The HSPA1A Knockout HeLa Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population targeting HSPA1A in the HeLa cell line. As a heterogeneous pool, these cells provide a loss-of-function model that avoids clonal biases while enabling robust analysis of gene disruption effects. The product is supplied as a ready-to-use polyclonal pool, generated through CRISPR/Cas9-mediated gene disruption, and is suitable for a range of biomedical applications without the need for monoclonal isolation.
The HeLa host cell line is an immortalized cervical epithelial cell line derived from cervical adenocarcinoma, positive for HPV18, and exhibits aneuploidy. Widely adopted in cancer research, HeLa cells offer high transfection efficiency and a well-characterized background ideal for studying gene function in malignancy-associated pathways. Their aggressive growth phenotype and extensive use in signaling and pharmacological studies make them a relevant context for HSPA1A knockout investigations.
HSPA1A encodes HSP70-1A, a stress-inducible molecular chaperone essential for protein folding, refolding, and degradation. Its expression is under the control of HSF1, NF-??B, p53, ATF1, CREB, and estrogen receptor. HSP70 interacts with co-chaperones including HSP40/DNAJ, BAG1, BAG3, CHIP/STUB1, HOP, and HIP, and binds Apaf-1 to inhibit apoptosome assembly, thereby suppressing caspase-9 and caspase-3 activation. It also modulates Bcl-2 and Bax stability and influences JNK signaling, positioning HSP70 as a critical node linking proteostasis and apoptosis.
Knockout of HSPA1A in HeLa cells disrupts HSP70-mediated protein quality control, leading to increased protein aggregation and enhanced apoptosis under stress. Loss of HSP70 sensitizes cells to chemotherapeutic agents such as cisplatin and proteasome inhibitors like bortezomib, reflecting its role in drug resistance. This polyclonal model enables the study of how HSP70 dysfunction impacts oncogenic signaling, proteotoxic stress, and apoptotic threshold in cervical carcinoma.
Typical applications include Western blotting for HSP70, HSF1, and cleaved caspase-3; RT-qPCR for HSPA1A, HSPA1B, and DNAJB1; cell viability assays under heat stress; Annexin V flow cytometry; proteasome activity measurement; and co-immunoprecipitation of HSP70 interactors. Drug sensitivity profiling further supports chemoresistance research. For additional information or technical support, please contact Ascent Research.
