Analytical Data
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Gene name
EEF1g
- Application
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Alternative Names
EF1G; GIG35
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P26641
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Expression Region
Ala2~Lys437
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Molecular Weight
54kDa
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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
EEF1G, or Elongation Factor 1 gamma, is a key protein involved in the protein synthesis process, specifically in the elongation phase of translation. As a member of the elongation factor family, EEF1G plays a critical role in facilitating the delivery of aminoacyl-tRNA to the ribosome, which is essential for the assembly of polypeptide chains during protein synthesis. Research on EEF1G has garnered significant attention due to its implications in various biological processes, including cell growth, proliferation, and stress response. Moreover, abnormal expression levels of EEF1G have been linked with several diseases, including cancer and neurodegenerative disorders, suggesting that it may serve as a potential biomarker for disease progression or a target for therapeutic interventions. The recombinant expression and characterization of EEF1G allow for a deeper understanding of its functional roles and regulatory mechanisms in cells. By utilizing recombinant DNA technology, researchers can produce EEF1G in sufficient quantities for detailed biochemical studies, enabling the exploration of its interaction with other protein factors and its contribution to the translational machinery. This research not only advances the fundamental knowledge of translation but also opens avenues for the development of novel strategies in the treatment of diseases associated with EEF1G dysregulation. Ultimately, the study of EEF1G and its recombinant forms promises to enhance our understanding of cellular processes and has potential implications in the fields of biotechnology and medicine.
