Analytical Data
-
Gene name
cap8A
- Application
-
Alternative Names
(Cancer/testis antigen 3.2)(CT3.2)(DSS-AHC critical interval MAGE superfamily 6)(DAM6)(MAGE XP-2 antigen)(MAGE-B2 antigen)
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P72367
-
Expression Region
1-319aa
-
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
Cap8A is a protein that has garnered significant interest in the field of biotechnology and molecular biology due to its unique properties and potential applications. This protein is derived from certain bacterial species, where it plays a critical role in cellular processes such as biofilm formation and pathogenicity. Research into Cap8A has intensified as scientists seek to understand its structural characteristics, functional mechanisms, and relevance in various biological contexts. Studies have indicated that Cap8A may interact with host immune systems, influencing bacterial virulence and persistence. Furthermore, its ability to form stable complexes and modular protein structures makes Cap8A an intriguing candidate for recombinant protein technologies. Such advancements could pave the way for innovative therapeutic strategies, including vaccine development or the engineering of novel biomaterials. By exploring Cap8A's properties and functions, researchers aim to unlock its potential in combating bacterial infections and understanding fundamental biological processes at the molecular level. This backdrop sets the stage for ongoing investigations into Cap8A, positioning it as a focal point for future studies in microbiology and protein engineering.
