Anti-DNAJB1

Heat shock protein 40 (HSP 40) family proteins bind to HSP 70 through their J-domain and regulate the function of HSP 70 by stimulating HSP 70 ATPase activity. HSP 40, also known as DnaJ, functions together with DnaK (HSP 70) and GrpE as a molecular chaperone, involving them in assembly and disassembly of protein complexes, protein folding, renaturation of denatured proteins, prevention of protein aggregation and protein export. HSP 40 stimulates the association between HSC 70 and HIP and translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. There are five known HSP 40 family proteins. Protein function: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). [The UniProt Consortium]