Novel Tools for Functional Analysis of CD11c: Activation-Specific, Activation-Independent, and Activating Antibodies.

Autor:	Sadhu, Chanchal, Hendrickson, Lee, Dick, KenO., Potter, TamaraG., Staunton, DonaldE.
Předmět:	DYE-ligand affinity chromatography IMMUNOGLOBULINS LIGAND binding (Biochemistry) DENDRITIC cells ANTIGEN presenting cells LYMPHOID tissue BIOCHEMISTRY MULTIDIMENSIONAL Aptitude Battery
Zdroj:	Journal of Immunoassay & Immunochemistry; Jan2008, Vol. 29 Issue 1, p42-57, 16p, 1 Chart, 6 Graphs
Abstrakt:	Functions and binding properties of four CD11c-specific mAbs are described here. The mAb 496B stimulated, while 496K inhibited ligand binding of CD11c. The stimulatory mAb, 496B, as well as the inhibitory mAbs BU15 and 496 K appear to act allosterically, as they do not bind the CD11c I domain. The mAb 3.9 bound preferentially to activated forms of CD11c and the binding was divalent cation dependent. CD11c binding to 3.9 recapitulates many of the integrin-ligand interactions. Our data suggest that 3.9 is a competitive antagonist, BU15 and 496K are allosteric antagonists, and 496B is an allosteric agonist of CD11c. These mAbs provide a set of tools to study the functions of the dendritic cell marker, CD11c. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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