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  • Product Name
    Phospho-PERK (Thr982) Antibody
  • Catalog No.
  • RRID
  • Source
  • Application
  • Reactivity
    Human, Mouse, Rat
  • Prediction
    Pig(90%), Bovine(90%), Horse(100%), Sheep(90%), Rabbit(90%), Dog(100%), Chicken(100%), Xenopus(100%)
  • UniProt
  • Mol.Wt
  • Concentration
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Product Information

Alternative Names:Expand▼

DKFZp781H1925; E2AK3_HUMAN; EC; 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

Predicted Reactivity:

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.





Storage Condition and Buffer:

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.

Immunogen Information


A synthesized peptide derived from human PERK around the phosphorylation site of Thr982.


>>Visit The Human Protein Atlas

Gene ID:

Gene Name:


Molecular Weight:

Observed Mol.Wt.: 125~140kD.
Predicted Mol.Wt.: 125kDa(Calculated)..

Subcellular Location:

Endoplasmic reticulum membrane.

Tissue Specificity:

Ubiquitous. A high level expression is seen in secretory tissues.


Research Background


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.

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.


ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity.

Subcellular Location:

Endoplasmic reticulum membrane>Single-pass type I membrane protein.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte

Tissue Specificity:

Ubiquitous. A high level expression is seen in secretory tissues.

Subunit Structure:

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.

Research Fields

Research Fields:

· 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.

WB Images(1)

IHC Images(1)

IF/ICC Images(2)

ELISA analysis of DF7576 showing specificity to Phospho-PERK (Thr982) Blocking Peptide peptide. Peptides concentration: 1ug/ml.
P-peptide: phospho-peptide; N-peptide: non-phospho-peptide.

Reference Citations:

1). Yao Y et al. A non-canonical pathway regulates ER stress signaling and blocks ER stress-induced apoptosis and heart failure. Nat Commun 2017 Jul 25;8(1):133 (PubMed: 28743963) [IF=12.121]

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

2). Cai Y et al. Betulinic acid chemosensitizes breast cancer by triggering ER stress-mediated apoptosis by directly targeting GRP78. Cell Death Dis 2018 May 25;9(6):636 (PubMed: 29802332) [IF=6.304]

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.

3). Li Y et al. eIF2α-CHOP-BCl-2/JNK and IRE1α-XBP1/JNK signaling promote apoptosis and inflammation and support the proliferation of Newcastle disease virus. Cell Death Dis 2019 Nov 26;10(12):891 (PubMed: 31767828) [IF=6.304]

4). Zhao YS et al. Hydrogen and Oxygen Mixture to Improve Cardiac Dysfunction and Myocardial Pathological Changes Induced by Intermittent Hypoxia in Rats. Oxid Med Cell Longev 2019 Mar 7;2019:7415212 (PubMed: 30984338) [IF=5.076]

5). Zheng Y et al. Betulinic Acid Suppresses Breast Cancer Metastasis by Targeting GRP78-Mediated Glycolysis and ER Stress Apoptotic Pathway. Oxid Med Cell Longev 2019 Aug 19;2019:8781690 (PubMed: 31531187) [IF=5.076]

6). Luo H et al. Targeting valosin-containing protein enhances the efficacy of radiation therapy in esophageal squamous cell carcinoma. Cancer Sci 2019 Nov;110(11):3464-3475 (PubMed: 31454136) [IF=4.966]

7). Liu Y et al. EndophilinA2 protects against angiotensin II-induced cardiac hypertrophy by inhibiting angiotensin II type 1 receptor trafficking in neonatal rat cardiomyocytes. J Cell Biochem 2018 Jun 20 (PubMed: 29923351) [IF=4.237]

8). Fan L;Li L;Yu X;Liang Z;Cai T;Chen Y;Xu Y;Hu T;Wu L;Lin L; et al. Jianpiyifei II Granules Suppress Apoptosis of Bronchial Epithelial Cells in Chronic Obstructive Pulmonary Disease via Inhibition of the Reactive Oxygen Species-Endoplasmic Reticulum Stress-Ca2+ Signaling Pathway. Front Pharmacol 2020 Apr 30;11:581. (PubMed: 32425799) [IF=4.225]

9). Wu X et al. Protective Effect of Patchouli Alcohol Against High-Fat Diet Induced Hepatic Steatosis by Alleviating Endoplasmic Reticulum Stress and Regulating VLDL Metabolism in Rats. Front Pharmacol 2019 Oct 1;10:1134 (PubMed: 31632274) [IF=4.225]

10). Wei J et al. Homer1a Attenuates Endoplasmic Reticulum Stress-Induced Mitochondrial Stress After Ischemic Reperfusion Injury by Inhibiting the PERK Pathway. Front Cell Neurosci 2019 Mar 15;13:101 (PubMed: 30930751) [IF=3.921]

11). Xie RJ et al. Calpain-2 activity promotes aberrant endoplasmic reticulum stress-related apoptosis in hepatocytes. World J Gastroenterol 2020 Apr 7;26(13):1450-1462 (PubMed: 32308346) [IF=3.665]

12). Li F et al. Icariin improves the cognitive function of APP/PS1 mice via suppressing endoplasmic reticulum stress. Life Sci 2019 Aug 7:116739 (PubMed: 31400352) [IF=3.647]

13). Sun ZM et al. Resveratrol protects against CIH-induced myocardial injury by targeting Nrf2 and blocking NLRP3 inflammasome activation. Life Sci 2020 Jan 27:117362 (PubMed: 31996295) [IF=3.647]

14). Zhang X et al. ER stress contributes to high-fat diet-induced decrease of thyroglobulin and hypothyroidism. Am J Physiol Endocrinol Metab 2019 Mar 1;316(3):E510-E518 (PubMed: 30620634) [IF=3.469]

15). Wang C et al. Endoplasmic Reticulum Stress Activation in Alport Syndrome Varies Between Genotype and Cell Type. Front Genet 2020 Feb 10;11:36 (PubMed: 32117450) [IF=3.258]

16). Wu K et al. Antitumor effect of ginsenoside Rg3 on gallbladder cancer by inducing endoplasmic reticulum stress-mediated apoptosis in vitro and in vivo. Oncol Lett 2018 Nov;16(5):5687-5696 (PubMed: 30344724)

17). Zhang J et al. Inhibition of the SIRT1 signaling pathway exacerbates endoplasmic reticulum stress induced by renal ischemia/reperfusion injury in type 1 diabetic rats. Mol Med Rep 2020 Feb;21(2):695-704 (PubMed: 31974604)


19). et al. Ginsenoside Rg1 protects against aging-induced renal interstitial fibrosis due to inhibition of tubular epithelial cells endoplasmic reticulum stress in SAMP8 mice.

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Catalog Number :

(Blocking peptide available as DF7576-BP)

Price/Size :

Tips: For phospho antibody, we provide phospho peptide(0.5mg) and non-phospho peptide(0.5mg).

Function :

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.

Format and storage :

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.

Precautions :

This product is for research use only. Not for use in diagnostic or therapeutic procedures.

High similarity Medium similarity Low similarity No similarity
Q9NZJ5 as Substrate
Site PTM Type Enzyme
T177 Phosphorylation
Y268 Phosphorylation
T441 Phosphorylation
S447 Phosphorylation
K452 Ubiquitination
S455 Phosphorylation
Y464 Phosphorylation
Y474 Phosphorylation
Y480 Phosphorylation
Y481 Phosphorylation
Y484 Phosphorylation
Y485 Phosphorylation
S555 Phosphorylation
T557 Phosphorylation
T561 Phosphorylation
S567 Phosphorylation
K581 Ubiquitination
Y585 Phosphorylation
Y619 Phosphorylation Q9NZJ5 (EIF2AK3)
K622 Ubiquitination
K669 Ubiquitination
S688 Phosphorylation
S694 Phosphorylation
T705 Phosphorylation
S715 Phosphorylation
S719 Phosphorylation
T802 Phosphorylation P31751 (AKT2) , P31749 (AKT1)
S803 Phosphorylation
S804 Phosphorylation
S811 Phosphorylation
S844 Phosphorylation
S845 Phosphorylation
S854 Phosphorylation
S856 Phosphorylation
T861 Phosphorylation
T862 Phosphorylation
T982 Phosphorylation
S1094 Phosphorylation
S1096 Phosphorylation
S1109 Phosphorylation
S1111 Phosphorylation
Q9NZJ5 as PTM Enzyme
Substrate Site Source
P05198 (EIF2S1) S49 Uniprot
P05198 (EIF2S1) S52 Uniprot
Q9BY44 (EIF2A) S265 Uniprot
Q9NZJ5 (EIF2AK3) Y619 Uniprot
IMPORTANT: For western blots, incubate membrane with diluted antibody in 5% w/v milk , 1X TBS, 0.1% Tween®20 at 4°C with gentle shaking, overnight.

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