Product: eIF2 alpha Antibody
Catalog: AF6087
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat, Pig
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 38kD; 36kD(Calculated).
Uniprot: P05198
RRID: AB_2834856

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Pig
Prediction:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
eIF2 alpha Antibody detects endogenous levels of total eIF2 alpha.
RRID:
AB_2834856
Cite Format: Affinity Biosciences Cat# AF6087, RRID:AB_2834856.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
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.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
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.
Sequence:
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED

Predictions

Predictions:

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.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
100
Chicken
100
Rabbit
100
Zebrafish
0
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

Function:

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.

PTMs:

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.

Family&Domains:

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.

References

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). 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.

3). 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]

4). 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

5). Deng L et al. -bambuterol and its enantiomers: Potential improvement of (R)-bambuterol in mice with colitis. Int Immunopharmacol 2022 Feb;103:108501. (PubMed: 34974400) [IF=5.714]

6). Zheng Y et al. ATP citrate lyase inhibitor triggers endoplasmic reticulum stress to induce hepatocellular carcinoma cell apoptosis via p‐eIF2α/ATF4/CHOP axis. J Cell Mol Med 2021 Feb;25(3):1468-1479. (PubMed: 33393219) [IF=5.295]

Application: WB    Species: Human    Sample: HepG2 cells

FIGURE 5 ACLY inhibitor triggers ER stress and activates p‐eIF2α/ATF4/CHOP axis in vitro. Western blot analysis of (A) ER stress‐related proteins (p‐eIF2α, eIF2α, ATF4 and CHOP) and (B) UPR signal transduction molecules (p‐PERK, PERK, p‐IRE1α, IRE1α and sXBP1) in HepG2 cells after administration of BMS‐303141. ATF4p‐eIF2α, eIF2α were activated 3 h post‐treatment; CHOP was activated 8 h post‐treatment. (* P < .05, ** P < .01 and *** P < .001, compared with control group) (C) Western blot analysis of protein expression after ATF4 knockdown. (D) Annexin V‐FITC/PI double staining was performed to determine the apoptosis rate of HepG2 cells after ATF4 knockdown via flow cytometry. (* P < .05, ** P < .01 and *** P < .001, compared with con siRNA group). All experiments were repeated 3 times

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=4.480]

Application: WB    Species: rat    Sample: cardiomyocytes

FIGURE 4| EndoA2 modulated the MAPK signaling pathway in response to ERS. G-L, Western blotting results show the expression levels of GRP78, p-PERK, p-eiF2α, ATF4, and CHOP after EndoA2 siRNA knockdown. Densitometric analyses show that EndoA2 siRNA knockdown increased the expression levels of GRP78, p-PERK, p-eiF2α, ATF4, and CHOP compared with those in the Ang II group. Transfection with neg had no significant effects (n = 5, *P < 0.05 vs control, #P < 0.05 vs AngII).

8). Ouyang R et al. FGF21 attenuates high uric acid‑induced endoplasmic reticulum stress, inflammation and vascular endothelial cell dysfunction by activating Sirt1. Mol Med Rep 2022 Jan;25(1):35. (PubMed: 34850960) [IF=3.423]

Application: WB    Species: human    Sample: HUVECs

Figure 1.| High UA levels inhibits FGF21 and Sirt1 expression levels and promotes endoplasmic reticulum stress in HUVECs.(C) Protein levels of ATF4, CHOP and p‑eIF2A/eIF2A were determined using western blotting. *P<0.05, **P<0.01 and ***P<0.001 vs. 0 mg/dl UA control group. FGF21, fibroblast growth factor 21; UA, uric acid; Sirt1,sirtuin 1; CHOP, eIF2A, eukaryotic initiation factor 2; ATF4, activating transcription factor 4; p‑, phosphorylated.

Application: WB    Species: Human    Sample: HUVECs

Figure 1. High UA levels inhibits FGF21 and Sirt1 expression levels and promotes endoplasmic reticulum stress in HUVECs. (A) mRNA expression levels of FGF21 and Sirt1 were determined using reverse transcription-quantitative PCR. (B) Protein expression levels of FGF21 and Sirt1 were determined using western blotting. (C) Protein levels of ATF4, CHOP and p-eIF2A/eIF2A were determined using western blotting. *P<0.05, **P<0.01 and ***P<0.001 vs. 0 mg/dl UA control group. FGF21, fibroblast growth factor 21; UA, uric acid; Sirt1, sirtuin 1; CHOP, eIF2A, eukaryotic initiation factor 2; ATF4, activating transcription factor 4; p-, phosphorylated.

9). Cui J et al. Downregulation of folate receptor α contributes to homocysteine‑induced human umbilical vein endothelial cell injury via activation of endoplasmic reticulum stress. Mol Med Rep 2020 Aug;22(2):1631-1638. (PubMed: 32626963) [IF=3.423]

10). Wu Y et al. Inonotus obliquus extract alleviates myocardial ischemia/reperfusion injury by suppressing endoplasmic reticulum stress. Mol Med Rep 2021 Jan;23(1):77. (PubMed: 33236154) [IF=3.423]

Application: WB    Species: rat    Sample: myocardium

Figure 6.| Expression of SIRT1, GRP78, p‑PERK, p‑eIF2α, CHOP, caspase‑12 and the mRNA levels of caspase‑12 in the myocardium. (A) Representative blots of SIRT1, GRP78, p‑PERK, p‑eIF2α, CHOP and caspase‑12. Semiquantitative analysis of (B) SIRT1, (C) GRP78, (D) p‑PERK, (E) p‑eIF2α, (F) CHOP and (G) caspase‑12.

Application: WB    Species: Rat    Sample: myocardium

Figure 6. Expression of SIRT1, GRP78, p-PERK, p-eIF2α, CHOP, caspase-12 and the mRNA levels of caspase-12 in the myocardium. (A) Representative blots of SIRT1, GRP78, p-PERK, p-eIF2α, CHOP and caspase-12. Semiquantitative analysis of (B) SIRT1, (C) GRP78, (D) p-PERK, (E) p-eIF2α, (F) CHOP and (G) caspase-12. (H) The mRNA levels of caspase-12 in the myocardium. Data are presented as the mean ± standard deviation. n=3. ##P<0.01 vs. Sham. *P<0.05 and **P<0.01 vs. MI/R. IOE, Inonotus obliquus extract; SIRT1, NAD-dependent protein deacetylase sirtuin-1; GRP78, glucose-regulated protein 78; PERK, protein kinase R-like endoplasmic reticulum kinase; eIF2α, eukaryotic translation initiation factor 2 subunit α; CHOP, C/EBP homologous protein; p, phosphorylated; MI/R, myocardial ischemia/reperfusion.

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