Analytical Data
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Gene name
btuF
- Application
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Alternative Names
btuF；yadT；Vitamin B12-binding Protein
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Species
Human
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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
P37028
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Expression Region
24-266aa
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AA Sequence
PRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNALSQVD
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Molecular Weight
53.9 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 btuF gene encodes a protein that plays a crucial role in the transport of cobalamin (vitamin B12) across the bacterial cell membrane, specifically in Escherichia coli. As vitamin B12 is essential for various cellular processes, including DNA synthesis and metabolic pathways, understanding the function of btuF and its encoded protein is vital for elucidating bacterial survival mechanisms and metabolism. The btuF protein is part of a larger ABC (ATP-binding cassette) transporter system, which is responsible for the high-affinity uptake of cobalamin from the environment. Research into the btuF recombinant protein focuses on elucidating its structure, functional dynamics, and interaction with other components of the transport system. By employing techniques such as X-ray crystallography, chromatography, and mutagenesis, scientists aim to characterize the binding sites and transport mechanisms, providing insights into how bacteria adapt to nutrient-limited environments. Additionally, the exploration of btuF can have broader implications for biotechnology and medicine, including potential applications in developing antibiotic strategies and understanding bacterial resistance mechanisms. Enriching our comprehension of btuF and its transport system can open new avenues for research in microbiology, ecosystem dynamics, and the role of vitamins in cellular physiology.
