The BAG2 Knockout HeLa Polyclonal Cells product is a CRISPR/Cas9-edited polyclonal knockout cell population derived from HeLa cells with targeted disruption of the BAG2 gene. This loss-of-function model enables investigation of the BAG2 co-chaperone, a key factor in protein quality control and apoptosis. The polyclonal format avoids clonal selection bias and provides a robust heterogeneous pool for functional genomic studies in proteostasis, oncology, and neurobiology.
The host HeLa cell line is a widely utilized human cervical adenocarcinoma epithelial cell model isolated in 1951. These cells are immortalized and positive for HPV18, expressing E6 and E7 oncoproteins that inactivate p53 and pRb. Their rapid proliferation, ease of transfection, and aneuploid karyotype make them a preferred substrate for gene editing and phenotypic assays. The cervical cancer origin offers an ideal background to examine BAG2 in oncogenic and proteotoxic stress contexts.
BAG2 acts as a co-chaperone that binds Hsp70/Hsc70 and the 26S proteasome, inhibiting CHIP (STUB1)-mediated ubiquitination and degradation of misfolded substrates. This stabilizes aggregation-prone proteins, including tau, polyglutamine-expanded proteins, and mutant huntingtin, potentially exacerbating proteotoxicity. BAG2 also modulates apoptosis through interactions with Bcl-2 family members and caspase-3. Upstream, HSF1 and proteotoxic stress (including TNF?? and IL-1??) regulate BAG2 expression. Downstream, BAG2 influences chaperone-mediated autophagy, interacting with p62/SQSTM1 and LC3, and functionally competes with BAG3 for Hsp70 binding, thereby governing protein triage.
In HeLa cells, BAG2 knockout is predicted to enhance CHIP-mediated ubiquitination and proteasomal clearance of substrates, while potentially sensitizing cells to apoptosis. The HPV18-transformed background provides a clean platform to dissect BAG2-dependent effects on protein aggregation, autophagy flux, and cell survival without neuronal lineage confounders. This model may also reveal altered sensitivity to proteasome inhibitors such as bortezomib, linking proteostasis to cancer cell vulnerability.
This polyclonal knockout product is suited for diverse assays including western blotting, ubiquitination assays, proteasome activity measurements, and immunofluorescence for protein aggregates. It supports functional analyses such as MTT viability tests, Annexin V apoptosis detection, LC3 puncta evaluation, and drug sensitivity screening with proteasome inhibitors. Applications include neurodegenerative disease modeling, proteostasis research, and drug response profiling. For more information, contact Ascent Research.
