The DCAF16 Knockout Raji Polyclonal Cells comprise a CRISPR/Cas9-edited polyclonal knockout cell population, designed to disrupt DCAF16 gene expression in the Raji B lymphocyte cell line. This product provides a heterogeneous pool of cells with targeted gene disruption, offering a rigorous loss-of-function model for studying DCAF16 biology without the need for single-cell cloning. The polyclonal format preserves biological complexity while ensuring robust knockout representation across the population, suitable for assays requiring population-level consistency.
The Raji cell line is a suspension-adapted human B lymphocyte model originally derived from a patient with Burkitt lymphoma. These cells are Epstein-Barr virus (EBV)-positive and exhibit characteristics of a lymphoblastoid cell line, making them a widely used system for investigating hematological malignancies, B-cell biology, and signal transduction. Their cancerous origin and continuous proliferation render them ideal for functional genomics and targeted protein degradation studies in a lymphoid context.
Mechanistically, DCAF16 functions as a substrate receptor for the CUL4-DDB1 E3 ubiquitin ligase complex. It directly interacts with DDB1, CUL4A/B, and RBX1 to facilitate the transfer of ubiquitin onto specific target proteins, tagging them for proteasomal degradation. This process is tightly regulated by neddylation of CUL4 and the COP9 signalosome. DCAF16 has been implicated in recruiting zinc finger proteins and engineered degron fusions such as FKBP12 to the proteasome, operating in cereblon (CRBN)-independent degradation pathways. Upstream regulators include the neddylation machinery, while downstream consequences involve ubiquitin?Cproteasome-mediated turnover of substrates.
In the context of Burkitt lymphoma and B-cell malignancies, DCAF16-dependent ubiquitination may influence oncogenic protein stability and cellular homeostasis. The Raji model enables dissection of CRL4DCAF16 substrate recognition and its role in lymphoid cancer biology. Given emerging strategies to harness DCAF16 for targeted protein degradation, this knockout model serves as a critical tool to validate DCAF16-dependency, characterize alternative degradation routes, and assess the cancer cell-intrinsic functions of the CRL4 complex.
Researchers can employ these polyclonal knockout cells in a variety of advanced applications, including Western blotting and RT-qPCR to confirm DCAF16 ablation, TMT-based quantitative proteomics to identify substrates, cycloheximide chase assays to monitor protein stability changes, and flow cytometry for apoptosis and cell cycle analysis. They are also suitable for screening DCAF16 ligands and molecular glues, and for discerning CRBN-independent degradation mechanisms. Each lot is verified for cell viability and population-level editing. For further details, please contact Ascent Research.
