Recombinant Human Eukaryotic Initiation Factor 4A-I (EIF4A1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00695P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Eukaryotic Initiation Factor 4A-I (EIF4A1) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00695P
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Product Overview

Description Recombinant Human Eukaryotic Initiation Factor 4A-I (EIF4A1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P60842
Target Symbol EIF4A1
Synonyms (eIF-4A-I)(eIF4A-I)(ATP-dependent RNA helicase eIF4A-1)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence SASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI
Expression Range 2-406aa
Protein Length Full Length of Mature Protein
Mol. Weight 53.5 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.
Protein Families DEAD box helicase family, eIF4A subfamily
Database References

HGNC: 3282

OMIM: 602641

KEGG: hsa:1973

STRING: 9606.ENSP00000293831

UniGene: PMID: 28911096

  • our data demonstrate that the common effects of eIF4A1 and eIF4E on translation are mediated by the coding region and 3'UTR PMID: 27879264
  • our data identify the eIF4F complex as an important upstream regulator of TORC1, which acts via TSC2 to inactivate TORC1 upon withdrawal of amino acids PMID: 26988032
  • Our results demonstrate that miR-133a plays a pivotal role in colorectal cancer by inhibiting cell proliferation, invasion, and migration by targeting oncogenic eukaryotic translation initiation factor 4A1, which acts as a tumor suppressor and may provide a new potential therapeutic target in colorectal cancer PMID: 28466778
  • miR-1284 can function as a new regulator to reduce gastric cancer multidrug resistant cells by targeting EIF4A1. PMID: 26936591
  • Studies indicate a developing focus on targeting eukaryotic initiation factor 4A eIF4A1 and eIF4A2 as cancer therapy. PMID: 26614665
  • Immunohistochemical analysis was performed on over 3000 breast tumors to investigate the relationship among expression of eIF4A1, the helicase-modulating proteins eIF4B, eIF4E and PDCD4, and clinical outcome. PMID: 25611378
  • Collectively, these data suggested that a potential role of NS4A in antagonizing host antiviral defense is by recruiting eIF4AI and escaping the translation inhibition mediated by PKR. PMID: 25866185
  • eIF4A functions as an adenosine triphosphate-dependent processive helicase when complexed with two accessory proteins, eIF4G and eIF4B. PMID: 26113725
  • demonstrate that DAP5 associates with eIF2beta and eIF4AI to stimulate IRES-dependent translation of cellular mRNAs PMID: 25779044
  • Studies indicate that eukaryotic initiation factor 4AI (EIF4AI) undergoes large conformational transitions, while unwinding RNA hairpins. PMID: 24909782
  • Data indicate that caspase recruitment domain family, member 11 protein CARD11 has complex 5'UTRs and is sensitive to eIF4A RNA helicase inhibition. PMID: 25320244
  • Increased Expression of EIF4A1 is associated with poor response to Brachytherapy in Cervical Cancer. PMID: 24844222
  • report of an eIF4A RNA helicase-dependent mechanism of translational control that contributes to oncogenesis and underlies the anticancer effects of silvestrol and related compounds PMID: 25079319
  • The E186 residue was found to be of significance for RNA-dependent ATPase activity for eIF4AI alone and in the presence of eIF4AI-binding domains of eIF4GI, binding between eIF4AI and eIF4GI domains were also significantly influenced by mutation of E186. PMID: 24471916
  • Findings implicate phosphorylation of eIF4G1(Ser1232) by Cdk1:cyclin B and its inhibitory effects on eIF4A helicase activity in the mitotic translation initiation shift. PMID: 24248602
  • Eukaryotic translation initiation factor 4A1 (eIF4A1) is a direct target of miR-US25-2-3p. PMID: 23747307
  • Regulation of MUC1-C expression is mediated by the PI3K/AKT pathway and the eIF4A RNA helicase. PMID: 22689062
  • The results indicated that eIF4AI and eIF4AII expression are linked and that the two protein isoforms exhibit functional differences. PMID: 22589333
  • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. PMID: 21840318
  • study found Burkholderia pseudomallei BPSL1549 acted as a potent cytotoxin against eukaryotic cells; it promotes deamidation of glutamine-339 of the translation initiation factor eIF4A, abolishing its helicase activity and inhibiting translation PMID: 22076380
  • analysis of the tandem MA-3 region of Pdcd4 protein and characterization of its interactions with eIF4A and eIF4G PMID: 21454508
  • Studies indicate that eIF4A (DDX2), together with its accessory proteins eIF4B and eIF4H, is thought to act as a helicase that unwinds secondary structures in the mRNA 5' UTR. PMID: 21427765
  • EIF4A and eIF4G proteins are not responsible for the selective translation of viral mRNAs and the translational shut-off of cellular protein synthesis. PMID: 21377182
  • Inhibition of eIF4A reduced the synthesis of APP and tau. PMID: 20927385
  • These findings identify PKP1 as a regulator of translation and proliferation via modulation of eIF4A1 activity. PMID: 20156963
  • Comparative characterization of two DEAD-box RNA helicases in superfamily II: human translation-initiation factor 4A and hepatitis C virus non-structural protein 3 (NS3) helicase. PMID: 11903057
  • Results indicate that not only binding to eIF4A but also prevention of eIF4A binding to the MA-3 domain of eIF4Gc contributes to the mechanism by which Pdcd4 inhibits translation. PMID: 15082783
  • analysis of cells of eIF4GIf molecules lacking either the PABP-binding site, the eIF3-binding site, the middle domain eIF4A-binding site, or the C-terminal segment that includes the second eIF4A-binding site PMID: 17130132
  • Results report that 15d-PGJ2 blocks translation through inactivation of translational initiation factor eIF4A. PMID: 18034160
  • the PDCD4 MA3 domains compete with the eIF4G MA3 domain and RNA for eIF4A binding. PDCD4 inhibits translation initiation by displacing eIF4G and RNA from eIF4A. PMID: 18296639
  • The interaction of eIF4AI with two accessory factors, eIF4B and eIF4H, was studied. PMID: 18719248
  • Study reports the topology of the eIF4A/4G/4H helicase complex, which is built from multiple experimentally observed domain-domain contacts. PMID: 19203580
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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