Recombinant Mouse Eukaryotic translation initiation factor 2 subunit 1 (Eif2s1)

Code CSB-YP741079MO
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Source Yeast
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Code CSB-EP741079MO
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Source E.coli
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Code CSB-EP741079MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP741079MO
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Source Baculovirus
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Code CSB-MP741079MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Eif2s1
Uniprot No.
Alternative Names
Eif2s1; Eif2aEukaryotic translation initiation factor 2 subunit 1; Eukaryotic translation initiation factor 2 subunit alpha; eIF-2-alpha; eIF-2A; eIF-2alpha
Species
Mus musculus (Mouse)
Expression Region
1-315
Target Protein Sequence
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ETMPIKINLI APPRYVMTTT TLERTEGLSV LNQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQL ERLERENAEV DGDDDAEEME AKAED
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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 a 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.
Gene References into Functions
  1. TorsinA was post-transcriptionally upregulated upon acute ER stress, suggesting a role in this response. Increased basal phosphorylation of eIF2alpha in DYT1 transgenic rats was associated with abnormal response to acute ER stress. Unbiased RNA-Seq-based transcriptomic analysis of embryonic brain tissue in heterozygous and homozygous DYT1 knockin mice confirmed presence of eIF2alpha dysregulation in the DYT1 brain. PMID: 29289717
  2. EIF2alpha regulates oligodendrocyte survival during differentiation. PMID: 27416896
  3. Data indicate that 5xFAD-related pathologies do not necessarily require hyperphosphorylation of eIF2alpha to emerge. PMID: 25883808
  4. Endoplasmic reticulum stress suppressed CReP expression in an IRE1 alpha-dependent manner, which increased eIF2alpha phosphorylation and consequently attenuated protein synthesis. PMID: 26031337
  5. eIF2alphaP acts as a molecular switch that dictates either cell survival or death by activated Akt in response to oxidative stress. PMID: 25590801
  6. aberrant phosphorylation of eukaryotic initiation factor-2a (eIF2a) may induce synaptic failure and neurodegeneration through persistent translational inhibition of global protein synthesis. PMID: 24889041
  7. Alteration of protein homeostasis and eIF2alpha phosphorylation status by pathogenic huntingtin appears to be an important cause of striatal cell death. PMID: 24594939
  8. Data indicate that prolonged endoplasmic reticulum stress inhibits protein synthesis independently of translation initiation factor eIF2alpha-P. PMID: 24648524
  9. This study demonistrated that Genetic deletion of eIF2alpha kinase PERK prevented enhanced phosphorylation of eIF2alpha and deficits in protein synthesis, synaptic plasticity and spatial memory in animal disease model of Alzheimer's disease. PMID: 23933749
  10. eIF2alpha phosphorylation in the context of the ER stress response plays a role in cell survival by counteracting the p53-mediated mitochondrial apoptosis in response to statins. PMID: 23354132
  11. eIF2a is hyperphosphorylated in the cortex of aged mice. Young human-ApoE4 targeted-replacement mice show increased p-eIF2a/eIF2a levels in both cortex and hippocampus. PMID: 22883908
  12. the induction of REDD1 gene expression was shown to require the protein kinase PERK and enhanced phosphorylation of its substrate, the alpha-subunit of eukaryotic initiation factor 2. PMID: 23000413
  13. Data show that protein kinase R as the principal kinase that mediates eukaryotic initiation factor 2alpha (eIF2alpha) phosphorylation by large RasGAP SH3-binding protein (G3BP)-induced granules. PMID: 22833567
  14. PTP1B deficiency modulates PERK-eIF2alpha phosphorylation and protein synthesis PMID: 22509299
  15. Ectopic expression of CReP restored the sensitivity of the Pten mutant hepatocytes to oxidative stress, confirming the functional significance of the downregulated CReP and upregulated phospho-eIF2alpha PMID: 22009178
  16. It was shown that urea-inducible GCN2 activation initiates the phosphorylation of eIF2alpha and the downstream increase of activating transcription factor 3. PMID: 21880833
  17. regulation of translation through eIF2alpha phosphorylation is dispensable in hematopoietic reconstitution but essential during late B-cell development. PMID: 21565905
  18. eIF2alpha phosphorylation acts in a cytoprotective manner, i.e., prevents apoptosis. PMID: 21076179
  19. Phospho-eIF2alpha level is important for BACE1 reduction to rescue cholinergic neurodegeneration and memory defects in Alzheimer's disease model. PMID: 20886088
  20. Data show that reduced phosphorylation of eIF2alpha by knocking out either PERK or GCN2 suppresses hypoxia-induced G(1) arrest and promotes apoptosis in accompany with activation of p53 signal cascade. PMID: 20072654
  21. Results demonstrate that mechanical stimulation reduces phosphorylation of eIF2alpha through inactivation of Perk. PMID: 20034494
  22. EIF2alpha phosphorylation in vaccinia virus infected cells is mediated by protein kinase R(PKR). PMID: 19846675
  23. Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses PMID: 12897138
  24. results indicate that glucose-stimulated protein synthesis in pancreatic beta-cells is regulated by the phosphorylation status of eukaryotic translation initiation factor 2(eIF2) alpha PMID: 15475356
  25. eIF2alpha phosphorylation-dependent translational control has a direct role in activating NF-kappaB during ER stress PMID: 15542827
  26. Data suggest that eIF2alpha kinases are integral to cellular stress pathways induced by proteasome inhibitors, and may be central to the efficacy of anticancer drugs that target the ubiquitin/proteasome pathway. PMID: 15684420
  27. HRI has an essential role in mediating arsenite stress-induced phosphorylation of eukaryotic translation initiation factor 2alpha, inhibition of protein synthesis, stress granule formation, and survival PMID: 15684421
  28. This analysis of eIF2alpha phosphorylation, coupled with earlier findings that the eIF4F complex is modified earlier during vesicular stomatitis virus infection, supports a temporal/kinetic model of translation control. PMID: 15705563
  29. reported that the mechanism for recognizing indispensable amino acid-deficient foods follows the conserved general control system, wherein uncharged transfer RNA induces phosphorylation of eukaryotic initiation factor 2 alpha via the GCN2 kinase PMID: 15774759
  30. phosphorylation of eIF2alpha and the consequent stress granules (SGs) assembly is important for shutoff to occur and that the localized SG disassembly PMID: 15930128
  31. regulation of mRNA translation through phosphorylation of eukaryotic initiation factor 2 (eIF2alpha) is essential to preserve the integrity of the endoplasmic reticulum and to increase insulin production to meet the demand imposed by a high-fat diet. PMID: 15980866
  32. PERK is responsible for the large increase in phosphorylated eIF2alpha and the suppression of translation early in reperfusion after transient global brain ischemia. PMID: 16000157
  33. Thus, AMPK may diminish adiposity via reduction of fat cell number through eIF2alpha-dependent translation shutdown. PMID: 16377306
  34. PKR-mediated phosphorylation of eIF2alpha contributes to inhibition of protein synthesis in the brain during status epilepticus PMID: 16492139
  35. Autophagy formation is a cellular defense mechanism against polyQ72-induced ER-stress-mediated cell death by degrading polyQ72 aggregates, with PERK/eIF2alpha phosphorylation being involved in polyQ72-induced LC3 conversion. PMID: 16794605
  36. Data show that Nck (isoforms 1 and 2) as a component of the CReP/PP1c holophosphatase complex contributes to maintain eIF2alpha in a hypophosphorylated state, and modulates translation and eIF2alpha signaling in response to ER stress. PMID: 16835242
  37. eIF2alpha phosphorylation is a major player in the cellular response to arsenite stress. PMID: 17170114
  38. These findings highlight the importance of a single phosphorylation site in eIF2alpha as a key regulator of late-long-term potentiation and long-term memory formation. PMID: 17418795
  39. induction of ER stress by MCF13 MLV infection results in an increase in the phosphorylation of the alpha-subunit of eif2, followed by elevation of c-IAP1 levels PMID: 18378896
  40. a switch from the conventional eukaryotic mode of translation initiation to the eIF2-independent mechanism occurs when eIF2 is inactivated by phosphorylation under stress conditions PMID: 18604219
  41. Study demonstrates the first link between regulation of translation and rRNA synthesis with phosphorylation of eIF2alpha, suggesting that this pathway may be broadly utilized by stresses that activate eIF2alpha kinases during cellular stress. PMID: 19470760
  42. The phosphorylation of eIF2alpha attenuates mRNA translation, prevents oxidative stress, and optimizes ER protein folding to support insulin production. PMID: 19583950
  43. Depending on the strength of ErbB2 signaling there is a differential regulation of CHOP and eIF2alpha phosphorylation. PMID: 19754954
  44. The authors show that eIF2alpha dephosphorylation by gamma(1)34.5 is crucial for viral neuroinvasion. PMID: 19759130

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Subcellular Location
Cytoplasm, Stress granule.
Protein Families
EIF-2-alpha family
Database Links
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