Analytical Data
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Gene name
Barstar
- Application
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Alternative Names
Ribonuclease inhibitor
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Species
Bacillus amyloliquefaciens
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11540
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Expression Region
2-90aa
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Molecular Weight
17.7 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
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Protein Description
Barstar is a small, stable protein derived from the bacterium Bacillus amyloliquefaciens, which acts as a specific inhibitor of the ribonuclease barnase. The interaction between Barstar and barnase serves as a classic model for studying protein-protein interactions, folding, and stability, making it a valuable tool in molecular biology. The interest in Barstar has grown due to its potential applications in biotechnology and medicine, including the development of targeted drug delivery systems and the engineering of protein-based therapeutics. Research on Barstar has revealed insights into the mechanisms of protein stability, aggregation, and folding pathways, and efforts to genetically modify Barstar have opened new avenues for improving its binding properties and adaptability to different conditions. Furthermore, Barstar's relatively simple structure and ease of manipulation make it an attractive candidate for use in laboratory studies that aim to better understand the principles of protein function and interaction dynamics. The ongoing exploration of Barstar's capabilities, particularly in the context of protein engineering and synthetic biology, continues to generate significant interest within the scientific community. Thus, understanding and harnessing the properties of Barstar could pave the way for innovative solutions in various fields, including therapeutics, agri-biotechnology, and bioengineering, reflecting the crucial role that this unique protein plays in advancing contemporary biological research and applications.
