Background: 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. DnaJC13 (DnaJ homolog subfamily C member 13), also designated receptormediated endocytosis 8 (RME-8), is a 2,243 amino acid protein that contains one J domain and functions to mediate endosomal trafficking. DnaJC13 also influences epidermal growth factor receptor (EGFR) levels and may be a potential therapeutic target in ErbB2-positive breast cancers.
Description: Rabbit polyclonal to DNAJC13
Immunogen: KLH conjugated synthetic peptide derived from DNAJC13
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 254 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.
