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High affinities IgE receptor antibody

Anti FcƒÃR1ƒ¿(human IgE receptor) monoclonal antibody (CRA2)


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Background

FcεR1α is subunit of the high affinity receptor of IgE to which it directly binds. FcεR1α is a tetrameric complex consisting of one α, one β and twoγ subunis. The latter two are required for signal transduction activity. The FcεR1 complex plays an important role in triggering allergic responses.
The CRA2 (AER24) monoclonal antibody reacts with the FcεR1α subunit on a region that overlaps the region of the IgE binding site, thus it competes with IgE for the receptor binding. Since the CRA1 (AER37) monoclonal antibody reacts with the site different from the IgE binding site on FcεR1α, it does not compete with IgE for the receptor binding. Combining the two antibodies, one can quantitatively measure the amounts of the IgE-bound FcεR1α.
This product is the IgG fraction purified from serum free culture medium of mouse hybridoma (CRA2) by propriety chromatography under mild conditions.

Application

1. Western blotting (`1ug/ml)
2. FACS
3. Immunohistochemistry
4. Titration of IgE-bound fraction of the FcεR1α using CRA1 and CRA2 antibodies


Figure : FACS analysis of CHO/αβγ cells (1x105) with CRA1 and CRA2 antibodies by indirect-immunostaining using FITC-labeled secondary antibody.

<Reference>
1. Ra C et al., Nature 341:752 (1989)
2. Hakimi J et al., J. Biol. Chem. 265:22079 (1990)
3. Takai T et al., Biosci. Biotechnol. Biochem. 64: 1856 (2000)(PubMed)

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