Purification and characterization of human recombinant IgE-Fc fragments that bind to the human high affinity IgE receptor

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Purification and characterization of human recombinant IgE-Fc fragments that bind to the human high affinity IgE receptor.

The Fc-region of immunoglobulin E (IgE) comprising C epsilon 2, C epsilon 3, and C epsilon 4 domains is sufficient for binding to the alpha chain of the high affinity IgE-Fc receptor (Fc epsilon RI alpha). In order to identify the smallest Fc fragment capable of binding to the Fc epsilon RI alpha with high affinity, various regions of the IgE-Fc molecule were expressed in COS cells and investig...

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A Soluble Form of the High Affinity IgE Receptor, Fc-Epsilon-RI, Circulates in Human Serum

Soluble IgE receptors are potential in vivo modulators of IgE-mediated immune responses and are thus important for our basic understanding of allergic responses. We here characterize a novel soluble version of the IgE-binding alpha-chain of Fc-epsilon-RI (sFcεRI), the high affinity receptor for IgE. sFcεRI immunoprecipitates as a protein of ∼40 kDa and contains an intact IgE-binding site. In hu...

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Crystal Structure of the Human High-Affinity IgE Receptor

Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolutio...

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Cloning, Expression and Characterization of Recombinant Human Fc Receptor Like 1, 2 and 4 Molecules

Background: The Fc receptor like (FCRL) molecules belong to the immunoglobulin (Ig) superfamily with potentially immunoregulatory <span style="font-va...

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Lymphocytes that Bind IgE

spontaneous rosettes with sheep erythrocytes (E), 10.6% cells having surface immunoglobulin (SIg), and 15.5% binding IgG as shown by rosette formation with IgG-coated ox red cells (E0A). Fractionation of the lymphocytes into populations rich in spontaneously E-rosetting cells and cells with SIg indicated that the majority of the lymphocytes forming E0'-IgE rosettes belonged to the SIg-positive ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1993

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)38627-2