Analytical Data
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Gene name
bioA
- Application
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Alternative Names
(7,8-diamino-pelargonic acid aminotransferase)(DAPA AT)(DAPA aminotransferase)(7,8-diaminononanoate synthase)(DANS)(Diaminopelargonic acid synthase)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12995
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Expression Region
1-429aa
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Molecular Weight
54.8 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
BioA is an essential enzyme involved in the biosynthesis of biotin, a vital cofactor for various metabolic processes in living organisms. The study of BioA recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. Understanding the structure and function of BioA can provide insights into biotin metabolism, which is crucial for organisms that require this nutrient for growth and development. Research has shown that biosynthesis of biotin involves complex biochemical pathways, making BioA a key target for genetic engineering and synthetic biology approaches. By producing BioA as a recombinant protein, researchers aim to elucidate its mechanism of action, enhance its activity, or even engineer it for improved stability and specificity. This enables the development of novel biocatalysts or diagnostic tools and contributes to a deeper understanding of metabolic disorders related to biotin deficiency. Moreover, studying BioA and its interactions with substrates could lead to innovative strategies for designing inhibitors that may serve as potential therapeutic agents. Overall, the investigation of BioA recombinant proteins not only advances fundamental science but also opens up new avenues for practical applications in health and industry.
