Analytical Data
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Gene name
bioB
- Application
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Alternative Names
(Biotin synthase BioB)(Adenosylmethionine-8-amino-7-oxononanoate aminotransferase BioA)(7,8-diamino-pelargonic acid aminotransferase)(DAPA AT)(DAPA aminotransferase)(7,8-diaminononanoate synthase)(DANS)(Diaminopelargonic acid synthase)
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Species
Bacteroides fragilis
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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
Q5LEY1
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Expression Region
1-748aa
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Molecular Weight
90.6 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
The study of bioB recombinant protein is rooted in the increasing importance of molecular biology and biotechnology in understanding and manipulating biological systems. BioB, an enzyme involved in the biosynthesis of riboflavin (vitamin B2), plays a crucial role in microbial metabolism and offers insights into vitamin production pathways. The recombinant expression of bioB in various host systems, such as E. coli, allows for the investigation of its structural and functional properties, essential for elucidating the biochemical mechanisms behind riboflavin synthesis. Furthermore, the production of bioB in a recombinant form facilitates its purification and characterization, enabling researchers to explore its potential applications in industrial biotechnology, including the development of biofermentation processes for riboflavin production. This research not only advances our fundamental understanding of microbial physiology but also opens avenues for designing more efficient bio-based production systems, thereby supporting sustainable practices in vitamin manufacturing. The functional analysis of bioB and its interactions with other pathways also provides valuable insights into metabolic engineering, paving the way for innovations in both health and nutrition sectors.
