Recombinant protein of human eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa (EIF2S1), 20 µg

Recombinant protein of human e

ukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa (EIF2S1), 20 µg
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  • ¥2900
  • OriGene已认证
  • TP300368
  • 2025年08月13日
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    gene_symbol:elF2 alpha
    Description:Recombinant protein of human eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa (EIF2S1), 20 µg
    Accn:NM_004094
    Unipro ID:P05198
    Synonyms:EIF-2; EIF-2A; EIF-2alpha; EIF2; EIF2A
    Species:Human
    Amount:20 ug
    Delivery time:4周
    Expression sequence:>RC200368 protein sequence Red=Cloning site Green=Tags(s) MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNEC VVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDD KYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKE ALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTD TDETELARQMERLERENAEVDGDDDAEEMEAKAED TRTRPLEQKLISEEDLAANDILDYKDDDDKV
    Tags:C-Myc/DDK
    PredictedMW:35.9 kDa
    Buffer:25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
    Stability:Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
    Bioactivity
    Purity:> 80% as determined by SDS-PAGE and Coomassie blue staining
    Concentration:>0.05 µg/µL as determined by microplate BCA method
    Preparation:Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
    Endotoxin
    Shipping
    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]).[supplied by OMIM, Feb 2010]

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