Analytical Data
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Gene name
birA
- Application
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Alternative Names
Bifunctional ligase/repressor BirA; Biotin--[acetyl-CoA-carboxylase] ligase; 6.3.4.15; Biotin--protein ligase; Biotin-[acetyl-CoA carboxylase] synthetase; birA; Bacillus subtilis (strain 168); DNA-binding; Ligase; Repressor
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Species
Others
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0CI75
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Expression Region
G66-G325, R124G, E323S, G325R
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Protein Length
Partial
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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 birA gene, originally identified in Escherichia coli, encodes for a biotin protein ligase, which plays a crucial role in the biotinylation of proteins by catalyzing the covalent attachment of biotin to specific lysine residues. This function is essential for a variety of cellular processes, including carboxylation reactions that are vital for fatty acid synthesis and gluconeogenesis. The study of birA and its resultant recombinant protein has gained significant attention due to its potential applications in biochemistry and molecular biology. Researchers have utilized the birA system to develop innovative biotinylation techniques, enabling the labeling of proteins with biotin, which in turn allows the subsequent purification and detection of these proteins through streptavidin-binding methods. Furthermore, birA's ability to specifically biotinylate proteins in live cells opens avenues for studying protein interactions, dynamics, and localization. The growing interest in protein engineering and synthetic biology has led to advances in birA technology, allowing for the manipulation of this system to enhance its efficiency and specificity for a range of applications, from targeted drug delivery to the development of biosensors. Overall, the exploration of birA recombinant protein not only provides insights into fundamental biological mechanisms but also contributes significantly to innovative biotechnological advancements.
