The GOLGB1 Knockout HT29 Polyclonal Cells product is a CRISPR/Cas9-edited polyclonal cell population derived from HT29 human colorectal adenocarcinoma epithelial cells. This pool harbors targeted disruptions in the GOLGB1 gene, leading to loss of giantin function, and is provided without clonal selection, thereby capturing phenotypic diversity while enabling robust loss-of-function studies. The polyclonal format reduces the influence of individual clone variability and is particularly suitable for assays where population-level responses are critical.
HT29 is a well-characterized epithelial cell line originally isolated from a colorectal adenocarcinoma. It retains mutant p53 expression and constitutively produces mucins, and can be induced to differentiate into enterocyte- and mucus-secreting phenotypes, making it a valuable model of the intestinal epithelium. This background is extensively used in colorectal cancer research, mucin biology, and glycobiology.
GOLGB1 encodes the giantin protein, a key component of the Golgi matrix that maintains stack organization through interactions with GM130 (GOLGA2) and the vesicle tethering factor p115 (USO1). Giantin functions downstream of PKA-mediated phosphorylation and Golgi stress signals, and acts upstream of glycosyltransferases and secretory cargo receptors. It is essential for COPI- and COPII-vesicle tethering at the Golgi, and its disruption leads to Golgi ribbon fragmentation, impaired N- and O-glycosylation, and altered secretory trafficking.
In the HT29 adenocarcinoma context, where Golgi integrity affects tumor cell secretion, migration, and drug resistance, GOLGB1 knockout enables mechanistic dissection of these processes. The polyclonal knockout population circumvents clonal biases and reflects the heterogeneity intrinsic to cancer cell phenotypes. This system is therefore highly relevant for studying Golgi fragmentation disorders and congenital disorders of glycosylation, as well as for exploring how giantin loss influences colorectal cancer progression.
Routine applications include immunofluorescence analysis of Golgi morphology using giantin and GM130 markers, lectin-based glycosylation profiling to detect glycan alterations, and secretion assays with alkaline phosphatase reporters. Additionally, cell migration and drug sensitivity screens can be performed to assess the functional consequences of giantin depletion. For technical inquiries regarding this product, please contact Ascent Research.
