CTSD Knockout Raji Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human Burkitt??s lymphoma Raji B lymphoblastoid cell line. These cells harbor a targeted disruption of the CTSD gene, which encodes the lysosomal aspartic protease cathepsin D. The polyclonal nature of this product provides a heterogeneous pool of edited cells with varying allelic modifications, serving as a robust tool for studying the loss-of-function effects of cathepsin D in B lymphocyte biology without the artifacts of clonal selection.
The Raji cell line is an Epstein-Barr virus (EBV)-positive B lymphoblastoid line established from a Burkitt??s lymphoma patient. Raji cells display a mature B cell phenotype, expressing surface immunoglobulins and markers characteristic of germinal center B cells. They are widely employed as a model system for studying B cell differentiation, lymphomagenesis, and EBV-driven oncogenic mechanisms. The well-characterized genetic and epigenetic landscape of Raji cells makes them an ideal host for investigating the molecular pathways that govern B cell survival, proliferation, and transformation.
Cathepsin D mediates lysosomal proteolysis and is implicated in protein turnover, antigen processing, apoptosis regulation, and extracellular matrix remodeling. Transcriptionally controlled by Sp1 and USF, it is induced by estrogen, EGF, and IGF-1. Downstream, it cleaves fibronectin and laminin, and activates pro-uPA, pro-MMP2, and pro-MMP9, promoting invasion. Cathepsin D interacts with cystatin C, mannose-6-phosphate receptors, and integrins, and modulates apoptosis via Bid. In Raji B cells, loss of CTSD disrupts these processes, potentially affecting NF-??B and PI3K/AKT signaling.
In the Raji B lymphoblastoid context, CTSD knockout impairs lysosomal function, leading to defective antigen processing and presentation??a key aspect of immune surveillance. Disruption of Bid-mediated apoptotic signaling and potential attenuation of NF-??B pathways may alter survival. Diminished extracellular matrix degradation reduces invasive behavior, making this system valuable for studying B cell malignancy and lysosomal contributions to lymphoma.
This polyclonal knockout population is suited for investigating lysosomal biology in B-cell lymphoma, the role of cathepsin D in antigen presentation, cancer invasion, drug resistance, and lysosomal storage disorders. Compatible assays include Western blotting, RT-qPCR, RNA-seq, flow cytometry, apoptosis and migration/invasion assays, enzymatic activity measurements, and drug sensitivity testing. This model provides a robust platform for mechanistic and translational studies. For further information, contact Ascent Research.
