Jurkat Fc Receptor Cells
Jurkat Fc Receptor Cells - Related Videos
03:32
An In Vitro Artificial Activation Assay for Studying Fc Receptor Activation by Antibodies
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This video demonstrates FcγRIIIa-driven events initiated by therapeutic antibodies in human natural killer cells. The artificial stimulation platform facilitates the exploration of downstream effector functions, encompassing cytoskeletal rearrangement, degranulation, chemokine/cytokine production, and signaling pathways mediated by the FcγRIIIa and Fc portions of antibodies involved in binding.
03:03
Measuring the Activation of Fc-Mediated Effector Functions by HA Antibodies
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This video demonstrates an assay measuring the antibody-mediated activation of T cell effector functions. Adding an influenza virus hemagglutinin (HA)-specific monoclonal antibody to transfected mammalian cells expressing HA results in the formation of immune complexes with HA. Upon introducing engineered T cells expressing Fc receptors and a luciferase reporter, the T cells are activated by the antibody-HA complexes, and this activation is detected by adding a luciferase substrate and...
04:47
A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies
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Cited by 6 •
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We describe a method to measure the activation of Fc-mediated effector functions by antibodies that target the influenza virus hemagglutinin. This assay can also be adapted to assess the ability of monoclonal antibodies or polyclonal sera targeting other viral surface glycoproteins to induce Fc-mediated immunity.
09:20
Rapid In Vitro Cytotoxicity Evaluation of Jurkat Expressing Chimeric Antigen Receptor using Fluorescent Imaging
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Cited by 3 •
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A protocol to evaluate quantitative tumor cell killing by Jurkat cells expressing chimeric antigen receptor (CAR) targeting single tumor antigen. This protocol can be used as a screening platform for rapid optimization of CAR hinge constructs prior to confirmation in peripheral blood-derived T cells.
08:48
Generating De Novo Antigen-specific Human T Cell Receptors by Retroviral Transduction of Centric Hemichain
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Cited by 3 •
2016
Herein we describe a novel method to generate antigen-specific T cell receptors (TCRs) by pairing the TCRα or TCRβ of an existing TCR, possessing the antigen-specificity of interest, with complementary hemichain of the peripheral T cell receptor repertoire. The de novo generated TCRs retain antigen-specificity with varying affinity.
FAQs
Fc-receptor cross-linking, rather than simple antibody binding, initiates the measurable response. Antibody-coated targets or immune complexes bring neighboring receptors together, activating intracellular signaling that reaches an NFAT-controlled transcriptional reporter. Luciferase output then provides a quantitative signal for comparing receptor engagement and downstream pathway activation under the tested conditions.
These cells separate antibody recognition from the intracellular readout. Fc receptors provide the binding interface for antibody-coated targets or immune complexes, while NFAT-driven luciferase reports signaling after receptor clustering. This arrangement lets investigators examine Fc-receptor engagement as a functional pathway, rather than treating antibody presence alone as evidence of immune effector activity.
These engineered lines offer a standardized, reproducible framework for measuring antibody-driven Fc-receptor responses without relying solely on primary immune cells. That distinction matters when investigators need to compare antibody functions or therapeutic potency under a consistent assay design. Their use does not replace biological studies, but provides a controlled complement to them.
An NFAT-driven luciferase signal indicates that receptor engagement has propagated into intracellular transcriptional signaling. It therefore serves as a quantifiable downstream readout, not a direct measurement of every immune function. In practice, stronger or weaker reporter responses can be used to compare conditions or antibody activities within the assay, while interpretation remains tied to Fc-receptor pathway activation.
A basic assay workflow begins with antibody-coated targets or immune complexes, followed by exposure to cells bearing Fc receptors. Binding and receptor cross-linking activate intracellular signaling, which drives the transcriptional reporter. The resulting luciferase signal is quantified and interpreted as evidence of Fc-receptor pathway activation, allowing antibody samples or conditions to be compared in a standardized format.
These cells are useful when the question concerns antibody-dependent cellular cytotoxicity or Fc-receptor engagement rather than antibody binding in isolation. Their reporter response supplies a measurable functional endpoint for comparing antibody activities and evaluating therapeutic antibody potency. Because the system does not rely solely on primary immune cells, it can provide a consistent platform for such comparative studies.
In infection and vaccine research, the assay can help characterize how antibody responses may contribute to host defense. Researchers can compare antibodies or immune complexes through their ability to engage Fc-receptor signaling, then use those measurements alongside studies of vaccine or antibody-based treatment performance. The result is functional context for immune responses, not merely a record of antibody presence.