The B3GNT4 Knockout HeLa Polyclonal Cells product consists of a CRISPR/Cas9-edited polyclonal knockout cell population in which the B3GNT4 gene has been disrupted in the HeLa host cell line. This heterogeneous knockout model provides a robust system to investigate loss-of-function phenotypes of B3GNT4, a glycosyltransferase involved in poly-N-acetyllactosamine chain elongation. The polyclonal format avoids clonal selection artifacts and is ideal for population-level studies of glycosylation-dependent processes.
The host cell line HeLa is an immortalized human cervical adenocarcinoma cell line widely used as an epithelial model in cancer research. Its well-characterized signaling networks, high transfection efficiency, and rapid growth make it suitable for generating knockout models. The cervical adenocarcinoma origin offers a relevant context for studying glycosylation alterations in epithelial cancers, particularly those affecting cell surface glycoproteins.
B3GNT4 encodes a beta-1,3-N-acetylglucosaminyltransferase that transfers GlcNAc to beta-linked galactose residues on glycoconjugates, extending poly-N-acetyllactosamine chains. It interacts with UDP-GlcNAc, glycoprotein acceptors, and galactosyltransferases like B4GALT1. Upstream, B3GNT4 is regulated by TNF-alpha, IL-1beta, STAT3, and NF-kB; downstream, it modulates glycosylation of integrin beta1, E-cadherin, EGFR, and MUC1. This enzymatic activity influences protein stability, receptor signaling, and cell adhesion, linking B3GNT4 to pathways of O-glycan biosynthesis, N-glycan processing, and glycosphingolipid metabolism.
In HeLa cells, B3GNT4 disruption likely alters the glycosylation profile of key molecules, impacting proliferation, migration, and immune interactions. EGFR and integrin beta1, critical for cancer cell signaling and adhesion, are known carriers of polylactosamine chains. Knockout of B3GNT4 can help elucidate how defective chain elongation affects these receptors?? functions and downstream pathways, providing insights into cervical adenocarcinoma biology.
Research applications include cancer glycobiology, analysis of polylactosamine-mediated adhesion and signaling, study of glycosylation in immune evasion, and drug targeting of glycosyltransferases. The polyclonal population is compatible with lectin blotting, RT-qPCR, western blotting, migration/invasion assays, flow cytometry, and co-immunoprecipitation. It enables functional comparisons between wild-type and knockout populations. For additional information, please contact Ascent Research.
