The DnaJ family is one of the largest of all 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, forming peptide binding domains responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DNAJC17 (DnaJ (Hsp40) homolog, subfamily C, member 17) is a 304 amino acid protein containing a J domain and a RRM (RNA recognition motif) domain.蛋白別名為：DNAJC17; DnaJ homolog subfamily C member 17;基因ID為：55192；蛋白質ID:Q9NVM6
應用類型
WB，ELISA補充：最優的抗體稀釋比例需要基于客戶實驗進行優化.建議的起始稀釋比例如下: WB: 1:500-1:2000, ELISA: 1:20000. Not yet tested in other applications.
免疫原
合成多肽：the N-terminal region of human DnaJC17. at AA rangle: 30-110
