The DCAF5 (DDB1- and CUL4-associated factor 5) antibody is a research tool targeting the DCAF5 protein, a substrate receptor component of the CUL4-DDB1 E3 ubiquitin ligase complex. DCAF5. also known as WDR40A, contains WD40 repeat domains that mediate protein-protein interactions, enabling substrate recognition for ubiquitination. This post-translational modification typically tags proteins for proteasomal degradation, regulating processes like DNA repair, cell cycle progression, and chromatin remodeling.
DCAF5 has gained attention due to its role in human diseases. Studies link it to cancer progression through dysregulated degradation of tumor suppressors or oncoproteins. Notably, DCAF5 is implicated in the turnover of the histone demethylase KDM4A, influencing epigenetic regulation. In hematological malignancies, DCAF5 overexpression correlates with genomic instability. Additionally, DCAF5 interacts with viral proteins, potentially aiding viral immune evasion.
Antibodies against DCAF5 are essential for studying its expression patterns, interactome, and subcellular localization via techniques like Western blot, immunofluorescence, and co-immunoprecipitation. They also facilitate functional studies using knockdown/knockout models. Recent interest in targeting ubiquitination pathways for cancer therapy has spurred the development of DCAF5-specific antibodies as potential diagnostic tools or therapeutic companions. However, the complete spectrum of DCAF5 substrates and regulatory mechanisms remains under investigation, necessitating further research to fully exploit its clinical potential.