The DnaJ family is one of the largest of all the chaperone families and 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 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. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJC3 (DnaJ homolog subfamily C member 3), also known as P58, HP58, PRKRI or P58IPK, is a Interferon-induced, double-stranded RNA-activated protein kinase inhibitor.
应用类型
WB
免疫原
A synthetic peptide corresponding to residues in Human DNAJC3
