Analytical Data
-
Gene name
btuC
- Application
-
Alternative Names
btuC; OE_2952FCobalamin import system permease protein BtuC
-
Species
Halobacterium salinarum
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B0R5G3
-
Expression Region
1-369aa
-
Molecular Weight
40.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 the btuC recombinant protein primarily centers on its role in bacterial cobalamin (vitamin B12) transport and metabolism. Cobalamin is an essential cofactor for various enzymatic reactions, particularly in prokaryotes and eukaryotes. The btuC gene is a fundamental component of the btuB-btuC-btuD operon in Escherichia coli, which encodes proteins involved in the high-affinity uptake of cobalamin. Research into btuC recombinant protein has gained significance due to its potential applications in biotechnology and medicine. Understanding the structure and function of btuC can provide insights into the mechanisms of cobalamin transport, which may lead to the development of novel strategies for combating bacterial infections or enhancing the nutritional value of foods. Additionally, characterizing this protein may unveil targets for peptide or small molecule intervention, impacting metabolic engineering and synthetic biology. The exploration of btuC also contributes to the broader understanding of microbial metabolism and adaptation to nutrient availability, pivotal in environmental microbiology and bioengineering applications. As such, btuC recombinant protein serves as a promising candidate for further research, aiming to elucidate its role and applications in various fields.
