The HSPA7 Knockout HeLa Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population targeting the human HSPA7 gene. This loss-of-function model enables investigation of stress-inducible Hsp70 chaperone functions in a well-characterized cervical carcinoma background. The knockout product format provides a heterogeneous pool of gene-disrupted cells, facilitating robust analysis of HSPA7-dependent processes without clonal selection artifacts.
The HeLa cell line, derived from Henrietta Lacks’ cervical adenocarcinoma, is HPV18-positive and exhibits inactivation of the tumor suppressors p53 and pRb by the viral oncoproteins E6 and E7, respectively. These immortalized epithelial cells serve as a widely accepted model for human cancer biology, particularly for studies on viral oncogenesis, signal transduction, and cellular stress responses. The integration of the HPV18 genome provides a relevant context for examining interactions between viral proteins and host chaperone networks.
HSPA7 encodes a stress-inducible member of the Hsp70 chaperone family, transcriptionally activated by HSF1 in response to thermal stress, oxidative stress, heavy metals, and inflammatory cytokines. This chaperone assists in protein folding and refolding, prevents aggregation of misfolded proteins, and interacts with co-chaperones such as HSP40, BAG family proteins, HOP, and the ubiquitin ligase CHIP to guide substrates toward refolding or proteasomal degradation. Mechanistically, HSPA7 inhibits the pro-apoptotic factor BAX and prevents the release of AIF and activation of caspases, thereby maintaining cell viability under proteotoxic conditions.
In HeLa cells, disruption of HSPA7 compromises the heat shock response and unfolded protein response, leading to increased sensitivity to thermal and chemical proteotoxic insults. Given the HeLa background??s deficiency in p53 and pRb pathways, this knockout model is particularly suited to dissect p53-independent stress response mechanisms and evaluate the interplay between chaperone-mediated cytoprotection and apoptotic signaling in cancer cells. The model also provides a platform to explore how HSPA7 contributes to stress granule formation and MAPK signaling under conditions relevant to tumor microenvironments and cancer therapy resistance.
Researchers can utilize these cells for mechanistic studies of the heat shock response, proteostasis, and stress-induced apoptosis using assays such as Western blotting, RT-qPCR for heat shock genes, cell viability tests under stress, Annexin V staining, and protein aggregation assays. The polyclonal knockout population supports the development and testing of chaperone-targeted therapeutic strategies for cancer and neurodegenerative diseases. For further information, please contact Ascent Research.
