The BAG2 Knockout Jurkat Polyclonal Cells are a CRISPR/Cas9-edited polyclonal population derived from the human Jurkat T-lymphocyte line, designed to disrupt the BAG2 gene. This product provides a loss-of-function model for investigating the roles of the BAG2 co-chaperone in protein quality control and apoptosis. The polyclonal format ensures a heterogeneous knockout, enabling robust population-level analyses without isolation of single-cell clones.
Jurkat cells are an immortalized T-cell line originally established from acute T-cell leukemia and are widely employed in studies of T-cell receptor signaling, apoptosis, and HIV infection. The E6-1 clone maintains a lymphoblastoid phenotype and exhibits well-characterized responses to stress and apoptotic stimuli, making it an ideal host for examining BAG2-mediated regulatory mechanisms.
BAG2 functions as a nucleotide-exchange-independent co-chaperone that interacts with HSPA1A (Hsp70) and the 19S proteasome subunit PSMC1, facilitating the delivery of ubiquitinated clients for degradation. It is regulated by HSF1 under heat shock and oxidative stress and acts upstream of tau (MAPT) clearance and caspase-3 activation. BAG2 forms complexes with CHIP/STUB1 and associates with BCL2 family members, thereby integrating protein folding and degradation with cell survival decisions.
In Jurkat T lymphocytes, BAG2??s involvement in proteasome-mediated proteolysis and apoptosis signaling is particularly pertinent, as these cells rely on tightly controlled apoptotic programs for immune function and cancer transformation. Disruption of BAG2 can reveal dependencies on chaperone-assisted degradation under proteotoxic stress, providing insights into how leukemic cells manage misfolded proteins and evade apoptosis.
Researchers can utilize these polyclonal knockout cells to dissect the HSPA1A/BAG2/PSMC1 axis using co-immunoprecipitation, measure proteasome activity with fluorogenic substrates, and monitor apoptosis via Annexin V/PI flow cytometry. Western blotting for phospho-tau or other aggregation-prone proteins can assess client processing, while immunofluorescence detects protein aggregates. The model supports investigations into neurodegenerative proteinopathies, ubiquitin-proteasome system dynamics, and stress response pathways in cancer. For additional technical information, please contact Ascent Research.
