Analytical Data
-
Gene name
cap5A
- Application
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P95695
-
Expression Region
1-222aa
-
Molecular Weight
26.4 kDa
-
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
Cap5A, an important protein found in certain bacterial species, has garnered significant interest in the field of microbiology and biotechnology due to its crucial role in virulence and adaptation. This protein is primarily associated with the pathogenicity of bacterial strains, influencing their ability to adhere to host tissues and evade the immune response. Research into Cap5A has revealed its involvement in forming capsular structures, which serve as protective barriers against host defense mechanisms, thereby enhancing the survival and infectious capacity of bacteria. Understanding the molecular mechanisms underlying Cap5A's function provides valuable insights into bacterial pathogenesis and opens up potential avenues for developing novel therapeutic strategies, including vaccines and antibody treatments. Furthermore, the recombinant production of Cap5A offers opportunities for studying its structure and function in detail, facilitating the exploration of its applications in biomedicine and vaccine development. As antibiotic resistance becomes a growing concern, targeting virulence factors like Cap5A might represent a promising approach to combat bacterial infections. Thus, ongoing research into the recombinant expression and functional characterization of Cap5A is crucial for advancing our understanding of bacterial behavior and developing effective interventions.











