RelevanceDNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus, a glycine/phenylalanine (G/F)-rich region, and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain.
ab103321 at 1/50 dilution staining DNAJC6 by immunohistochemistry in formalin-fixed and paraffin-embedded Human brain tissue followed by peroxidase conjugation of the secondary antibody and DAB staining.
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