The B4GALT1 Knockout NCI-H1703 Polyclonal Cells product provides a CRISPR/Cas9-edited polyclonal population of NCI-H1703 human lung squamous cell carcinoma cells with targeted disruption of the B4GALT1 gene. This loss-of-function model offers a consistent polyclonal knockout background without single-cell cloning, suitable for studying the glycosylation-dependent roles of beta-1,4-galactosyltransferase 1.
Derived from a human lung squamous cell carcinoma, NCI-H1703 cells are a standard model for this cancer subtype, widely used to explore molecular mechanisms of tumorigenesis, metastasis, and therapeutic resistance. Their well-characterized adhesive and migratory properties, alongside known genomic alterations, make them an ideal host for examining glycosylation changes relevant to squamous cell carcinoma progression.
B4GALT1 encodes beta-1,4-galactosyltransferase 1, which catalyzes the addition of galactose to N-acetylglucosamine on glycoproteins and glycolipids, forming the Gal??1-4GlcNAc linkage. This reaction is pivotal in N-glycan, O-glycan, and glycosphingolipid biosynthesis, and generates ligands for galectins. B4GALT1 is transcriptionally regulated by Sp1 and CREB1, and interacts with alpha-lactalbumin (LALBA) as well as the UDP-galactose transporter SLC35A2. In the glycosylation network, it cooperates with ST6GAL1, MGAT5, and LGALS1 (galectin-1). Disruption of B4GALT1 eliminates this galactosylation step, leading to truncated glycans that alter downstream signaling through adhesion molecules and growth factor receptors.
In NCI-H1703 cells, loss of B4GALT1 impairs glycosylation of key proteins such as integrin ??1, E-cadherin, and EGFR, reducing galectin-mediated signaling and potentially weakening cell adhesion, migration, and receptor activation. This knockout model thus enables dissection of B4GALT1’s role in lung cancer metastasis, cell?Ccell interactions, and galectin-dependent processes. It is also pertinent to congenital disorders of glycosylation and the study of glycan alterations in drug resistance.
Research applications include lectin blotting (RCA I, L-PHA), flow cytometric glycan analysis, adhesion and transwell migration assays, proliferation studies, and mass spectrometric glycomic profiling. The product is well suited for investigating glycoprotein ligand identification and galectin-mediated signaling pathways in lung squamous cell carcinoma. For further details, please contact Ascent Research.
