Analytical Data
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Gene name
BOC
- Application
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6AZB0
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Expression Region
Lys668~Thr866
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Molecular Weight
23kDa
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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 research on Recombinant Proteins of BOC (Bacillus Oligosaccharide Components) has gained significance due to their potential applications in biotechnology and medicine. BOC operates as a model organism for studying protein expression and folding, given its ability to produce and secrete complex proteins efficiently. The increasing demand for biopharmaceuticals, particularly in the fields of vaccine development and therapeutic proteins, has driven the exploration of BOC's recombinant protein capabilities. Researchers aim to harness BOC's unique metabolic pathways to enhance yield and functionality of proteins, addressing challenges in traditional expression systems such as E. coli and yeast. The specific focus on BOC stems from its ability to perform post-translational modifications, which are crucial for the bioactivity of many proteins. Additionally, the implications of producing therapeutic proteins with enhanced stability and activity make BOC a promising candidate in the recombinant protein field. Current studies emphasize optimizing culture conditions, gene cloning techniques, and purification processes to maximize efficiency and efficacy of the recombinant proteins derived from BOC.
