The PARP12 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population engineered via CRISPR/Cas9-mediated gene disruption of PARP12 in the Raji B lymphoblastoid cell line. This loss-of-function model facilitates dissection of PARP12-dependent mechanisms in a human B lymphocyte background. The polyclonal format provides a heterogeneous knockout population suitable for bulk functional studies.
The Raji cell line, derived from a Burkitt lymphoma patient, is a human B lymphoblastoid line positive for Epstein-Barr virus (EBV). It serves as a well-characterized model for EBV-associated lymphomagenesis, B cell signaling, and antiviral innate immunity, making it highly relevant for studying PARP12 function in these contexts.
PARP12 is an interferon-induced mono-ADP-ribosyltransferase that mediates antiviral responses. It is upregulated by type I interferons (IFN-??/??) and interferon regulatory factors (IRFs). PARP12 catalyzes ADP-ribosylation of target proteins, including translation factors eIF4G and eIF4E, and promotes stress granule assembly via interactions with G3BP1 and TIA-1. These actions regulate protein translation and stress granule dynamics. Additionally, PARP12 modulates NF-??B signaling by influencing p65 phosphorylation and interacts with IRF3, thereby controlling pro-inflammatory cytokine production and viral replication. It forms functional complexes with other PARP family members, such as PARP13/ZAP, linking interferon signaling to post-transcriptional control.
In the EBV+ Raji context, PARP12 knockout enables investigation of the interplay between antiviral innate immunity and B cell lymphomagenesis. EBV manipulates host innate immune pathways, and PARP12 may restrict viral replication while influencing tumor cell survival. The polyclonal knockout population allows assessment of how PARP12 loss impacts NF-??B activity, stress granule formation, and translational control in lymphoma cells. This model may reveal vulnerabilities in EBV-associated Burkitt lymphoma and identify PARP12-dependent signaling nodes.
Key research applications include viral infection assays to study antiviral innate immunity, co-immunoprecipitation for substrate identification, and immunofluorescence to monitor stress granule markers (G3BP1, TIA-1). NF-??B reporter assays and RNA-seq can delineate PARP12-dependent transcriptional programs. The cells are also suited for high-throughput screening of antiviral or anticancer compounds, and for evaluating PARP12 as a therapeutic target. For additional details, please contact Ascent Research.
