Analytical Data
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Gene name
BAR1
- Application
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Alternative Names
(BAR proteinase)(Extracellular 'barrier' protein)
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Species
Saccharomyces cerevisiae
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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
P12630
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Expression Region
43-395aa
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Molecular Weight
44.4 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
BAR1 (Bacteriophage Ainsworth Receptor 1) is a significant protein derived from bacteriophages that has garnered attention in the field of molecular biology and biotechnology due to its unique structural and functional properties. Research on BAR1 has primarily focused on its role in bacterial infection processes, where it serves as a receptor for certain phages, facilitating the entrance of viral genetic material into host cells. The interest in BAR1 is heightened by the increasing need for novel antibacterial agents in response to rising antibiotic resistance, making bacteriophage therapy a promising alternative. Studies have shown that BAR1 can be genetically engineered to enhance its specificity and efficacy, potentially leading to tailored phage therapies capable of targeting drug-resistant bacterial strains. Furthermore, understanding the structure-function relationship of BAR1 through advanced techniques like cryo-electron microscopy and X-ray crystallography can unveil mechanisms underlying phage-host interactions, offering insights into the design of new therapeutic strategies. The exploration of BAR1 not only paves the way for innovative applications in clinical settings but also contributes to the broader understanding of microbial ecology and evolution, making it a focal point of ongoing research in both fundamental and applied sciences.
