The JAGN1 Knockout Jurkat Polyclonal Cells are a polyclonal population of Jurkat T lymphocytes generated by CRISPR/Cas9-mediated disruption of the JAGN1 gene. This product provides a loss-of-function model for studying the role of JAGN1 in endoplasmic reticulum (ER) homeostasis and N-glycosylation within a human T-cell context. The polyclonal format comprises a mixed pool of edited cells, offering robust and representative functional analysis without the biases associated with single-cell clones. These cells serve as a versatile tool for investigating ER stress pathways, glycosylation-dependent signaling, and immune cell function.
The host Jurkat cell line is an immortalized human T lymphocyte line originally derived from the peripheral blood of a 14-year-old male with acute T cell leukemia. Jurkat cells are extensively characterized and widely employed in T-cell signaling, apoptosis, and leukemia research due to their well-defined signaling networks and ease of genetic manipulation. Their suspension growth and authentic T-cell receptor signaling make them an ideal chassis for exploring the consequences of gene knockouts on lymphoid biology and oncogenic processes.
JAGN1 encodes an endoplasmic reticulum-resident protein that is essential for normal N-glycosylation and granulocyte differentiation. In Jurkat cells, JAGN1 disruption is predicted to impair N-glycan processing, leading to accumulation of misfolded proteins and activation of the unfolded protein response (UPR). Key UPR sensors??PERK, IRE1, and ATF6??transduce stress signals to downstream effectors such as GRP78/BiP, CHOP, and the spliced transcription factor XBP1, which orchestrate adaptive or apoptotic outcomes. JAGN1 interacts with ER chaperones including calnexin and calreticulin and functionally partners with glycosylation enzymes such as COSMC and C1GALT1, positioning it at the nexus of glycoprotein quality control.
Within the Jurkat T-cell context, loss of JAGN1 offers a unique model to dissect how ER stress and glycosylation defects influence lymphoid cell physiology and leukemogenesis. Given that JAGN1 mutations underlie severe congenital neutropenia and myelodysplastic syndrome, this knockout model may reveal conserved mechanisms linking ER dysfunction to immune cell survival and transformation. Altered glycosylation can modify cell-surface receptor expression and cytokine signaling, potentially impairing T-cell activation, proliferation, and apoptosis.
This knockout product is suited for a broad range of applications, including profiling UPR activation via western blotting for GRP78/BiP and CHOP, flow cytometric assessment of cell cycle and apoptosis, and RT-qPCR analysis of ER stress target genes. N-glycan profiling and immunofluorescence microscopy can delineate glycosylation alterations and ER morphological changes. The cells are also valuable for drug screening to identify ER stress modulators or glycosylation inhibitors, and for dissecting UPR signaling in leukemia using phospho-specific readouts for PERK and eIF2??. For additional details or custom inquiries, please contact Ascent Research.
