The B4GALT1 Knockout HAP1 Polyclonal Cells product comprises a CRISPR/Cas9-edited polyclonal population of HAP1 cells carrying a targeted disruption of the B4GALT1 gene. This loss-of-function model enables systematic investigation of beta-1,4-galactosyltransferase 1 in a human near-haploid background. The polyclonal format provides a diverse allelic representation for downstream functional genomics and screening applications, avoiding the biases of single-cell clonal expansion while maintaining robust knockout representation.
HAP1 is a chronic myeloid leukemia-derived cell line with a near-haploid karyotype, adherent fibroblast-like morphology, and expression of the BCR-ABL1 fusion oncogene. Its haploid nature facilitates efficient gene targeting and simplifies genotype?Cphenotype correlations, making it a widely adopted model for genetic screens and CRISPR-based functional studies. The line??s adherent growth supports cell-based assays requiring stable monolayer cultures, including adhesion, migration, and proliferation measurements.
B4GALT1 encodes a Golgi-resident glycosyltransferase that catalyzes the transfer of galactose from UDP-galactose to terminal N-acetylglucosamine residues, forming ??1,4-linkages in N- and O-glycans and glycolipids. In the mammary gland, its interaction with the cofactor alpha-lactalbumin redirects substrate specificity toward glucose to produce lactose. B4GALT1 expression is regulated by transcription factors such as CREB and ELF3 and by hormonal cues including prolactin and glucocorticoids. Downstream, B4GALT1-dependent galactosylation modifies glycoproteins like laminin and integrins, generates lactosylceramide, and controls terminal glycan structures that mediate cell?Ccell and cell?Cmatrix interactions. The enzyme also functionally cooperates with other glycosyltransferases, including ST6GAL1. Disruption of B4GALT1 therefore perturbs glycoconjugate biosynthesis and alters the glycan landscape critical for cellular recognition, signaling, and adhesion.
In the HAP1 background, B4GALT1 knockout provides a simplified system to dissect glycosylation-dependent phenotypes without the confounding effects of diploid compensation. Because HAP1 cells already harbor oncogenic BCR-ABL1 signaling, they are particularly suited for studying how altered glycosylation contributes to cancer cell adhesion, immune evasion, and metastatic potential. Loss of B4GALT1 is expected to impair galactosylation of surface receptors and extracellular matrix proteins, thereby modulating integrin-mediated adhesion, cell migration, and proliferation. This makes the model valuable for cancer glycosylation research and for validating B4GALT1 as a potential therapeutic target in malignancies where aberrant glycosylation drives progression.
Researchers can employ this polyclonal knockout panel in a wide range of experiments. Glycan profiling by lectin blotting with RCA-I or mass spectrometry glycomics directly assesses galactosylation changes. Functional assays such as cell adhesion and proliferation assays quantify phenotypic consequences of impaired glycosylation. The line is also ideal for CRISPR off-target analysis and transcriptomic studies via RNA-seq to uncover global gene expression changes linked to glycan remodeling. Moreover, it supports drug target validation and synthetic lethal screens in the context of congenital disorders of glycosylation. For additional technical details or to discuss custom applications, please contact Ascent Research.
