Analytical Data
-
Gene name
clpB
-
简介
ClpB protein is a key component in the stress-induced multichaperone system, which cooperates with DnaK, DnaJ and GrpE to promote cell recovery from heat-induced injury. Upstream of DnaK, ClpB processes protein aggregates and upon binding stimulates their ATPase activity. clpB Protein, E.coli (K476C) is the recombinant E. coli-derived clpB protein, expressed by E. coli , with tag free.
- Application
-
Alternative Names
clpB; Chaperone protein ClpB
-
Species
E.coli
-
Source
E. coli
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P63286
-
Expression Region
M1-Q857, K476C
-
Protein Length
Full Length
-
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
ClpB is a heat-shock protein belonging to the AAA+ ATPase family, crucial for protein quality control in cells. Its primary function is to facilitate the refolding of aggregated proteins, thereby maintaining cellular protein homeostasis, especially under stress conditions such as heat shock or oxidative stress. ClpB operates in concert with other molecular chaperones, such as GroEL and DnaK, forming a sophisticated cellular machinery that prevents protein misfolding and aggregation. Research on recombinant ClpB has gained significant interest due to its potential applications in biotechnology and medicine. It has been studied for its role in enhancing protein solubility, aiding in the refolding of therapeutic proteins, and improving yields in recombinant protein production. Furthermore, understanding ClpB's structure and function could provide insights into the molecular mechanisms of protein aggregation diseases, such as Alzheimer's and Parkinson's. By manipulating ClpB through genetic engineering or chemical modifications, scientists aim to develop novel strategies to combat these diseases and improve the biopharmaceutical production process. As a result, ClpB serves as a model system for investigating protein dynamics and chaperone interactions, making its study vital for advancing both basic and applied biological research.
