The HS3ST1 Knockout Ca Ski Polyclonal Cells product comprises a CRISPR/Cas9-edited polyclonal population of Ca Ski human cervical epithelial carcinoma cells carrying a targeted disruption of the HS3ST1 gene. This loss-of-function model eliminates the expression of heparan sulfate 3-O-sulfotransferase 1, enabling researchers to study the biological consequences of abrogating 3-O-sulfation of heparan sulfate in a well-characterized HPV-16-positive cervical cancer background. The polyclonal nature preserves population-level heterogeneity while ensuring robust gene knockout across the cell pool, making it suitable for functional genomics studies that do not require clonal isolation.
The parental Ca Ski cell line was established from a metastatic cervical epidermoid carcinoma deposit in the mesentery of a patient. These adherent epithelial cells harbor integrated human papillomavirus type 16 (HPV-16) genomes and express viral oncoproteins E6 and E7, which inactivate p53 and retinoblastoma protein, respectively. Ca Ski cells are widely employed as a model system for HPV-associated cervical carcinogenesis, tumor biology, and preclinical drug screening. Their relevance extends to studies of viral-host interactions, oncogenic signaling, and therapeutic response evaluation.
HS3ST1 is a sulfotransferase that catalyzes the transfer of sulfate groups from the cofactor 3′-phosphoadenosine-5′-phosphosulfate (PAPS) to the 3-O position of glucosamine residues within heparan sulfate chains. This rare modification generates high-affinity binding sites for antithrombin, a serpin that inhibits coagulation factors thrombin and factor Xa, thereby amplifying anticoagulant activity. Additionally, 3-O-sulfated heparan sulfate modulates interactions with growth factors such as FGF2 and VEGF, influencing proliferative signaling downstream of FGFR1. The HS3ST1-dependent sulfation pattern also serves as a critical attachment receptor for herpes simplex virus type 1 (HSV-1) glycoprotein D, facilitating viral entry and cell-to-cell spread. Thus, HS3ST1 integrates functions across hemostasis, growth factor signaling, and viral infectivity.
In the context of Ca Ski cervical carcinoma cells, HS3ST1 disruption allows dissection of how heparan sulfate fine structure controls malignancy-associated phenotypes. Since HPV oncoproteins drive uncontrolled proliferation, the loss of 3-O-sulfation may alter FGF2-mediated mitogenic signaling, affecting tumor cell growth and migration. Moreover, Ca Ski cells express abundant heparan sulfate proteoglycans, making them an ideal platform to examine changes in extracellular matrix ligand presentation and viral susceptibility. Investigation of HS3ST1 knockout in this disease-relevant model can reveal novel links between glycosaminoglycan modifications and cervical cancer progression, while also providing a tool to explore antithrombotic mechanisms in a transformed epithelial environment.
This polyclonal knockout population enables glycomic profiling to confirm altered sulfation patterns and functional assays such as antithrombin binding and thrombin inhibition. Growth factor signaling can be assessed by phospho-ERK activation upon FGF2 stimulation, and cell migration by wound-healing assays. HSV-1 infectivity assays quantify heparan sulfate-dependent viral entry. The model also supports drug screening for sulfation modulators. For additional information, customization, or technical support, please contact Ascent Research.
