Human Recombinant EIF2S1 protein, His Tag (V2LY-0526-LY3822)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant EIF2S1 protein, His Tag consist of Amino Acid: Full Length and predicts a molecular mass of 40 kDa.
Molecule Mass
40 kDa
Sequence
Amino Acid: Full Length
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
Batch dependent.
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
Tirs, NaCl, Glycerol
Preservative
None
Storage
Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
More Infomation

Target

Full Name
Eukaryotic Translation Initiation Factor 2 Subunit Alpha
Research Area
Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:16289705).

This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (PubMed:16289705).

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 (PubMed:16289705).

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 (PubMed:16289705).

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 (PubMed:19131336, PubMed:33384352).
Biological Process
Aging Source: Ensembl
Cellular response to amino acid starvation Source: UniProtKB
Cellular response to heat Source: Ensembl
Cellular response to oxidative stress Source: ARUK-UCL
Cellular response to UV Source: UniProtKB
Negative regulation of guanyl-nucleotide exchange factor activity Source: Ensembl
Negative regulation of translational initiation in response to stress Source: UniProtKB
PERK-mediated unfolded protein response Source: UniProtKB
Positive regulation of neuron death Source: ParkinsonsUK-UCL
Positive regulation of type B pancreatic cell apoptotic process Source: Ensembl
Protein autophosphorylation Source: Ensembl
Response to endoplasmic reticulum stress Source: UniProtKB
Response to manganese-induced endoplasmic reticulum stress Source: Ensembl
Stress granule assembly Source: ARUK-UCL
Cellular Location
Stress granule. Colocalizes with NANOS3 in the stress granules.
PTM
Phosphorylation at Ser-49 and Ser-52 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, while concomitantly initiating the preferential translation of integrated stress response (ISR)-specific mRNAs (PubMed:15207627, PubMed:18032499, PubMed:19131336). Substrate for at least 4 kinases: EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2 (By similarity). Phosphorylated; phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation and UV irradiation (By similarity).
(Microbial infection) Phosphorylation by vaccinia virus protein E3 and rotavirus A 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.
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For research use only. Not intended for any clinical use.

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