FCER1A
Reactivity: Human
WB, ELISA
Host: Mouse
Polyclonal
unconjugated
Application Notes
1) Western blotting: ~1 g/mL 2) FACS 3) Immunohistochemistry 4) Titration of IgE-bound fraction of the FcepsilonR1alpha using CRA1 and CRA2 antibodies
Restrictions
For Research Use only
Format
Liquid
Concentration
0.9 mg/mL
Buffer
PBS ( pH 7.4), 50 % glycerol
Preservative
Azide free
Storage
-20 °C/-80 °C
Storage Comment
-20 C (For long term storage: -70 C)
Takai, Yuuki, Iwamoto-Yasue, Okumura, Ra: "Epitope analysis and primary structures of variable regions of anti-human FcepsilonRI monoclonal antibodies, and expression of the chimeric antibodies fused with human constant regions." in: Bioscience, biotechnology, and biochemistry, Vol. 64, Issue 9, pp. 1856-67, (2001) (PubMed).
Hakimi, Seals, Kondas, Pettine, Danho, Kochan: "The alpha subunit of the human IgE receptor (FcERI) is sufficient for high affinity IgE binding." in: The Journal of biological chemistry, Vol. 265, Issue 36, pp. 22079-81, (1991) (PubMed).
Ra, Jouvin, Blank, Kinet: "A macrophage Fc gamma receptor and the mast cell receptor for IgE share an identical subunit." in: Nature, Vol. 341, Issue 6244, pp. 752-4, (1989) (PubMed).
Target
Fc epsilon RI/FCER1A (FCER1A)
(Fc Fragment of IgE Receptor Ia (FCER1A))
FcεR1alpha is subunit of the high affinity receptor for IgE to which IgE directly binds. FcεR1alpha is a tetrameric complex consisting of one alpha, one beta and two γ subunits. 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 FcεR1alpha 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 FcεR1alpha, it does not compete with IgE for the receptor binding. Combining the two antibodies, one can quantitatively measure the amounts of the IgE-bound FcεR1alpha.