The IGHMBP2 Knockout HT29 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population derived from the human HT29 colorectal adenocarcinoma cell line. This product enables loss-of-function studies of the IGHMBP2 gene, which encodes an ATP-dependent helicase involved in ribosome biogenesis, DNA repair, and stress granule dynamics. The polyclonal pool comprises a genetically heterogeneous mixture of HT29 cells carrying disruptions within IGHMBP2, providing a versatile tool that avoids clonal selection biases.
HT29 cells, isolated from a human colorectal adenocarcinoma, display adherent epithelial morphology and are widely used to model intestinal epithelial differentiation and colorectal cancer. They retain a moderate differentiation phenotype and express key intestinal markers, making them suitable for dissecting signaling pathways governing epithelial homeostasis and oncogenesis. Their robust handling and rapid proliferation facilitate CRISPR-based knockout studies and functional validation.
IGHMBP2 is an ATP-dependent helicase that preferentially binds structured RNA/DNA substrates. Upstream, it is regulated by c-Myc and mTORC1 signaling. It interacts with ribosomal proteins, G3BP1, and TIA-1 within stress granules, mediating ribosome assembly and translation of mRNAs with highly structured 5?? UTRs. IGHMBP2 acts downstream of mTORC1 to modulate stress granule dynamics in concert with G3BP1 and TIA-1. Additionally, it participates in DNA damage signaling, where its ATPase activity promotes resolution of secondary structures at stalled replication forks, thereby influencing cell survival under stress and proteostasis.
In HT29 cells, IGHMBP2 disruption impairs ribosome biogenesis and sensitizes cells to stress-induced damage, providing a platform to study SMARD1 and CMT2S pathology. As HT29 cells are a colorectal cancer model, this knockout also enables exploration of IGHMBP2??s role in tumor cell proliferation, survival, and stress adaptation. The polyclonal population mimics genetic heterogeneity, offering insight into how diverse IGHMBP2 mutations impact cancer cell fitness and drug response.
Applications include investigating ribosome biogenesis defects via ribosome profiling, studying stress granule dynamics by immunofluorescence, and modeling neurodegenerative mechanisms with apoptosis assays. Cancer biology studies can employ proliferation and drug sensitivity screens. Validation methods include Western blotting, RT-qPCR, flow cytometry, and RNA-seq. For details or ordering, contact Ascent Research.
