Analytical Data
-
Gene name
EIF3G
- Application
-
Alternative Names
Eukaryotic translation initiation factor 3
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O75821
-
Expression Region
2-320aa
-
Molecular Weight
51.5 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
EIF3G, or Eukaryotic Translation Initiation Factor 3 Subunit G, is a critical component of the eukaryotic translation initiation machinery. It plays a significant role in the recruitment of mRNA and the assembly of the ribosomal initiation complex, making it essential for the overall protein synthesis process. Research into EIF3G has garnered attention due to its involvement in various cellular processes, including cell proliferation, differentiation, and survival. Importantly, EIF3G has been implicated in several diseases, notably cancer, where its overexpression can contribute to tumor progression and metastasis. Given its role in translation and its potential as a therapeutic target, scientists have focused on characterizing recombinant EIF3G to better understand its structure and function. The study of its recombinant forms allows for detailed investigations into the mechanisms by which EIF3G interacts with other initiation factors and mRNA, facilitating the elucidation of its precise role in translation regulation. Furthermore, recombinant EIF3G can be utilized in drug discovery efforts aimed at modulating its activity, providing a valuable avenue for developing innovative cancer therapies. Understanding the biochemical properties and interactions of EIF3G through recombinant protein studies is crucial to advancing our knowledge of translation initiation and its implications in health and disease.
