Analytical Data
-
Gene name
esxC
- Application
-
Alternative Names
(Ess extracellular protein C)
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0C051
-
Expression Region
1-130aa
-
Molecular Weight
22.4 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
The esxC gene, part of the esx locus found in mycobacterial species such as Mycobacterium tuberculosis, codes for a protein implicated in the secretion system essential for the virulence and pathogenicity of these bacteria. The study of esxC and its corresponding protein has garnered significant interest due to its crucial role in mediating host-pathogen interactions and modulating immune responses. Research has shown that esxC is involved in the secretion of effector proteins that can interfere with the host's immune system, allowing the bacteria to evade detection and persist within macrophages. Understanding the structure, function, and mechanisms of esxC protein is vital for unraveling the complex strategies employed by mycobacteria to establish infection and for the development of novel therapeutic strategies, including vaccines and targeted treatments. Investigations into esxC also provide insights into the broader context of protein secretion systems in pathogenic bacteria, highlighting potential avenues for intervention in mycobacterial diseases. As drug-resistant strains of tuberculosis continue to pose a critical global health challenge, deepening our understanding of esxC may prove essential in combating these infections and improving treatment outcomes.
