In Stock Cell Lines
The PRNP Knockout RK13 Cell Line is a CRISPR/Cas9-edited rabbit kidney epithelial cell line with targeted disruption of the PRNP gene, which encodes the cellular prion protein (PrPC). PrPC is a GPI-anchored glycoprotein that mediates signaling through STIP1 and LRP1, activates PKA and ERK1/2 pathways, and modulates cell adhesion via NCAM1 while regulating copper homeostasis. This knockout model enables rigorous investigation of PrPC-dependent processes in epithelial cells, including prion infection, copper transport, and signaling. It is suitable for western blotting, immunofluorescence, phospho-ERK analysis, copper uptake assays, and anti-prion compound screening, advancing research in prion diseases and neurodegeneration.
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The PRNP Knockout RK13 Cell Line is a CRISPR/Cas9-edited knockout cell line generated from the RK13 rabbit kidney epithelial cell line. This product provides a targeted loss-of-function model for the PRNP gene, which encodes the cellular prion protein (PrPC), enabling researchers to interrogate PrPC-dependent cellular mechanisms in a clean genetic background.
Initially established as a spontaneously immortalized line, RK13 cells retain key characteristics of kidney epithelium, including polarized morphology, tight junction formation, and active membrane transport systems. Their robust proliferation and amenability to transfection make them a practical host for gene-editing and a reliable platform for biochemical and functional assays. In the context of PrPC, RK13 cells allow investigation of adhesion, copper homeostasis, and signaling within an epithelial framework.
PRNP encodes PrPC, a glycosylphosphatidylinositol-anchored cell surface glycoprotein that mediates signaling through direct binding to STIP1 and LRP1, triggering downstream activation of PKA and ERK1/2. ERK1/2 phosphorylates CREB and modulates BCL2 family members, linking PrPC to cell survival and stress responses. PrPC also interacts with NCAM1 to promote cell adhesion and participates in copper metabolism by binding copper ions. Transcriptional control is exerted by SP1, AP-1, p53, and HIF1A, while post-translational regulation involves copper ions and oxidative stress. Interacting partners further include laminin, glycosaminoglycans, amyloid-beta peptides, tau, HSP90, and caveolin-1, connecting PrPC to pathways relevant to prion diseases, Alzheimer??s disease, and Parkinson??s disease.
In kidney epithelial cells, PrPC contributes to copper reabsorption and barrier integrity, and its knockout in the RK13 line offers a defined system to dissect these roles. The RK13 line is also permissive to prion infection; thus, the PRNP knockout allows separation of PrPC-dependent steps in prion propagation, internalization, and cytotoxicity from PrPC-independent effects. Moreover, this model permits evaluation of how PrPC influences responses to amyloid-beta oligomers, tau aggregates, and oxidative insults in an epithelial context, providing insights that complement neuronal studies.
Experimental approaches include standard gene expression analysis by RT-qPCR and Western blot, subcellular localization by immunofluorescence, and protein?Cprotein interaction mapping via co-immunoprecipitation. Signaling pathway activity can be assessed through phospho-ERK and cAMP-PKA assays. Functional studies utilizing copper uptake measurements and cell adhesion assays directly test PrPC-dependent phenotypes. This cell line also serves as a host for cell-based prion infection assays to screen anti-prion compounds and to study PrPC??s role in the replication of prions and the propagation of pathogenic protein aggregates. For further technical inquiries, please contact Ascent Research.
