The FKBP2 Knockout Raji Polyclonal Cells are a CRISPR/Cas9-mediated gene-disrupted cell pool derived from the human Raji B lymphoblast line, designed to eliminate functional FKBP2 expression without isolation of monoclonal derivatives. This polyclonal knockout population provides a physiologically heterogeneous model, reflecting the genetic variability likely encountered in tumor cell populations, while enabling loss-of-function analyses of the ER-resident peptidyl-prolyl isomerase FKBP2.
The Raji cell line, established from a Burkitt??s lymphoma patient, is a suspension-growing B lymphoblastoid line that serves as a workhorse in B-cell malignancy research. Raji cells maintain key features of transformed B cells, including constitutive signaling cascades relevant to survival and proliferation, and are sensitive to ER stress perturbations. Their lymphoid identity makes them an ideal host for examining how protein folding defects intersect with B-cell pathobiology.
FKBP2 is an ER-luminal chaperone that catalyzes prolyl isomerization, accelerating the rate-limiting step of protein folding. It functions in concert with the core ER quality-control machinery, physically interacting with BiP/GRP78, calnexin, calreticulin, and newly synthesized polypeptides. FKBP2 activity is integrated into the unfolded protein response (UPR): under ER stress, UPR sensors such as ATF6 and IRE1?? activate transcriptional programs including XBP1, which in turn upregulate folding catalysts. By facilitating proper protein maturation, FKBP2 contributes to the termination of ER stress signaling and restoration of homeostasis.
Disruption of FKBP2 in Raji cells is predicted to hinder efficient protein folding, leading to chronic UPR activation and potentially triggering apoptosis or adaptive survival responses. Given that B lymphomas often rely on heightened ER capacity to manage immunoglobulin synthesis and oncogenic protein loads, FKBP2 knockout provides a tractable model to study how impaired prolyl isomerization affects the balance between cell death and malignant growth. Key readouts include UPR markers such as the ER chaperone BiP and the pro-apoptotic transcription factor CHOP.
This product is ideally suited for investigating the role of ER protein quality control in B-cell malignancies, identifying small-molecule modulators of the UPR, and dissecting FKBP2-mediated folding pathways. Compatible assay formats include immunoblotting for BiP and CHOP, quantitative RT-PCR for XBP1 mRNA splicing, Annexin V-based apoptosis detection by flow cytometry, and luminescent or fluorescent ER stress reporters. For further details or bulk order inquiries, please contact Ascent Research.
