Description
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. It serves as a co-chaperone for HSPA5 and binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. Recombinant human DNAJB11 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques