The DNAJC14 antibody targets the DNAJC14 protein, a member of the Hsp40/DnaJ family of molecular chaperones. DNAJC14. also known as Hsp40 homolog subfamily C member 14. functions as a co-chaperone for Hsp70 proteins, aiding in protein folding, translocation, and degradation. It contains a conserved J-domain critical for Hsp70 interaction and plays roles in cellular stress responses, endoplasmic reticulum (ER)-associated degradation (ERAD), and viral replication processes. Studies link DNAJC14 to host-pathogen interactions, particularly in hepatitis C virus (HCV) and dengue virus replication, where it modulates viral polyprotein processing.
Antibodies against DNAJC14 are widely used in research to detect and quantify the protein in techniques like Western blotting, immunoprecipitation, and immunofluorescence. These tools help elucidate its regulatory mechanisms in cellular pathways, including autophagy, apoptosis, and oncogenic signaling (e.g., Wnt/β-catenin). Commercial DNAJC14 antibodies are typically raised in rabbits or mice, available as monoclonal or polyclonal forms, with validation in specific applications.
Despite its established roles, DNAJC14's precise molecular mechanisms remain incompletely understood. Ongoing research focuses on its potential as a therapeutic target in viral infections, cancer, and neurodegenerative diseases. Antibody-based studies continue to uncover its tissue-specific expression patterns and interactions with disease-associated proteins.