HSPA2 Knockout SK-HEP-1 Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population derived from the SK-HEP-1 human liver adenocarcinoma epithelial line via targeted HSPA2 gene disruption. As a polyclonal pool, this model provides a heterogeneous loss-of-function system that avoids clonal biases inherent to single-cell clones, enabling robust population-level interrogation of HSPA2 biology.
SK-HEP-1 cells, isolated from a liver adenocarcinoma, serve as a well-established adherent epithelial model for hepatocellular carcinoma research. This cell line retains key oncogenic properties and liver-specific pathways, making it ideal for studying tumor cell proteostasis, drug response, and stress adaptation mechanisms.
HSPA2 encodes a stress-inducible molecular chaperone of the HSP70 family that is transcriptionally upregulated by heat shock factor 1 (HSF1) under heat stress, oxidative stress, and hypoxia (via HIF1A). The protein cooperates with co-chaperones DNAJB1, BAG1, STIP1/HOP, and HSP90 to perform ATP-dependent folding and prevent aggregation of client proteins. Among its clients, HSPA2 stabilizes AKT and ERK kinases, which promote survival and proliferation signaling, and interacts with BCL2 family members to regulate apoptosis. Thus, HSPA2 integrates upstream stress signals with downstream survival and cell death decisions.
In SK-HEP-1 liver cancer cells, HSPA2 disruption compromises proteostasis and diminishes the chaperone??s ability to buffer oncogenic stress, leading to destabilization of AKT/ERK signaling and sensitization to apoptosis. This polyclonal knockout pool is therefore valuable for examining chaperone addiction in hepatocellular carcinoma, testing chemotherapeutic sensitivity, and exploring the mechanistic link between heat shock response and tumor cell survival.
This knockout model supports diverse experimental workflows, including western blotting and RT-qPCR for expression profiling, flow cytometry for apoptosis quantification, MTT-based proliferation assays, and co-immunoprecipitation to probe protein interactions. Heat shock response assays can directly assess stress-induced chaperone activity. Broad applications span cancer biology, protein homeostasis, stress signaling, and drug screening in liver cancer contexts. For additional details, contact Ascent Research.
