The DPP7 Knockout Raji Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal cell population derived from the Raji B lymphocyte line, engineered to disrupt the DPP7 gene. This loss-of-function model abrogates DPP7 protease activity, enabling functional studies of the encoded lysosomal serine protease with dipeptidyl peptidase activity. The polyclonal format offers a heterogeneous knockout pool that minimizes clonal selection artifacts, suitable for population-level analyses of lysosomal proteolysis.
Raji cells are an Epstein-Barr virus (EBV)-transformed lymphoblastoid cell line originating from a Burkitt’s lymphoma patient. They serve as a well-established model for B-cell biology and lymphoma research, exhibiting robust proliferation and characteristic surface markers. This background provides a physiologically relevant context for examining DPP7’s role in B-cell lymphoma survival, as these cells rely on functional lysosomal pathways for degradation and recycling, processes potentially subverted in cancer.
DPP7 is a lysosomal serine protease that functions downstream of the transcription factors TFEB and MITF, master regulators of lysosomal biogenesis. The protease cleaves N-terminal dipeptides from peptide substrates within the lysosome, contributing to the terminal stages of protein degradation and modulating autophagic flux. Its activity intersects with key components of the autophagy-lysosome pathway, including cathepsins CTSD and CTSB, lysosomal membrane proteins LAMP1 and LAMP2, and the autophagic cargo receptor SQSTM1/p62, as well as the autophagosome marker MAP1LC3B. DPP7-mediated peptide processing may influence lysosomal amino acid sensing and signaling cascades that control cell metabolism and survival.
In the Raji B-lymphoma background, DPP7 knockout creates a platform to dissect the dependency of malignant B cells on lysosomal proteolysis. As autophagy can support tumor cell survival under stress, loss of DPP7 function may impair bulk protein degradation and disrupt homeostasis, sensitizing cells to apoptosis. This model is therefore valuable for exploring the intersection of lysosomal biology and lymphoma pathogenesis, particularly the role of DPP7 in maintaining viability through autophagy-dependent nutrient recycling.
Research applications include detailed autophagy flux measurements using Western blotting for LC3 and p62, lysosomal activity assays with fluorogenic substrates, and cell viability assessments via MTT assay or flow cytometry (Annexin V/PI). The cells also facilitate immunofluorescence studies of lysosomal distribution (LAMP1) and RT-qPCR profiling of lysosomal gene expression. The DPP7 knockout polyclonal population serves as a robust tool for protease inhibitor screening and functional genetic studies. For additional product information or technical support, please contact Ascent Research.
