HSPA4L Knockout HT29 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human colorectal adenocarcinoma cell line HT29. This product features disruption of the HSPA4L gene using CRISPR/Cas9-mediated gene editing, creating a heterogeneous pool of cells with targeted loss-of-function modifications. The polyclonal format provides a flexible tool for studying HSPA4L function without the constraints of clonal selection, making it suitable for a broad range of functional assays in stress biology and cancer research.
The HT29 cell line is a well-established model of human colorectal adenocarcinoma, isolated from a primary tumor of a 44-year-old Caucasian female. HT29 cells exhibit epithelial morphology and retain several characteristics of intestinal epithelial cells, including the ability to differentiate under specific conditions. Widely used in cancer research, drug screening, and studies of epithelial cell differentiation and tumorigenesis, this cell line provides a physiologically relevant context for investigating colorectal cancer molecular mechanisms.
HSPA4L encodes an Hsp70 family chaperone that plays a critical role in protein folding and cellular stress responses. The protein is regulated by heat shock factor 1 (HSF1) and is activated by heat stress and oxidative stress. HSPA4L interacts with co-chaperones including DNAJB1, BAG3, STUB1, and HSPA8, and operates within the HSF1-mediated heat shock response pathway alongside HSPA1A and HSP90AA1. Mechanistically, HSPA4L facilitates the refolding of denatured proteins and modulates apoptotic signaling, thereby protecting cells from stress-induced apoptosis through interactions with these co-chaperone partners.
In the context of HT29 colorectal adenocarcinoma cells, HSPA4L knockout provides a powerful system to dissect the role of chaperone-mediated protein homeostasis in cancer cell survival and stress adaptation. Colorectal cancer cells frequently encounter proteotoxic stress due to rapid proliferation and genomic instability, relying on heat shock proteins for survival. Disruption of HSPA4L in this model enables investigation of its contribution to drug resistance mechanisms, apoptotic regulation, and the cellular response to therapeutic stressors such as chemotherapeutic agents.
Researchers can employ this HSPA4L polyclonal knockout cell population in diverse functional assays. Typical applications include assessing cell viability under heat stress or chemotherapeutic insult, monitoring apoptotic induction via Annexin V flow cytometry, and analyzing stress-induced gene expression changes by RT-qPCR or Western blotting. Co-immunoprecipitation experiments can further elucidate altered interactions with co-chaperones like DNAJB1 and BAG3. These cells are also suitable for studying the impact of HSPA4L loss on colorectal cancer cell signaling and for screening compounds that target heat shock response pathways. For further information, please contact Ascent Research.
