CD23/Fc epsilon RII Antibody [Unconjugated] Summary
Mouse myeloma cell line NS0-derived recombinant human CD23/Fc epsilon RII
Accession # P06734
Detects human CD23/Fc epsilon RII in direct ELISAs and Western blots.
<0.10 EU per 1 μg of the antibody by the LAL method.
Test in a species/application not listed above to receive a full credit towards a future purchase.
- Western Blot 0.1 ug/mL
- Blockade of Receptor-ligand Interaction
- Immunocytochemistry 5-15 ug/mL
Packaging, Storage & Formulations
|Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for CD23/Fc epsilon RII Antibody [Unconjugated]
- CD23CD23 antigen
- CLEC4JC-type lectin domain family 4 member J
- C-type lectin domain family 4, member J
- Fc epsilon RII
- Fc fragment of IgE, low affinity II, receptor for (CD23)
- FCE2Fc fragment of IgE, low affinity II, receptor for (CD23A)
- Immunoglobulin E-binding factor
- low affinity immunoglobulin epsilon Fc receptor
- Lymphocyte IgE receptor
CD23 (also named B cell differentiation antigen) is a member of subgroup II of the C-type (Ca++-dependent) lectin superfamily (1-5). Human CD23 is a 47 kDa, type II transmembrane glycoprotein that is expressed by a wide variety of cell types (6-10). The full-length receptor is 321 amino acids (aa) in length and contains a 274 aa extracellular region, a 26 aa transmembrane segment, and a 21 aa cytoplasmic domain. The extracellular region contains a C-type lectin domain and a connecting stalk with coiled-coil topography (3, 11). The lectin domain binds both protein and carbohydrate in an apparently Ca++ independent manner (11). The coiled-coil region contributes to oligomerization (11, 12). The lectin domain in human CD23 (aa 162-284) shares 64%, 62%, and 68% aa sequence identity with the lectin domains in mouse, rat, and bovine CD23, respectively. In the cytoplasmic region, two FC isoforms exist which arise from alternate start sites (6, 12). The “a” (or long) isoform begins with the sequence MEEGQYS and is constitutively expressed by B cells. It is believed to participate in IgE-mediated endocytosis (13). The “b” (or short) isoform begins with MNPPSQ and is induced on a wide variety of cell types by IL-4 (6). Fcb reportedly contributes to IgE-mediated phagocytosis (13). Fcb expressing cells include eosinophils, monocytes, visceral smooth muscle and intestinal epithelium (6, 14, 15). At least four soluble forms of CD23 are known to exist. They range in molecular weight from 25 kDa to 37 kDa, with the 25 kDa form predominating in sera (16). Soluble CD23 (sFc) is generated by metalloprotease (ADAM8; ADAM15; ADAM28) and cysteine-protease activity (16-18). Cleavage usually occurs between aa 150-160 (7, 8). It is unclear if sequential metalloprotease-cysteine protease activity is necessary for the generation of all soluble forms. Both soluble and membrane-bound CD23 show bioactivity. Ligands for CD23 include CD21, IgE, CD11b, and CD11c (19-21). CD23 binding to CD11b and Cd11c on monocytes results in oxidative product generation and proinflammatory cytokine release (21). On B cells, sCD23 induces IgE secretion by binding CD21. Conversely, secreted IgE will, in turn, bind B cell membrane CD23, rendering it unavailable for cleavage, and thus shutting down IgE production (11).
- Kijimoto-Ochiai, S. (2002) Cell. Mol. Life Sci. 59:648.
- Heyman, B. (2000) Annu. Rev. Immunol. 18:709.
- Bajorath, J. and A. Aruffo (1996) Protein Sci. 5:240.
- Drickamer, K. (1993) Curr. Opin. Struct. Biol. 3:393.
- Drickamer, K. (1999) Curr. Opin. Struct. Biol. 9:585.
- Yokota, A. et al. (1988) Cell 55:611.
- Ludin, C. et al. (1987) EMBO J. 6:109.
- Ikuta, K. et al. (1987) Proc. Natl. Acad. Sci. USA 84:819.
- Kikutani, H. et al. (1986) Cell 47:657.
- Letellier, M. et al. (1988) J. Immunol. 141:2374.
- Hibbert, R.G. et al. (2005) J. Exp. Med. 202:751.
- Beavuil, A.J. et al. (1992) Proc. Natl. Acad. Sci. USA 89:753.
- Yokota, A. et al. (1992) Proc. Natl. Acad. Sci. USA 89:5030.
- Belleau, J.T. et al. (2005) Clin. Mol. Allergy 3:6.
- Tu, Y. et al. (2005) Gastroenterology 129:928.
- Marolewski, A.E. et al. (1998) Biochem. J. 333:573.
- Fourie, A.M. et al. (2003) J. Biol. Chem. 278:30469.
- Karagiannis, S.N. et al. (2001) Immunology 103:319.
- Aubry, J-P. et al. (1992) Nature 358:505.
- Sarfati, M. and G. Delespeese (1988) J. Immunol. 141:2195.
- Lecoanet-Henchoz, S. et al. (1995) Immunity 3:119.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed
for 1 year from date of receipt.
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