibody|HRI antibody|HsPEK antibody|Pancreatic eIF2 alpha kinase antibody|Pancreatic eIF2-alpha kinase antibody|PEK antibody|PRKR like endoplasmic reticulum kinase antibody|PRKR-like endoplasmic reticulum kinase antibody|WRS antibody|Anti-PERK antibody (ab65142)
SCBT cat No: sc-377400|sc-9481|sc-7383|sc-13073|sc-9476|
PERK Monoclonal Antibody
|Catalogue No.|| |
PERK Monoclonal Antibody detects endogenous levels of PERK protein.
Purified recombinant fragment of human PERK expressed in E Coli
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:10000
PERK Antibody was tube-contained. Ascitic fluid containing 0.03% sodium azide.
PERK Antibody was purified using affinity purification.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Eukaryotic translation initiation factor 2-alpha kinase 3 antibody, PRKR-like endoplasmic reticulum kinase antibody, Pancreatic eIF2-alpha kinase antibody, HsPEK antibody
|Protein names|| |
Eukaryotic translation initiation factor 2-alpha kinase 3 , PRKR-like endoplasmic reticulum kinase , Pancreatic eIF2-alpha kinase , HsPEK
|Protein 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. / ATP + a protein = ADP + a phosphoprotein. / Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction.
|Protein tissue specificity|| |
Ubiquitous. A high level expression is seen in secretory tissues.
|Involvement in disease|| |
Wolcott-Rallison syndrome (WRS) [MIM:226980]: 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. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP. / Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. / Contains 1 protein kinase domain.
|Protein post-translational modifications|| |
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.
|Protein cellular localization|| |
Endoplasmic reticulum membrane; Single-pass type I membrane protein
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St John’s Laboratory Ltd.
|Product type|| |
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