Human Interferon-γ- Receptor I (IFN-γ RI) is a 25kD, 227 amino acid residue containing protein that belongs to type II cytokine receptor family. IFN-γ RI has a crucial role in ligand-binding and signaling. Ligand IFN-γ induces tyrosine phosphorylation in IFN-γ RI which in turn leads to the formation of a docking site on the activated receptor for Stat1 that specifically activates IFN-γ induced gene transcription. Anti-Interferon γ Receptor I (IFN-γ RI) antibody can be used in neutralization assay using a confluent culture of HeLa cells. Goat anti-Interferon γ Receptor I (IFN-γ RI) antibody reacts specifically with recombinant human IFN-γ RI. The product has shown no cross-reactivity for recombinant human IFN-γ RII.
Immunogen
recombinant human IFN-γ Receptor I extracellular domain expressed in NSO cells.
Application
Anti-Interferon γ Receptor I (IFN-γ RI) antibody can be used in indirect ELISA and western blot.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing carbohydrates.
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Cytokines are the principal regulators of cell proliferation and differentiation of hematopoietic cells and these responses are initiated through activation of hematopoietic cytokine receptors. Although the receptor intracellular domains lack any kinase domains, activation of cytokine receptors lead to rapid
Annual review of immunology, 15, 563-591 (1997-01-01)
During the last several years, the mechanism of IFN gamma-dependent signal transduction has been the focus of intense investigation. This research has recently culminated in the elucidation of a comprehensive molecular understanding of the events that underlie IFN gamma-induced cellular
Herein we report that interferon-gamma (IFN gamma) induces the rapid and reversible tyrosine phosphorylation of the IFN gamma receptor. Using a panel of receptor intracellular domain mutants, we show that a membrane-proximal LPKS sequence (residues 266-269) is required for ligand-induced
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