Jagged1-fc

Jagged1-Fc is a recombinant fusion protein that combines the Notch ligand Jagged1 with an antibody Fc domain, providing a controlled tool for studying Notch signaling in developmental biology. When immobilized on a culture surface, Jagged1-Fc engages Notch receptors on neighboring cells and promotes receptor cleavage, releasing the Notch intracellular domain, which enters the nucleus and regulates target gene expression. Researchers use this reagent to manipulate cell fate, differentiation, tissue patterning, and developmental signaling in cultured cells and organoid models. Its defined presentation of Jagged1 helps clarify how ligand-receptor interactions influence development and disease-related cellular behavior.

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Research

JoVE EoE - Antibody-Based Technologies

Measuring the Activation of Fc-Mediated Effector Functions by HA Antibodies

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2025

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...

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow

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Cited by 3 •

2014

Compared with traditional affinity chromatography using protein A agarose bead-packed columns, protein A membrane adsorbers can significantly speed laboratory-scale isolation of antibodies and other Fc fragment-expressing proteins. Appropriate analysis and quantification methods can further accelerate protein processing, allowing isolation/characterization to be completed in one workday, instead of 20+ work hours.

A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies

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Cited by 6 •

2018

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.

An In Vitro Artificial Activation Assay for Studying Fc Receptor Activation by Antibodies

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2025

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.

Stimulation of Notch Signaling in Mouse Osteoclast Precursors

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Cited by 13 •

2017

Notch signaling is a form of cellular communication that relies upon direct contact between cells. To properly induce Notch signaling in vitro, Notch ligands must be presented to cells in an immobilized state. This protocol describes methods for in vitro stimulation of Notch signaling in mouse osteoclast precursors.

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