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The antibody against EIF2S1 was raised in rabbit using the Peptide sequence around phosphorylation site of Serine 49 (L-L-S(p)-E-L) derived from Human eIF2a. as the immunogen. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy usi This antibody has been validated on ELISA, WB, IHC, IF.
The antibody against EIF2S1 was raised in rabbit using the Peptide sequence around phosphorylation site of Serine 49 (L-L-S(p)-E-L) derived from Human eIF2a. as the immunogen. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy usi This antibody has been validated on ELISA, WB, IHC, IF.
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Western blot analysis of extracts from Hela cells untreated or treated with starvation using eIF2a(phospho-Ser49) Antibody.
| Cat.No | ADC-43581A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | EIF2S1 |
| Form | Liquid | Species Reactivity | Human, Mouse, Rat |
| Storage Buffer | PH 7.4, 0.02% sodium azide and 50% glycerol., 150mM NaCl, Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+) | Application | ELISA, IF, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Peptide sequence around phosphorylation site of Serine 49 (L-L-S(p)-E-L) derived from Human eIF2a. | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P05198 |
Uniprot Id
P05198
Target Species
Human
Target Name
EIF2S1
Target Full Name
Eukaryotic translation initiation factor 2 subunit 1
Target 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. EIF2S1/eIF-2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to an attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming.
Target Subcellular Location
Cytoplasm, Stress granule.
Target Protein Families
EIF-2-alpha family
Target Synonyms
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
Target Background
The translation initiation factor EIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, EIF2, and GTP. EIF2 is composed of 3 nonidentical subunits, the 36-kD EIF2-alpha subunit (EIF2S1), the 38-kD EIF2-beta subunit (EIF2S2; MIM 603908), and the 52-kD EIF2-gamma subunit (EIF2S3; MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of EIF2-alpha (Ernst et al., 1987 [PubMed 2948954]).
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