Analytical Data
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Gene name
ETF1
- Application
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Alternative Names
SUP45L1; ERF1; ERF; eRF1, TB3-1; RF1; Sup45(Yeast Omnipotent Suppressor 45)Homolog-Like 1; Polypeptide Chain Release Factor 1; Protein Cl1
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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 95% as determined by SDS-PAGE.
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Uniprot
P62495
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Expression Region
Ala2~Val221
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Molecular Weight
28kDa
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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
The study of ETF1 (Elongation Factor Ts-1) recombinant protein has gained significant attention due to its critical role in various cellular processes, particularly in protein synthesis and cellular stress responses. As a member of the elongation factor family, ETF1 facilitates the binding of aminoacyl-tRNA to ribosomes, thereby influencing the efficiency and accuracy of translation during protein synthesis. Research into ETF1 has highlighted its importance not only in basic cellular biology but also in the context of disease, as alterations in its expression or function can be linked to various pathologies, including cancers and neurodegenerative disorders. Furthermore, the ability to produce ETF1 as a recombinant protein opens avenues for detailed structural and functional analyses, enabling insights into its interactions and mechanisms of action. The recombinant form allows researchers to explore its potential applications in biotechnology and therapeutic developments, including the design of targeted treatments that can modulate protein synthesis in diseased cells. Overall, understanding ETF1 through recombinant protein studies enhances our knowledge of cellular dynamics and holds promise for advancing therapeutic strategies in medicine.
