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. DNAJC21 (DnaJ homolog subfamily C member 21), also known as DNAJA5 or JJJ1, is a 531 amino acid protein that contains two C2H2-type zinc fingers and one J domain. Expressed in placenta, pancreas, kidney and brain, DNAJC21 may be a co-chaperone for HSP 70.
Description: Rabbit polyclonal to DNAJC21
Immunogen: KLH conjugated synthetic peptide derived from DNAJC21
Specificity: ·Reacts with Human, Mouse, Pig, Dog and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 62 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.
