Background: 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.
Description: Rabbit polyclonal to DNAJC17
Immunogen: KLH conjugated synthetic peptide derived from DNAJC17
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 34 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
