Analytical Data
-
Gene name
EIF4EBP3
- Application
-
Alternative Names
EIF4EBP3Eukaryotic translation initiation factor 4E-binding protein 3; 4E-BP3; eIF4E-binding protein 3
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O60516
-
Expression Region
1-100aa
-
Molecular Weight
26.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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-binding protein 3 (EIF4EBP3) is a member of the EIF4EBP family, which plays a critical role in the regulation of protein synthesis and cell growth. These proteins act as essential regulators of cap-dependent translation, primarily by binding to the eukaryotic translation initiation factor 4E (eIF4E), thereby inhibiting its interaction with the mRNA cap structure. The phosphorylation state of EIF4EBP3 is crucial for its function; when phosphorylated, it dissociates from eIF4E, allowing for the initiation of translation. Research has shown that EIF4EBP3 is involved in various cellular processes, including stress response, cell proliferation, and apoptosis, making it a significant player in cancer biology and metabolic diseases. Given its regulatory role, [EIF4EBP3] has emerged as a potential therapeutic target in cancer treatment, where dysregulation of translation initiation is a hallmark of tumor progression. Furthermore, understanding its precise mechanisms of action and interactions with other cellular pathways can provide insights into innovative treatment strategies. The recombinant expression of EIF4EBP3 allows for in-depth studies of its structural and functional characteristics, potentially leading to the identification of small molecules that can modulate its function. This research is essential for elucidating the broader implications of EIF4EBP3 in health and disease, opening new avenues for therapeutic development in conditions characterized by altered protein synthesis. As such, studies involving recombinant proteins like EIF4EBP3 are pivotal in both fundamental biology and translational research, highlighting their importance in the quest for targeted therapies.











