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 wi...

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Veröffentlicht in:	The Journal of biological chemistry 1993-06, Vol.268 (18), p.13118-13127
Hauptverfasser:	BASU, M, HAKIMI, J, NETTLETON, M. Y, KOCHAN, J. P, DHARM, E, KONDAS, J. A, WEN-HUI TSIEN, PILSON, R. S, PING LIN, GILFILLAN, A, HARING, P, BRASWELL, E. H
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies, immunoglobulins Binding Sites Biological and medical sciences Cells, Cultured Chromatography, Gel Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Fundamental immunology Glycosylation Histamine Release Humans Immunoglobulin E - metabolism Immunoglobulin Fc Fragments - isolation & purification Immunoglobulin Fc Fragments - metabolism Molecular immunology Rats Receptors, IgE - isolation & purification Receptors, IgE - metabolism Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Structure
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