Analytical Data
-
Gene name
BFP
- Application
-
Alternative Names
pBI-SS(Tom)(TP)101-EGFP
-
Species
Others
-
Source
E. coli
-
Tag
His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
DQ399412
-
Expression Region
C228-C1455
-
Protein Length
Partial
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
HtrA (High temperature requirement A) proteins are serine proteases that play crucial roles in bacterial stress response, protein quality control, and pathogenesis. In many pathogenic bacteria, such as *Escherichia coli* and *Helicobacter pylori*, HtrA is involved in the protection of cells under heat shock and other stressful conditions by facilitating the degradation of misfolded proteins. Additionally, it has been implicated in the regulation of virulence factors and can influence biofilm formation, making it an attractive target for antibiotic development. The study of recombinant HtrA proteins has gained momentum, as these proteins can be expressed, purified, and characterized to better understand their structure-function relationships. Recent advances in recombinant DNA technology have enabled researchers to produce large quantities of HtrA proteins, allowing for in-depth biochemical and biophysical analyses. Studying these proteins not only sheds light on their mechanistic roles in bacterial survival and pathogenicity but also opens avenues for therapeutic interventions against bacterial infections. Thus, the exploration of HtrA as a recombinant protein serves as a promising frontier in microbial research and drug development, bridging knowledge gaps that exist in bacterial cell biology and host-pathogen interactions.
