The GYPC Knockout SK-HEP-1 Polyclonal Cells product comprises a heterogeneous population of SK-HEP-1 cells subjected to CRISPR/Cas9-mediated disruption of the GYPC gene, generating a polyclonal knockout model with diverse editing events across the cell pool. This population-level knockout strategy avoids single-cell clonal selection, providing a representative loss-of-function system that reflects the genetic variability inherent in CRISPR-based gene disruption. The product is designed for researchers requiring a robust GYPC-deficient hepatocellular carcinoma model without clonal bias, enabling broad assessment of GYPC-dependent phenotypes in liver adenocarcinoma cells.
SK-HEP-1 is a human liver adenocarcinoma epithelial cell line originally derived from the ascitic fluid of a patient with hepatocellular carcinoma. This widely used model exhibits an adherent growth pattern and retains features relevant to hepatic cancer, including metabolic activity and representative oncogenic pathway profiles. The cell line serves as a platform for investigating hepatocellular carcinoma biology, drug responses, and epithelial cell signaling. In this context, GYPC expression patterns and functional contributions remain poorly characterized, positioning the knockout model as a valuable tool for uncovering non-erythroid roles of glycophorin C.
The GYPC gene encodes glycophorin C, an integral membrane glycoprotein best known for its critical structural role in erythrocytes, where it connects the plasma membrane to the underlying spectrin?Cactin cytoskeleton. This anchoring is mediated through direct interactions with protein 4.1R (EPB41) and p55 (MPP1), and indirectly via associations with dematin (DMTN) and band 3 (SLC4A1). The extracellular domain of glycophorin C also acts as a receptor for Plasmodium falciparum EBA-140, facilitating malarial invasion. Transcriptional regulation by GATA1, KLF1, and erythropoietin receptor signaling governs its erythroid expression. Although these molecular assemblies are classically defined in red blood cells, analogous membrane?Ccytoskeleton linkages and protein interaction networks may operate in epithelial cells, where GYPC could influence cell shape, adhesion, and mechanical stability.
The GYPC knockout in SK-HEP-1 cells provides a unique model for dissecting glycophorin C function in a hepatic carcinoma background, moving beyond traditional erythrocyte studies. By ablating GYPC expression, researchers can examine its contribution to hepatocellular carcinoma cell architecture, migratory behavior, and interactions with extracellular matrices. The model may reveal novel roles for GYPC in membrane organization or cell adhesion pathways that are dysregulated in liver cancer. Additionally, it enables comparative studies between erythroid and non-erythroid compartments, potentially identifying tissue-specific functions of the protein and its binding partners.
This polyclonal knockout product supports a range of experimental applications, including investigation of membrane?Ccytoskeleton dynamics, malaria invasion mechanisms (by ectopic expression of EBA-140 receptors), and blood group antigen research. Typical assays include western blotting and flow cytometry to confirm GYPC depletion, co-immunoprecipitation with EPB41 or MPP1 to probe residual interactions, immunofluorescence for localization studies, and osmotic fragility tests if redifferentiation protocols are applied. The model is also suited for functional assays measuring cell adhesion, invasion, or response to mechanical stress. For further details or custom inquiries, please contact Ascent Research.
