The DNAJC8 antibody is a research tool designed to target the DNAJC8 protein, a member of the J-domain-containing cochaperone family. DNAJC8. also known as heat shock protein 40 (Hsp40) homolog subfamily C member 8. functions as a co-chaperone for Hsp70 proteins, aiding in protein folding, trafficking, and degradation. It plays a regulatory role in diverse cellular processes, including stress response, apoptosis, and signal transduction. The DNAJC8 protein contains a conserved J-domain that mediates interaction with Hsp70. along with additional domains for substrate recognition.
Antibodies against DNAJC8 are primarily used in molecular and cell biology to study its expression, localization, and interactions. They enable techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore DNAJC8’s involvement in diseases such as cancer, neurodegenerative disorders, and metabolic syndromes. Dysregulation of DNAJC8 has been linked to disrupted protein homeostasis, contributing to pathological aggregation of misfolded proteins.
Available as monoclonal or polyclonal forms, DNAJC8 antibodies are validated for specificity across species, often human, mouse, or rat. Researchers utilize these antibodies to dissect DNAJC8’s role in stress adaptation pathways and its potential as a therapeutic target. Current studies focus on its interplay with client proteins and Hsp70 in disease models, offering insights into chaperone network dynamics.