Analytical Data
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Gene name
EIF4E1
- Application
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Alternative Names
CUM1
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O23252
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Expression Region
S59-A235
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Protein Length
Partial
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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
Related Products
Protein Description
Eukaryotic translation initiation factor 4E (eIF4E) is a critical component of the translation initiation machinery, specifically involved in the recognition and binding of the 5' cap structure of mRNA. It plays a vital role in regulating gene expression at the translational level and is known to influence cellular processes such as growth, proliferation, and apoptosis. Dysregulation of eIF4E has been implicated in various human diseases, including cancer, where elevated levels are often associated with poor prognosis due to enhanced protein synthesis of oncogenes. The recombinant expression of eIF4E1, its principal variant, allows for detailed studies of its functional properties, interaction with other translation factors, and its role in pathological conditions. Utilizing recombinant technology to produce eIF4E1 can facilitate the understanding of its mechanisms in translation control and potentially uncover novel therapeutic targets. Furthermore, investigating the structural and functional dynamics of eIF4E1 provides insights into the modulation of translation under various physiological and stress conditions, establishing a foundation for future research aimed at the development of eIF4E-targeted therapies. As such, the study of eIF4E1 recombinant protein serves not only academic interests but also holds significant promise for clinical applications in modulating translation-related diseases.
