Analytical Data
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Gene name
EIF3E
- Application
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Alternative Names
Eukaryotic translation initiation factor 3 subunit 6 Viral integration site protein INT-6 homolog eIF-3 p48
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60228
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Expression Region
1-445aa
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Molecular Weight
79.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
EIF3E (Eukaryotic Translation Initiation Factor 3 Subunit E) is a crucial component of the eukaryotic translation initiation complex, playing a significant role in the regulation of protein synthesis. Recent research has highlighted its involvement not only in the initiation of translation but also in various cellular processes, including cell growth, proliferation, and stress response. Given its pivotal function in protein synthesis, EIF3E has emerged as a potential target for therapeutic interventions, particularly in the context of cancer, where its expression is often found to be dysregulated. Studies have shown that alterations in EIF3E activity can significantly impact tumorigenesis and cancer progression, making it a subject of intense investigation. Recombination techniques for producing EIF3E protein have been developed to facilitate detailed studies of its structure, function, and interaction with other translation initiation factors. Understanding the precise mechanisms by which EIF3E influences translation and cellular dynamics may provide insights into novel therapeutic strategies and enhance our comprehension of the molecular underpinnings of diseases where protein synthesis is disrupted. Thus, the study of EIF3E recombinant protein is not only relevant for basic biology but also holds promise for advancing translational research in oncology and other fields related to protein synthesis dysregulation.
