Background: The DnaJ family is one of the largest of all chaperone families and has evolved with diverse cellular localization and functions. Presence of a J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are derived from Escherichia coli and are under the control of 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. DnaJ proteins contain cysteine rich regions that are composed of zinc fingers, which form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJC4 (DnaJ homolog subfamily C member 4), also known as HSPF2, MCG18 or DANJC4, is a 241 amino acid membrane protein that contains one J domain.
Description: Rabbit polyclonal to DNAJC4
Immunogen: KLH conjugated synthetic peptide derived from DNAJC4
Specificity: ·Reacts with Human, Mouse and Rat.
·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 28 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.
