The HS3ST1 Knockout KYSE-150 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population derived from the human KYSE-150 esophageal squamous cell carcinoma line. This product provides a genetically heterogeneous pool carrying targeted HS3ST1 disruptions, enabling robust loss-of-function analyses without clonal selection artifacts. The polyclonal format retains natural genetic variability while effectively ablating HS3ST1 function, making it suitable for pooled screens and reproducible phenotypic assessments.
The parental KYSE-150 cell line originates from a poorly differentiated esophageal squamous cell carcinoma, a malignancy with aggressive invasion and high metastatic potential. Widely used as an in vitro model, KYSE-150 cells recapitulate deregulated growth factor signaling, altered adhesion, and invasive capacity. Their epithelial origin and cancer properties make them ideal for studying sulfotransferase contributions to tumor progression and associated pathophysiology.
HS3ST1 encodes a heparan sulfate 3-O-sulfotransferase that transfers sulfate from 3′-phosphoadenosine-5′-phosphosulfate (PAPS) to glucosamine residues of heparan sulfate proteoglycans. This modification generates high-affinity binding sites for antithrombin, accelerating the inhibition of thrombin and factor Xa. 3-O-sulfated heparan sulfate also serves as an essential entry receptor for HSV-1 by interacting with glycoprotein D. HS3ST1 activity is influenced by upstream FGF and TGF-?? signals, and the enzyme functions within glycosyltransferase complexes. Downstream consequences include antithrombin activation, modulation of FGF2 signaling, and viral infectivity, placing HS3ST1 at a critical node in hemostasis and host?Cpathogen interactions.
In KYSE-150 cells, HS3ST1 knockout disrupts the sulfation code of heparan sulfate, which orchestrates growth factor receptor binding and protease regulation. Loss of 3-O-sulfation may attenuate oncogenic signaling downstream of FGF and TGF-?? receptors, reducing proliferation, migration, and invasion. Additionally, abrogation of antithrombin-binding sites may alter pericellular coagulation, offering insight into the metastatic niche?Cthrombosis interplay. This model provides a powerful system to dissect sulfotransferase contributions to esophageal cancer phenotypes.
Researchers can use this knockout pool in diverse applications. Coagulation studies may employ aPTT, PT, and antithrombin binding assays to quantify loss of anticoagulant heparan sulfate. Virologists can validate eliminated HSV-1 susceptibility using entry assays. Cancer biology investigations can rely on migration and invasion assays, immunofluorescence, and western blotting for EMT markers. LC-MS analysis permits precise quantification of sulfation patterns. For further information, please contact Ascent Research.
