Analytical Data
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Gene name
EIF4G1
- Application
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Alternative Names
p220
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Species
Human
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Source
E. coli
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Tag
N- His-B2M-JD & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q04637
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Expression Region
1250-1599aa
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Molecular Weight
46.6 kDa
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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
EIF4G1, or eukaryotic translation initiation factor 4 gamma 1, plays a crucial role in the initiation of translation, a fundamental process for protein synthesis in eukaryotic cells. It acts as a scaffold that interacts with various components of the translation machinery, including the ribosome, mRNA, and other initiation factors. The importance of EIF4G1 is underscored by its involvement in multiple cellular processes, including cell proliferation, differentiation, and response to stress. Dysregulation of EIF4G1 has been implicated in various diseases, particularly cancers, where its expression levels can be significantly altered, leading to enhanced proliferation of tumor cells. Researchers have turned to the study of recombinant EIF4G1 proteins to better understand its complex interactions and functions. By using techniques such as molecular cloning, expression, and purification, scientists are able to produce and analyze these proteins in vitro. This research aims to decipher the mechanisms by which EIF4G1 contributes to translation regulation and how its aberrant activity may lead to disease states. Understanding EIF4G1's structure and function could provide insights into novel therapeutic targets, as modulating its activity might offer new avenues for tackling translation-related diseases. Thus, the study of recombinant EIF4G1 is not only vital for basic biology but also holds potential significance for the development of innovative strategies in disease treatment and prevention.
