DnaJ Antikörper

The DnaJ family, one of the largest of all the chaperone families, has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat-shock induced proteins are derived from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. Members of this family contain cysteine-rich regions that are composed of zinc fingers that form a peptide-binding domain responsible for the chaperone function. They are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB7 (DnaJ homolog subfamily B member 7), also designated HSC3, is a 309 amino acid protein that contains one J domain and is thought to act as a co-chaperone.