CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. It is found both as a transmembrane receptor protein and in a soluble form, which is generated by proteolytic cleavage of membrane bound CD23. The predominant soluble form of CD23 (sCD23) consists of 172 amino acids corresponding to the extracellular domain of the full length precursor. sCD23, in addition to binding IgE, also exerts a number of IgE independent activities, such as promoting the activation and differentiation of B-cells and stimulating the release of pro-inflammatory cytokines from monocytes. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.
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CD23, the low affinity receptor for IgE, belongs to the C-type lectin structural family and plays a role in the regulation of IgE synthesis and IgE mediated activities. Recombinant human sCD23 is a 19.2 kDa non-glycosylated protein containing 172 amino-acid residues.
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
International archives of allergy and applied immunology, 90 Suppl 1, 41-44 (1989-01-01)
The low-affinity receptor for IgE (FcERII or CD23) is a membrane 45-kD glycoprotein which is cleaved by an autoproteolytic mechanism into soluble 37-, 33- and 25-kD fragments that are capable of binding to IgE (IgE-binding factors, IgE-BFs). FcERIIa (which is
The Journal of allergy and clinical immunology, 86(3 Pt 1), 333-344 (1990-09-01)
The role of soluble fragments of CD23 and their relationship to interleukin-4 (IL-4) in the in vitro production of IgE by normal human peripheral blood mononuclear cells was examined. Most donors' cells were induced to produce IgE in vitro by
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