Analytical Data
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Gene name
yscF
- Application
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Alternative Names
/
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Species
Burkholderia thailandensis
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Source
Yeast
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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
Q2T727
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Expression Region
1-89aa
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Molecular Weight
11.4kDa
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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
YscF is a crucial protein associated with the type III secretion system (T3SS) in various pathogenic bacteria, playing a significant role in the assembly of the secretion needle complex that facilitates the translocation of virulence factors into host cells. The T3SS is a sophisticated molecular apparatus that allows bacteria to inject effector proteins directly into eukaryotic cells, thereby manipulating host cellular processes and promoting bacterial virulence. Research on YscF and its structural and functional properties has garnered interest due to its potential as a target for therapeutic interventions against bacterial infections. Understanding YscF's role in the T3SS could provide insights into the mechanisms of bacterial pathogenesis and lead to the development of novel antimicrobial strategies. Furthermore, the production and characterization of recombinant YscF proteins enable detailed studies of the protein's interactions and structural dynamics, which are essential for elucidating the assembly mechanisms of the T3SS. This research not only contributes to our understanding of bacterial virulence but also paves the way for innovative approaches to combat bacterial diseases through targeted therapies.
