Analytical Data
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Gene name
btuD
- Application
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Alternative Names
btuD；Vitamin B12 import ATP-binding Protein BtuD
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Species
E.coli
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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
B0R5G4
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Expression Region
1-398aa
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AA Sequence
MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRLEDTTAASATRADIAAADVIAVPVAAAARPGVRGLLTGAVPTLAVGDAAGAPEWADRLVACDAVVSAVGALADTPSDGV
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Molecular Weight
40.5 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
Related Products
Protein Description
The study of recombinant proteins, particularly the btuD gene product, has gained significant attention in the field of molecular biology and biotechnology. btuD encodes a protein implicated in the transport and utilization of cobalamin (vitamin B12) in bacteria, playing a crucial role in cellular metabolism and growth. Understanding the function and structure of the btuD protein not only enhances our comprehension of microbial nutrient acquisition but also aids in developing potential biotechnological applications, such as the creation of biosensors or novel therapeutic strategies. The elucidation of the btuD protein's mechanisms could contribute to advancements in pharmaceuticals and agricultural sciences, particularly in enhancing nutrient availability. Researchers employ various techniques, including genetic engineering and protein expression systems, to produce recombinant btuD proteins for functional studies and crystallography, facilitating insights into its role within the cobalamin transport system. Given the rising interest in microbial systems for industrial applications, the study of the btuD protein has the potential to unlock novel approaches for optimizing microbial growth and productivity in various biotech sectors. Ultimately, the comprehensive exploration of btuD and its functionalities could bridge gaps in our understanding of microbial ecology and nutrient cycles, paving the way for innovative solutions to address global challenges in health and sustainability.
