Analytical Data
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Gene name
EIF4EBP1
- Application
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Alternative Names
EIF4EBP1；EIF4EL1；EIF4F;Eukaryotic translation initiation factor 4E
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13541
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Expression Region
2-118aa
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AA Sequence
SGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI
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Molecular Weight
19.4kDa
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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, plays a crucial role in the regulation of protein synthesis and cell growth by interacting with the translation initiation factor 4E. This protein is a key player in the mTOR (mechanistic target of rapamycin) signaling pathway, which is known to influence various cellular processes, including metabolism, growth, and proliferation. Dysregulation of EIF4EBP1 has been implicated in several diseases, including cancer and neurodegenerative disorders, making it a significant target for research. Understanding the structure and function of recombinant EIF4EBP1 can provide insights into its regulatory mechanisms and interactions with other cellular proteins. Moreover, the study of its phosphorylation state, which regulates its binding affinity for EIF4E, can shed light on how cells adapt to different growth conditions and stresses. By employing recombinant DNA technology, researchers can produce EIF4EBP1 in vitro, allowing for detailed biochemical studies and potential therapeutic developments. This research not only enhances our knowledge of translation regulation but also opens avenues for developing novel strategies to manipulate protein synthesis in various disease contexts, contributing to advancements in targeted therapies.
