Analytical Data
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Gene name
BUsg_347
- Application
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Alternative Names
BUsg_347; Porin-like protein BUsg_347
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Species
strain Sg
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8K9I8
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Expression Region
24-369aa
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Molecular Weight
59 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
BUsg_347 is a recombinant protein derived from the bacterial species Burkholderia pseudomallei, a pathogen known to cause melioidosis, a severe infectious disease. The study of BUsg_347 is significant due to its potential role in immune response modulation and pathogenesis associated with Burkholderia infections. Previous research has indicated that proteins from this bacterium might interact with host immune systems, influencing the course of infection. Given the increasing incidence of melioidosis in tropical regions and the bacterium's bioterrorism potential, understanding the molecular mechanisms of BUsg_347 could provide insights into vaccine development and therapeutic interventions. Additionally, the characterization of BUsg_347 allows for the exploration of its structural properties, functional activities, and its potential use as a biomarker for diagnosing Burkholderia infections. Thus, studying BUsg_347 not only contributes to the fundamental knowledge of host-pathogen interactions but also holds promise for public health advancements in combating infectious diseases caused by Burkholderia species.
