Analytical Data
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Gene name
ETFa
- Application
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Alternative Names
ETFa；Electron transfer flavoProtein subunit alpha. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13804
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Expression Region
1-333aa
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AA Sequence
MFRAAAPGQLRRAASLLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK
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Molecular Weight
62.1kDa
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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
Research on ETFa (Eukaryotic Translation Factor a) recombinant proteins has gained significant attention in recent years due to their critical role in protein synthesis and cellular function within eukaryotic organisms. ETFa is a vital component of the translation machinery, facilitating the accurate recognition of initiation codons and the assembly of ribosomes during the initiation phase of protein translation. As post-translational modifications and interactions with other translation factors influence protein activity and stability, understanding ETFa structure and function is crucial for elucidating its role in various biochemical pathways. Moreover, recombinant ETFa proteins serve as valuable tools in biotechnological applications, including protein engineering and the development of novel therapeutic strategies. The ability to produce ETFa in sufficient quantities allows researchers to investigate its dynamics, interactions, and regulatory mechanisms in detail, paving the way for advancements in synthetic biology and drug development. Consequently, ongoing studies focus on optimizing the expression and purification of ETFa recombinant proteins, exploring their functional properties, and determining their potential implications in disease models. By unraveling the complex relationships between ETFa and cellular processes, researchers aim to contribute to a deeper understanding of gene expression regulation and the development of innovative solutions to combat various diseases.
