Analytical Data
-
Gene name
clpC
- Application
-
Alternative Names
clpC; SAV0525ATP-dependent Clp protease ATP-binding subunit ClpC
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q99W78
-
Expression Region
1-147aa
-
Molecular Weight
32.4 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
ClpC is a chaperone protein belonging to the Clp (caseinolytic protease) family, which plays a critical role in protein homeostasis within various bacterial and eukaryotic cells. Its primary functions include protein folding, assembly, and degradation, thus ensuring that misfolded or aggregated proteins are effectively managed. The significance of ClpC has gained increasing attention in the research community due to its involvement in essential cellular processes, such as stress response, regulation of enzyme activity, and adaptation to environmental changes. Studies have shown that ClpC is essential for the survival of certain pathogenic bacteria, making it a potential target for the development of novel antimicrobial agents. The ability to produce recombinant ClpC proteins in heterologous expression systems enables researchers to investigate its functional properties, interaction with other proteins, and mechanisms of action in more detail. Furthermore, understanding the structure and dynamics of ClpC can reveal insights into its role in various biochemical pathways and its potential implications in diseases associated with protein misfolding. Overall, the study of recombinant ClpC proteins is crucial for advancing our knowledge of protein quality control mechanisms and developing targeted therapeutic strategies.
