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.

DnaJC17 Polyclonal Antibody detects endogenous levels of DnaJC17 protein.

Optimal working dilutions should be determined experimentally by the investigator. Suggested starting dilutions are as follows: WB: 1:500-1:2000, ELISA: 1:20000. Not yet tested in other applications.

DnaJC17 Polyclonal Antibody product listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.

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