DPY19L4 Knockout HAP1 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population targeting the DPY19L4 gene. This product supplies a heterogeneous pool of HAP1 cells with gene disruptions, enabling loss-of-function studies without single-cell cloning. The polyclonal format is ideal for pooled screening applications and functional assays requiring population-level responses.
The host HAP1 cell line originates from the KBM-7 chronic myeloid leukemia line and is haploid for most chromosomes except chromosome 8. This near-haploid karyotype facilitates clean knockout phenotypes, as only one allele needs disruption. HAP1 cells are adherent, exhibit fibroblast-like morphology, and serve as a robust platform for haploid genetic screening, drug target identification, and pathway analysis.
DPY19L4 encodes a C-mannosyltransferase that catalyzes C-mannosylation of tryptophan residues in nascent proteins within the endoplasmic reticulum. Key substrates include thrombospondin type-1 repeat-containing proteins, and DPY19L4 cooperates with ER quality control components to ensure proper protein folding. Deficiency in this gene impairs glycosylation-dependent folding and is associated with idiopathic generalized epilepsy and neurodevelopmental disorders, highlighting its role in neuronal development.
The HAP1 haploid background provides a unique advantage for studying DPY19L4 loss, as it eliminates compensation from a second allele. This knockout model allows direct investigation of C-mannosylation defects on ER stress, protein processing, and cellular fitness. It is particularly suited for genetic interaction screens to uncover novel nodes in glycosylation pathways or synthetic lethal interactions.
Applications include assessing glycosylation status via Western blotting and lectin blotting, monitoring ER morphology by immunofluorescence, and measuring unfolded protein response markers by RT-qPCR. The cells also support apoptosis and drug sensitivity assays for disease modeling. They can be used in proteomic studies to identify novel C-mannosylated substrates. For more information, contact Ascent Research.
