In Stock Cell Lines
Mus musculus (Mouse)
Pancreas (pancreatic duct)
Adherent
The B3gnt4 Knockout PANC02 Cell Line is a CRISPR/Cas9-edited murine pancreatic cancer cell line lacking functional B3gnt4 glycosyltransferase. Derived from the syngeneic C57BL/6 PANC02 model, this knockout enables interrogation of how B3gnt4-mediated glycosylation of targets such as integrin beta1 and EGFR regulates tumor cell adhesion, migration, and metastasis. Researchers can use this line to study glycosylation-dependent mechanisms in pancreatic cancer progression, perform in vitro migration/invasion assays, and assess tumor growth in immunocompetent mouse models, supporting preclinical drug testing and metastasis research.
BARX2 Knockout HAP1 Polyclonal Cells
Cat. No. ARG22048
LZTS2 Knockout NCI-H1975 Polyclonal Cells
Cat. No. ARG17114
FGFR1 Knockout CAL27 Polyclonal Cells
Cat. No. ARG11639
BCL7B Knockout SK-HEP-1 Polyclonal Cells
Cat. No. ARG32354
DMPK Knockout HEK293T Polyclonal Cells
Cat. No. ARG38981
EXOSC1 Knockout HEK293T Polyclonal Cells
Cat. No. ARG3614
The B3gnt4 Knockout PANC02 Cell Line is a genetically engineered murine pancreatic cancer cell line with CRISPR/Cas9-mediated disruption of the B3gnt4 gene. This knockout model enables loss-of-function studies of beta-1,3-N-acetylglucosaminyltransferase 4 in a syngeneic C57BL/6-derived background. The stable edited cell population provides a consistent platform for examining the impact of altered glycosylation on tumor cell behavior without the need for continuous selection.
The parental PANC02 cell line originates from a C57BL/6 mouse pancreatic adenocarcinoma and serves as a widely used syngeneic model for pancreatic cancer research. It recapitulates key features of human disease, including Kras-driven signaling, and supports tumor growth in immunocompetent hosts. This background is particularly valuable for studying tumor?Cimmune interactions and testing immunotherapies in a physiologically relevant setting.
B3gnt4 encodes a Golgi glycosyltransferase that transfers N-acetylglucosamine to galactose residues on glycoproteins and glycolipids, forming polylactosamine chains. Its activity is regulated upstream by KRAS and EGFR signaling and influences downstream targets such as integrin beta1 and EGFR through glycan modification. The enzyme functions within glycosphingolipid biosynthesis and N-/O-glycan processing pathways, using UDP-N-acetylglucosamine to extend lactosylceramide-based glycans. It interacts with molecular chaperones and other glycosyltransferases in the Golgi. Disruption of B3gnt4 removes this catalytic function, leading to truncated glycans on adhesion receptors and altered signal transduction, which may impair cell adhesion and migration.
In PANC02 cells, B3gnt4 knockout disrupts glycosylation patterns critical for tumor cell?Cmatrix interactions and metastatic potential. This model permits analysis of how glycan-dependent adhesion and signaling contribute to pancreatic cancer progression in a syngeneic, immune-competent environment. Researchers can thus delineate the role of B3gnt4 in immune evasion and evaluate whether targeting this glycosyltransferase represents a therapeutic strategy.
Typical applications include confirming knockout by RT-qPCR and western blot, assessing glycosylation changes via lectin flow cytometry, and measuring migration/invasion using Transwell assays. In vivo syngeneic tumor models in C57BL/6 mice allow investigation of primary tumor growth and metastasis. The line is also suitable for preclinical drug testing to explore responses in a glycosylation-deficient context. For further technical details, please contact Ascent Research.
