Analytical Data
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Gene name
ETFb
- Application
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Alternative Names
ETF-B; MADD; FP585
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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
P38117
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Expression Region
Ala2~Ile255
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Molecular Weight
31kDa
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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
Related Products
Protein Description
ETFb (Eukaryotic Translation Factor b) recombinant protein has garnered significant attention in molecular biology and biotechnology due to its essential role in the eukaryotic protein synthesis process. As a crucial component of the translation machinery, ETFb facilitates the recognition of aminoacyl-tRNA and helps ensure the fidelity of protein synthesis. The study of ETFb recombinant proteins is pivotal for understanding the intricacies of translational regulation and its implications in various biological processes, including cell growth, differentiation, and stress responses. Furthermore, malfunctions or mutations in ETFb can lead to various diseases, including cancer, highlighting its importance in medical research. The ability to produce ETFb as a recombinant protein enables scientists to delve deeper into its functional mechanisms, explore interaction networks with other translation factors, and develop potential therapeutic interventions. The advances in recombinant DNA technology have made it feasible to produce ETFb in heterologous systems, paving the way for detailed structural and functional studies. This research not only enhances our fundamental understanding of protein synthesis but also opens avenues for biotechnological applications, including the development of novel protein engineering techniques and therapeutic agents targeting translation-related disorders. Thus, the study of ETFb recombinant protein stands at the intersection of basic research and applied sciences, illustrating its relevance in both academic and clinical settings.
