clpB Protein, E.coli

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 is the recombinant E. coli-derived clpB protein, expressed by E. coli , with tag free. The total length of clpB Protein, E.coli is 857 a.a., .

ClpB operates as a pivotal component within a stress-induced multi-chaperone system, collaboratively orchestrating cellular recovery from heat-induced damage alongside DnaK, DnaJ, and GrpE. Acting upstream of DnaK, ClpB plays a crucial role in processing protein aggregates, with its ATPase activity stimulated upon protein binding. The ensuing ATP hydrolysis facilitates the unfolding of denatured protein aggregates, potentially exposing new hydrophobic binding sites on ClpB-bound aggregates. This orchestrated process contributes to the solubilization and refolding of denatured protein aggregates, an essential cooperative effort involving DnaK. In its functional state, ClpB forms a homohexamer, and the oligomerization is intricately regulated by ATP, underscoring the dynamic nature of its involvement in cellular stress responses.

E.coli

E. coli

Tag Free

P63286 (M1-Q857)

75205855

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.