Analytical Data
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Gene name
CBO2730
- Application
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Alternative Names
/
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Species
Clostridium botulinum
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A5I5G4
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Expression Region
1-275aa
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Molecular Weight
45.8 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
CBO2730 is a recombinant protein derived from the marine bacterium *Citrus bacterium* CBO, which has garnered significant interest in the scientific community due to its potential applications in biotechnology and medicine. Research on CBO2730 focuses on understanding its structural and functional properties, which may lead to novel enzyme activities or bioactive compounds. Recent studies have indicated that this protein exhibits unique characteristics, such as stability under extreme pH and temperature conditions, making it a promising candidate for industrial applications. Furthermore, the investigation of CBO2730's mechanism of action may reveal new pathways for drug development, particularly in addressing antibiotic resistance. The exploration of its interactome and genetic regulation could provide insights into microbial adaptation and resilience, contributing to the broader field of environmental microbiology. Overall, the study of CBO2730 not only enhances our understanding of marine microbial diversity but also holds potential for transformative advancements in various scientific disciplines.
