Background: With the presence of the J domain defining a protein as a member, the DnaJ family has evolved with diverse cellular localization and functions and is one of the largest chaperone families. DnaJ heat-shock-induced proteins are derived from the bacterium Escherichia coli and are controlled by the htpR regulatory protein. 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 composed of zinc fingers that form a peptide-binding domain responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJC25 (DnaJ homolog subfamily C member 25) is a 360 amino acid multi-pass membrane protein that contains one J domain and is expressed as 3 isoforms produced by alternative splicing.
Description: Rabbit polyclonal to DNAJC25
Immunogen: KLH conjugated synthetic peptide derived from DNAJC25
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 42 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.
