Analytical Data
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Gene name
FADH1
- Application
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Alternative Names
FADH1;Oxaloacetate decarboxylase. mitochondrial
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Species
Mouse
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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
Q8R0F8
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Expression Region
1-221aa
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AA Sequence
MASTKPLSRFWEWGKNIVCVGRNYADHVKEMRSTVLSEPVLFLKPSTAYAPEGSPVLMPAYCRNLHHEVELGVLLGKRGEAIPEAAAMDYVAGYALCLDMTARDVQEECKKKGLPWTLAKSFTSSCPVSAFVPKEKIPDPHALRLWLKVNGELRQEGKTSSMIFSIPYIISYVSKIITLEEGDLILTGTPKGVGPIKENDEIEAGIDGVVSMRFKVKRSEY
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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
FADH1, a flavin adenine dinucleotide-dependent enzyme, has garnered significant attention in the field of biochemistry and molecular biology due to its crucial role in various metabolic pathways, particularly in the oxidation of fatty acids and the metabolism of carbohydrates. Research into FADH1 recombinant proteins has expanded, focusing on their structure, function, and potential applications in biotechnology and medicine. Understanding the enzymatic mechanisms involving FADH1 is essential for elucidating metabolic processes and developing strategies to manipulate these pathways for therapeutic purposes. Moreover, the recombinant expression of FADH1 in heterologous systems allows researchers to produce large quantities of the protein for detailed kinetic studies and structural analyses. These investigations aim to enhance our comprehension of the enzyme's catalytic properties, substrate specificity, and interaction with cofactors. Additionally, FADH1 holds promise for biocatalytic applications in industrial processes, such as biofuel production and the synthesis of valuable compounds. The ongoing research on FADH1 recombinant proteins not only contributes to fundamental biological knowledge but also opens avenues for innovative solutions to address challenges in energy production and metabolic diseases.
