Analytical Data
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Gene name
EIF4EBP1
- Application
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Alternative Names
4EBP1; BP-1; PHAS-I; Phosphorylated Heat And Acid-Stable Protein Regulated By Insulin 1
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q62622
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Expression Region
Ser2~Ile117
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Molecular Weight
20kDa
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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
EIF4EBP1, also known as eukaryotic translation initiation factor 4E-binding protein 1, is a pivotal regulator of protein synthesis, influencing cellular growth, proliferation, and survival. It functions primarily by binding to the eukaryotic translation initiation factor 4E (eIF4E), inhibiting its interaction with the mRNA cap structure and thereby controlling the initiation of translation. Dysregulation of EIF4EBP1 has been implicated in various diseases, including cancer, where its expression and activity can significantly affect tumorigenesis and response to treatment. Therefore, researchers have focused on elucidating the structural and functional properties of EIF4EBP1, particularly in understanding how its phosphorylation state and protein interactions dictate its role in translation regulation under different cellular conditions. Recombinant EIF4EBP1 protein studies enable detailed investigation of its biological functions, mechanisms of action, and potential as a therapeutic target. By producing and characterizing recombinant forms of EIF4EBP1, scientists aim to better understand its regulatory network, interactions with other translation factors, and its role in disease progression. This research ultimately contributes to the broader field of translational control and offers insights into developing novel strategies for treating diseases associated with impaired protein synthesis.
