Product: Phospho-eIF2 alpha (Ser51)[Ser52] Antibody
Catalog: AF3087
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 38kD; 36kD(Calculated).
Uniprot: P05198
RRID: AB_2834524

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

WB 1:500-1:2000, IHC 1:50-1:500, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Phospho-eIF2 alpha (Ser51) Antibody detects endogenous levels of eIF2 alpha only when phosphorylated at Ser52, which site historically referenced as Ser51.
Cite Format: Affinity Biosciences Cat# AF3087, RRID:AB_2834524.
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
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.


EIF 2 alpha; EIF 2; EIF 2A; EIF 2alpha; eIF-2-alpha; eIF-2A; EIF-2alpha; EIF2 alpha; EIF2; EIF2A; EIF2S1; Eukaryotic translation initiation factor 2 subunit 1 alpha 35kDa; Eukaryotic translation initiation factor 2 subunit 1 alpha; Eukaryotic translation initiation factor 2 subunit 1; Eukaryotic translation initiation factor 2 subunit alpha; IF2A_HUMAN;


eIF2A a translation initiation factor that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40s ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P05198 As Substrate

Site PTM Type Enzyme
S5 Phosphorylation
K12 Ubiquitination
S26 Phosphorylation
S49 Phosphorylation Q9NZJ5 (EIF2AK3) , Q9BQI3 (EIF2AK1) , P19525 (EIF2AK2) , Q75MR0 (HRI)
S52 Phosphorylation B4DS64 (PRKRIR) , P51812 (RPS6KA3) , P19525 (EIF2AK2) , P28482 (MAPK1) , Q75MR0 (HRI) , Q9BQI3 (EIF2AK1) , Q9NZJ5 (EIF2AK3) , Q05655 (PRKCD) , Q16539 (MAPK14) , Q9P2K8 (EIF2AK4)
S58 Phosphorylation
K61 Ubiquitination
K80 Ubiquitination
Y82 Phosphorylation
S86 Phosphorylation
K87 Ubiquitination
S91 Phosphorylation
K97 Ubiquitination
K101 Acetylation
K101 Ubiquitination
K104 Ubiquitination
K106 Ubiquitination
S110 Phosphorylation
K123 Ubiquitination
R133 Methylation
K141 Acetylation
K141 Ubiquitination
K143 Acetylation
K143 Ubiquitination
Y147 Phosphorylation
Y150 Phosphorylation
K154 Methylation
K154 Ubiquitination
S158 Phosphorylation
T185 Phosphorylation
K190 Ubiquitination
Y200 Phosphorylation
Y202 Phosphorylation
K209 Ubiquitination
S219 Phosphorylation
K226 Ubiquitination
Y235 Phosphorylation
T245 Phosphorylation
K259 Ubiquitination
K265 Ubiquitination
R266 Methylation
K276 Ubiquitination
T279 Phosphorylation
T281 Phosphorylation
T284 Phosphorylation
K312 Ubiquitination

Research Backgrounds


Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.


Substrate for at least 4 kinases: EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation. Phosphorylated; phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation and UV irradiation (By similarity).

Subcellular Location:

Cytoplasm>Stress granule.
Note: Colocalizes with NANOS3 in the stress granules.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Heterotrimer composed of an alpha, a beta and a gamma chain. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interaction with METAP2 protects EIF2S1 from inhibitory phosphorylation (By similarity). Interacts with ABCF1 isoform 2. Associates with ribosomes. Interacts with DDX3X in an RNA-independent manner.


Belongs to the eIF-2-alpha family.

Research Fields

· Cellular Processes > Transport and catabolism > Autophagy - animal.   (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Genetic Information Processing > Translation > RNA transport.

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· 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 > Herpes simplex infection.


1). Li X et al. Upregulation of BCL-2 by acridone derivative through gene promoter i-motif for alleviating liver damage of NAFLD/NASH. Nucleic Acids Res 2020 Sep 4;48(15):8255-8268. (PubMed: 32710621) [IF=19.160]

Application: WB    Species: mouse    Sample: liver

Figure 7. Effect of A22 on ameliorating apoptosis, ER stress, inflammation, metabolic syndrome, and fibrogenesis in HF diet-fed mice. (A) Effect of A22 on BCL-2 gene transcription. (B) Effect of A22 on BAX gene transcription. (C) Effect of A22 on expressions of apoptosis-related proteins in liver. The extracted proteins from the liver were immunoblotted with specific antibodies, and quantified based on the loading control of ACTIN. (D) Effect of A22 on ER stress. The UPR proteins (IRE-1, PERK, elF-2 and CHOP) were analyzed by using western Blot. (E) Effect of A22 on expressions of inflammatory factors. (F) Effect of A22 on expressions of fibrogenic proteins.

2). Wen H et al. A marine-derived small molecule induces immunogenic cell death against triple-negative breast cancer through ER stress-CHOP pathway. Int J Biol Sci 2022 Apr 11;18(7):2898-2913. (PubMed: 35541893) [IF=10.750]

3). Wen H et al. A marine-derived small molecule induces immunogenic cell death against triple-negative breast cancer through ER stress-CHOP pathway. Int J Biol Sci 2022 Apr 11;18(7):2898-2913. (PubMed: 35541893) [IF=10.750]

4). 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=9.685]

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.

5). 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=7.310]

Application: WB    Species: rat    Sample: endoplasmic reticulum?

Figure 3: |The H2-O2 mixture-induced inhibition of ER stress caused by CIH for 35 d: (a) the ER stress markers GRP 78, caspase 12, and CHOP protein expressions; (b–d) the ratios of p-PERK, p-eIF2α/eIF2α, and p-IRE 1/IRE 1 in the left ventricle

6). Jin H et al. Microcystin-leucine arginine induced the apoptosis of GnRH neurons by activating the endoplasmic reticulum stress resulting in a decrease of serum testosterone level in mice. Ecotoxicol Environ Saf 2021 Jan 15;208:111748. (PubMed: 33396074) [IF=7.129]

7). 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=6.780]

Application: WB    Species: mouse    Sample: hippocampus

Fig.6 |Effects of ICA on the PERK signaling in the hippocampus of APP/PS1 mice. The phosphorylation of PERK and eIF2α, as well ATF4 and CHOP proteins expression were increased in APP/PS1 mice, ICA treatment significantly decreased their levels. (A, B) Immunoblots of PERK, p-PERK, eIF2α, p-eIF2α, ATF4 and CHOP.

8). Fei H et al. CTRP1 Attenuates Cerebral Ischemia/Reperfusion Injury via the PERK Signaling Pathway. Front Cell Dev Biol 2021 Aug 4;9:700854. (PubMed: 34422821) [IF=6.081]

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=5.810]

Application: WB    Species: rat    Sample: liver

FIGURE 5 | PA treatment attenuated HFD-induced VLDLR expression in rats. (A) Representative immunoreactive bands of eIF2α, p-eIF2α, ATF4, and VLDLR

10). Wang H et al. The novel curcumin derivative 1g induces mitochondrial and ER-stress-dependent apoptosis in colon cancer cells by induction of ROS production. Front Oncol 2021 Jun 14;11:644197. (PubMed: 34195069) [IF=5.738]

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