Recombinant Human Eukaryotic translation initiation factor 2 subunit 1 (EIF2S1)

Code CSB-YP007523HU
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP007523HU
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP007523HU-B
Size Pls inquire
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP007523HU
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP007523HU
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
EIF2S1
Uniprot No.
Alternative Names
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
Species
Homo sapiens (Human)
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 ENMPIKINLI APPRYVMTTT TLERTEGLSV LSQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQM 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.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

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 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.
Gene References into Functions
  1. Our study revealed that p-eIF2alpha was upregulated in breast cancer and represented a novel predictor of prognosis in patients with triple-negative subtype. PMID: 28294178
  2. hypusine-eIF5A-facilitated translation elongation promotes arsenite-induced polysome disassembly and stress granule assembly in cells subjected to adverse environmental conditions PMID: 20376341
  3. analysis of the ER stress response in immunogenic cell death and the potential value of eIF2alpha phosphorylation as a biomarker for this clinically relevant variant of apoptosis [review] PMID: 25749194
  4. The data highlight independent interactions of PP1 and eIF2alpha with GADD34, demonstrating that GADD34 functions as a scaffold both in vitro and in cells PMID: 26095357
  5. These experiments connect embryonic stem cell growth factors to eIF2alpha phosphorylation. PMID: 26406898
  6. We identified EIF2A phosphorylation as a novel early molecular event occurring in response to NAMPT inhibition and mediating protein synthesis arrest. PMID: 26542945
  7. The results suggest that dephosphorylation of eIF2a by GADD34 plays an important role in doxorubicin resistance of MCF-7/ADR cells. PMID: 26743901
  8. The Newcastle disease virus-induced translation shutoff at late infection times was attributed to sustaining phosphorylation of eIF2a, which is mediated by continual activation of PKR and degradation of PP1. PMID: 26869028
  9. GHRH and GHRH-R loops are involved in placental choriocarcinoma cell line viability and apoptosis through Akt and eIF2a pathways. PMID: 26917260
  10. These findings suggest that phosphorylated-eIF2alpha regulates synaptic actions of nicotine in both mice and humans, and that reduced phosphorylated-eIF2alpha may enhance susceptibility to nicotine (and other drugs of abuse) during adolescence. PMID: 26928076
  11. This review consolidates current information regarding eIF2alpha phosphorylation in neurons and its impact in neurodegenerative diseases. PMID: 26994324
  12. Increased phosphorylation of eIF2alpha in chronic myeloid leukemia cells stimulates secretion of matrix modifying enzymes. PMID: 27802179
  13. Stress-resistant translation of c-Src mRNA is mediated by eIF2A. PMID: 27899592
  14. Results mechanistically link multiple forms of dystonia and put forth a new overall cellular mechanism for dystonia pathogenesis, impairment of eIF2alpha signaling, a pathway known for its roles in cellular stress responses and synaptic plasticity. PMID: 27939583
  15. Single amino acid substitution in LC-CDR1 induces Russell body phenotype that attenuates cellular protein synthesis through eIF2alpha phosphorylation and thereby downregulates IgG secretion despite operational secretory pathway traffic. PMID: 28379093
  16. These results demonstrate a previously unrecognized role of IL24 in inhibition of translation, mediated through both phosphorylation of eIF2alpha and dephosphorylation of 4E-BP1, and provide the first direct evidence for translation control of gene-specific expression by IL24 PMID: 28461326
  17. eukaryotic elongation factor 2 has a role in proliferation and invasion of lung squamous cell carcinoma PMID: 27542262
  18. a novel, positive role for PKR activation and eIF2alpha phosphorylation in human globin mRNA splicing, is reported. PMID: 28374749
  19. Data show that eIF2Balpha and eIF2Bbeta bind to adjacent surfaces on eIF2alpha-N-terminal domains (NTDs). PMID: 29036434
  20. Data show that eIF5-mimic protein (5MP) represses non-AUG translation by competing with translation initiation factor 5 (eIF5) for the Met-tRNAi-binding factor eIF2. PMID: 28981728
  21. These data indicate that PERK regulates radioresistance in oropharyngeal carcinoma through NF-kB activation-mediated phosphorylation of eIF2alpha PMID: 28418119
  22. The stem-loop of noncoding RNA 886 is structural feature not only critical for inhibiting PKR autophosphorylation, but also the phosphorylation of its cellular substrate, EIF-2alpha. PMID: 28069888
  23. overexpression of eIF5 and 5MP induces translation of ATF4. PMID: 27325740
  24. Through pathway analysis it was suggested the involvement of eIF2 and mTOR in host cells upon Chlamydia trachomatis infection. PMID: 27134121
  25. PERK-eIF2alpha-ATF4 signaling pathway mediated by endoplasmic reticulum stress involved in osteoblast differentiation of periodontal ligament cells under cyclic mechanical force. PMID: 27079961
  26. EnR stress assessed by expression of PERK and p-eIF2alpha was significantly associated with tumor infiltrating lymphocytes (TILs) in HER2-positive breast cancer. PMID: 27272779
  27. we unravels a new miRs-based mechanism that helps maintain intracellular proteostasis and promote cell survival during ER stress through upregulation of miR-30b-5p and miR-30c-5p which target eIF2alpha and thereby inhibit the p-eIF2alpha/ATF4/CHOP pro-apoptotic pathway, identifying miR-30b-5p and miR-30c-5p as potentially new targets for anti-cancer therapies. PMID: 26898246
  28. Our work suggests that OLA1 is a novel translational GTPase and plays a suppressive role in translation and cell survival, as well as cancer growth and progression. PMID: 26283179
  29. a delay in eIF2-bound GTP hydrolysis should occur. In this work, we reconstructed this situation and found that such a delay leads to the redistribution of initiation complexes in favor to downstream AUG codons. PMID: 26717981
  30. The reactive oxygen species-generating NADPH oxidase-4 (Nox4) is induced downstream of ATF4, binds to a PP1-targeting subunit GADD34 at the endoplasmic reticulum, and inhibits PP1 activity to increase eIF2alpha phosphorylation and ATF4 levels. PMID: 26742780
  31. Classical swine fever virus (CSFV) infection increased the phosphorylation of eukaryotic translation initiation factor (eIF)2alpha and its kinase PKR. The activation of PKR during CSFV infection is beneficial to the virus. PMID: 25899421
  32. eIF2alpha phosphorylation plays a role in hypoxia-induced translational attenuation PMID: 12370288
  33. phosphorylation of eIF2alpha during early brain reperfusion is carried out by PERK, these findings suggest that there is prolonged activation of the unfolded protein response in the reperfused brain. PMID: 12687390
  34. multiple domains in I-1 target cellular PP1 complexes, and I-1 has a role as a cellular regulator of eIF2alpha phosphorylation PMID: 15345721
  35. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. PMID: 16373505
  36. Our results demonstrate that Ebp1 is a new dsRNA-binding protein that acts as a cellular inhibitor of eIF2alpha phosphorylation suggesting that it could be involved in protein translation control PMID: 16631606
  37. Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis PMID: 16717090
  38. We propose that SG modeling can occur via both eIF2alpha phosphorylation-dependent and -independent pathways that target translation initiation. PMID: 16870703
  39. functional eIF2alpha played an essential role in PS-341-induced Noxa expression PMID: 16928686
  40. stress-induced phosphorylation of eIF2 alpha is directly coupled to mitochondrial apoptosis regulation via translational repression of MCL-1 PMID: 17553788
  41. the induction of the PKR/eIF2alpha cellular response may be a previously unrecognized general feature of at least the Dependovirus genus of the Parvovirinae PMID: 17715234
  42. PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation PMID: 18063576
  43. ATF4 contributes to basal ATF5 transcription, and eIF2 kinases direct the translational expression of multiple transcription regulators by a mechanism involving delayed translation reinitiation PMID: 18195013
  44. MEK functions to enhance GCN2-dependent eIF2alpha phosphorylation rather than suppressing dephosphorylation PMID: 18287093
  45. Proteasomal but not lysosomal inhibitors enhanced GADD34 stability and eukaryotic initiation factor 2alpha (eIF-2alpha) dephosphorylation, a finding consistent with GADD34's role in assembling an eIF-2alpha phosphatase PMID: 18794359
  46. GADD34 translation is regulated by a unique 5'UTR uORF mechanism to ensure proper GADD34 expression during eIF2alpha phosphorylation PMID: 19131336
  47. Strategies that maintain eIF2alpha in a hyperphosphorylated state may be a novel therapeutic approach to maximize bortezomib-induced apoptosis and reduce residual disease and recurrences in multiple myeloma. PMID: 19190324
  48. Unlike other DNA damage response-inducing agents, RITA treatment of cells induced a p53-dependent increase in phosphorylation of the eif2 alpha, requiring PKR-like endoplasmic reticulum kinase activity, and led to the downregulation of HIF-1alpha PMID: 19223463
  49. UV-induced eIF2alpha phosphorylation by activation of both PERK and GCN2 via oxidative stress and l-arginine starvation signaling pathways. PMID: 19586904
  50. PKR is activated in adenovirus-infected cells with multiple layers of regulation imposed on eIF2alpha phosphorylation by the E1B-55K/E4orf6 complex, which also regulates viral late protein synthesis PMID: 19605483

Show More

Hide All

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

HGNC: 3265

OMIM: 603907

KEGG: hsa:1965

STRING: 9606.ENSP00000256383

UniGene: Hs.151777

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X