Analytical Data
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Gene name
CBU
- Application
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Alternative Names
CBU；Outer membrane Protein P1
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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
Q83EK8
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Expression Region
1-252aa
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AA Sequence
METTTKLAIGVSALCCLASAAFAGGPDIPMIDMNGFHIGLGFGYKSYTYDQVGTVTVTTNGGTVLSVLHPVSASITQFGPVGELGYTFASDWWIAGVKAQYQYDNVRSVHIMDAPLVGSNYSYRTRLGSHLTAMLLAGIKVNEANAVYLEAGYSTVWGKTTLFGPGPVAVSMKNRLNGGIAGIGWRHYFMNNVFLDLSYDYALYRSKSNSVTLSSATASAEGTAIGVSGTVQNPKRVAINGITATVNYLFNI
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Molecular Weight
26.7 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 CBU (Codon-optimized Bacillus subtilis-Expressed Recombinant Proteins) has gained significant attention in the field of biotechnology and protein engineering. CBU proteins are particularly notable for their high yield and stability, which are crucial for various applications ranging from industrial enzymes to therapeutic proteins. Bacillus subtilis is an ideal host organism due to its ability to secrete proteins directly into the culture medium, simplifying purification processes. Research has focused on optimizing codon usage to enhance protein expression levels, as the genetic code can vary significantly among different organisms. By adjusting codon bias to match the host's translational machinery, scientists aim to improve the efficiency of recombinant protein production. Additionally, CBU proteins often exhibit enhanced structural integrity and functional properties, making them suitable for diverse applications in medicine, agriculture, and environmental science. Current studies explore the engineering of CBU proteins to enhance their specificity, activity, and stability, while minimizing immunogenicity for therapeutic purposes. As the demand for sustainable and efficient bioprocessing techniques grows, the advancement in CBU research plays a pivotal role in developing innovative solutions for global challenges.
