The QTGAL Knockout HAP1 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from HAP1 cells. This heterogeneous pool harbors targeted disruptions in the QTGAL gene, offering a flexible loss-of-function model for glycobiology research. Because it avoids clonal selection, it captures a range of editing outcomes, making it suitable for population-level studies of galactosyltransferase function.
HAP1 is a near-haploid human cell line originating from KBM-7 chronic myeloid leukemia cells. It features adherent growth, p53 deficiency, and single-copy chromosomes that facilitate efficient CRISPR/Cas9 editing and genetic analysis. Its leukemic background preserves oncogenic signaling pathways relevant to cancer research, while p53 loss perturbs cell cycle control, providing a permissive system for studying glycosylation-related processes.
QTGAL is a putative galactosyltransferase that transfers galactose from UDP-galactose to glycoconjugates, participating in N-glycan, O-glycan, and glycosphingolipid biosynthesis. Upstream regulators include the SP1 transcription factor and nutrient-sensing mechanisms that modulate UDP-galactose availability. QTGAL interacts with the UDP-galactose transporter, glycosyltransferase families (B4GALT, ST3GAL, GALNT), and ER chaperones calnexin and calreticulin to ensure proper glycosylation. Downstream, QTGAL-mediated glycan modifications affect cell surface glycoproteins, glycolipids, and extracellular matrix components, thereby influencing cell adhesion, signaling, and immune recognition. Loss of QTGAL may therefore disrupt glycocalyx integrity and alter intercellular communication.
In the HAP1 leukemic context, QTGAL knockout enables dissection of glycosylation??s role in cancer. Aberrant glycosylation is a hallmark of malignancy, impacting proliferation, migration, and immune evasion. The near-haploid, p53-deficient background simplifies genetic manipulation and accentuates transformed phenotypes, while key metabolic enzymes like UGP2 and GALE connect QTGAL to galactose metabolism. This model can reveal how glycocalyx remodeling drives leukemogenesis and drug resistance.
These cells support applications such as lectin blotting, glycoprotein western blotting, flow cytometry with lectins, and mass spectrometry-based glycomic profiling to characterize glycan alterations. Functional assays like cell adhesion, migration, and invasion studies further probe QTGAL??s role in cancer cell behavior. The polyclonal format is also valuable for drug target discovery screens evaluating therapeutic vulnerabilities linked to glycosylation. For further information or ordering details, please contact Ascent Research.
