DKFZp781H1925; E2AK3_HUMAN; EC 126.96.36.199; Eif2ak3; Eukaryotic translation initiation factor 2 alpha kinase 3; Eukaryotic translation initiation factor 2-alpha kinase 3; Heme regulated EIF2 alpha kinase; HRI; HsPEK; Pancreatic eIF2 alpha kinase; Pancreatic eIF2-alpha kinase; PEK; PRKR like endoplasmic reticulum kinase; PRKR-like endoplasmic reticulum kinase; WRS;
WB 1:1000-3000, IHC 1:50-1:200, IF/ICC 1:100-500, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat
Pig(90%), Bovine(90%), Horse(100%), Sheep(90%), Rabbit(90%), Dog(100%), Chicken(100%), Xenopus(100%)
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Phospho-PERK (Thr982) Antibody detects endogenous levels of PERK only when phosphorylated at Thr982.
Please cite this product as: Affinity Biosciences Cat# DF7576, RRID:AB_2833024.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
A synthesized peptide derived from human PERK around the phosphorylation site of Thr982.
Observed Mol.Wt.: 125~140kD.
Predicted Mol.Wt.: 125kDa(Calculated)..
Endoplasmic reticulum membrane.
Ubiquitous. A high level expression is seen in secretory tissues.
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.
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.
ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.
Endoplasmic reticulum membrane>Single-pass type I membrane protein.
Ubiquitous. A high level expression is seen in secretory tissues.
Forms dimers with HSPA5/BIP in resting cells (By similarity). Oligomerizes in ER-stressed cells (By similarity). Interacts with DNAJC3 and MFN2 (By similarity). Interacts with TMEM33 (PubMed:26268696). Interacts with PDIA6 (PubMed:24508390).
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.
· Cellular Processes > Cell growth and death > Apoptosis.(View pathway)
· Cellular Processes > Transport and catabolism > Autophagy - animal.(View pathway)
· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.(View pathway)
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Infectious diseases: Viral > Hepatitis C.
· Human Diseases > Infectious diseases: Viral > Measles.
· Human Diseases > Infectious diseases: Viral > Influenza A.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).
· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.
Application: WB Species:rat; Sample:Not available
Fig. 4 AGGF1 protein therapy regulates ER stress signaling and apoptosis. TAC or sham mice were treated with AGGF1 or PBS (left) and characterized (n = 6/group, **P < 0.01). a AGGF1 regulates TAC-induced ER stress signaling in mice. Protein extracts from heart samples were used for western blot analysis for ER stress signaling markers (n = 6/group, **P < 0.01). b Representative images for immunostaining analysis of heart sections for KDEL receptor-positive cells. Scale bar, 50 μm. c Representative images of TUNEL staining for apoptosis from heart sections. Scale bar, 50 μm. d Western blot analysis for apoptosis markers in heart tissues (n = 6/group, **P < 0.01). e Real-time RT-PCR analyses for ATF4, ATF6, CHOP, Ero1α, and GADD34 in heart tissues from TAC or sham mice treated with AGGF1 or PBS (n = 5/group, **P < 0.01). f Western blot analysis showing that AGGF1 protein treatment increased the levels of ATF4 and p-eIF2α, and decreased the level of sXBP1 in H9C2 cells treated with ISO for 48 h. The effects of AGGF1 were abolished by overexpression of CHOP by transient transfection of an expression plasmid as compared with the empty vector. No effect was observed for p-PERK (n = 3/group, **P < 0.01, N.S., Non-significant). g Real-time RT-PCR analysis for GADD34 in H9C2 cells transfected with an expression plasmid for CHOP or empty vector control, and then treated with ISO in combination with AGGF1 or PBS for 48 h (n = 3/group, *P < 0.05). Data are shown as the mean ± s.d. from at least three independent experiments. For a–e, statistical analysis was carried out by a Student’s two-tailed t-test; for f, g, statistical analysis was carried out by one-way analysis of variance
Application: WB Species:human; Sample:MCF-7,MDA-MB-231
Fig. 5 BA triggers breast cancer cells apoptosis via ER stress-mediated pathway. a MCF-7 and MDA-MB-231 cells were treated with the indicated concentrations of BA for 24 h, and the protein levels of ER stress-associated signals were stimulated by BA in a dose-dependent manner, including GRP78, p-PERK/PERK, p-eIF2α/eIF2α, CHOP, and caspase-12. b MCF-7 and MDA-MB-231 cells were treated with BA alone or in combination with taxol for 24 h, the expression levels of GRP78, p-PERK/PERK, p-eIF2α/eIF2α, CHOP, and caspase-12 were also significantly upregulated following drug administration, especially in the co-treatment group, indicating the ER stress-mediated apoptosis pathway was aggravatedly activated by drug combination.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
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 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|T802||Phosphorylation||P31751 (AKT2) , P31749 (AKT1)||Uniprot|