Analytical Data
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Gene name
ETFb
- Application
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Alternative Names
ETFb;Electron transfer flavoProtein subunit beta
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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
P38117
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Expression Region
1-255aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAELRVLVAVKRVIDYAVKIRVKPDRTGVV TDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALA MGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDD CNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAV VTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDP PQRTAGVKVETTEDLVAKLKEIGRI
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Molecular Weight
30 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
ETFb (Electron Transport Flavoprotein beta) is a crucial component of the mitochondrial electron transport chain, playing a significant role in cellular respiration and energy production. Research on ETFb recombinant proteins has gained momentum due to their potential applications in metabolic pathways and therapeutic interventions. Mutations or dysfunctions in ETFb can lead to various metabolic disorders, including certain types of mitochondrial myopathies. Furthermore, understanding ETFb's structure and function can facilitate the development of targeted therapies for such conditions. Recent advancements in protein engineering and recombinant DNA technology have enabled scientists to produce ETFb in microbial systems, allowing for detailed biochemical studies and high-throughput screening of potential drug candidates. The study of ETFb not only enhances our understanding of mitochondrial biology but also provides insights into broader metabolic processes, making it a focal point in both basic research and clinical investigations aimed at improving the treatment of metabolic diseases.











