The DNAJA2 Knockout Jurkat Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population engineered for the disruption of the DNAJA2 gene in Jurkat cells. This mixed population model provides a flexible loss-of-function system for investigating DNAJA2-dependent processes without the need for single-cell cloning. The knockout was achieved through CRISPR/Cas9-mediated gene disruption, resulting in a heterogeneous cell pool that enables robust functional studies of DNAJA2 biology in a T-cell context.
Jurkat cells are an immortalized human T lymphocyte line derived from a 14-year-old male with acute T cell leukemia. They serve as a widely used model system for studying T cell signaling, activation, and apoptosis, as well as cancer biology. Their robust growth characteristics and well-characterized signaling pathways make them ideal for examining the roles of co-chaperones like DNAJA2 in immune cell function and stress responses.
DNAJA2 is a J-domain co-chaperone that partners with Hsp70 family proteins (HSPA1A/HSPA8 and Hsc70) to stimulate ATP hydrolysis, thereby facilitating protein folding, translocation, and degradation. It is a critical component of the protein homeostasis network, linking the Hsp70 chaperone cycle to the ubiquitin-proteasome system. DNAJA2 expression is regulated by HSF1 transcription factor in response to heat shock, oxidative stress, and the unfolded protein response. Upon activation, DNAJA2 recruits Hsp70 to client proteins??including misfolded and aggregation-prone species??and in concert with ubiquitin ligases and proteasomal subunits, directs substrates for proteasomal degradation. Through these interactions, DNAJA2 maintains cellular proteostasis and modulates stress signaling pathways.
In Jurkat T cells, disruption of DNAJA2 is expected to impair the Hsp70 chaperone cycle, leading to accumulation of misfolded proteins and compromised stress responses. Given the heavy reliance of rapidly dividing leukemia cells on efficient protein folding and degradation, DNAJA2 knockout may sensitize these cells to proteotoxic stress, affect T cell receptor signaling cascades, and alter apoptotic thresholds. This model thus provides a valuable platform for dissecting the interplay between chaperone networks and malignant T cell biology.
This polyclonal knockout cell population is ideally suited for a range of applications in protein homeostasis research, including analysis of Hsp70 co-chaperone function, proteasome activity assays, and protein aggregation studies. It can be used to investigate cancer cell stress responses, screen for modulators of proteostasis, and examine T cell activation pathways via flow cytometry or Western blot-based approaches. Co-immunoprecipitation experiments may reveal altered interactions between Hsp70 and client proteins. Additionally, the cells enable functional assays for apoptosis and survival signaling under stress conditions. For further information or to discuss customization options, please contact Ascent Research.
