The extracellular domain (160 amino acids) of mouse CD152 is fused to mouse IgG2a Fc domain in which mutations to the complement (C1q) and FcγR I binding sites of the Fcγ2a fragment render the Fc fusion protein incapable of direct antibody directed cytotoxicity (ADCC) and complement directed cytotoxicity (CDC).
Biochem/physiol Actions
CD152 (CTLA4), a cell surface glycoprotein expressed at low levels on activated T cells, is a high affinity receptor for the costimulatory molecules CD80 (B7-1) and CD86 (B7-2). A related cell surface glycoprotein, CD28, binds to CD80 and CD86 with lower affinity. The soluble CD152/Fc chimeric fusion protein blocks the B7/CD28 signaling pathway by binding to CD80 and CD86.
High affinity receptor for the costimulatory molecules CD80 (B7-1) and CD86 (B7-2); blocks the B7/CD28 signaling pathway by binding to CD80 and CD86.
Physical form
Lyophilized from solution of 0.2 μm filtered, in phosphate buffered saline, pH 7.4, with no preservative added.
Preparation Note
Purified from serum-free tissue culture supernatant
Journal of immunology (Baltimore, Md. : 1950), 155(3), 1165-1174 (1995-08-01)
To test the hypothesis that blockade of B7-triggered costimulation by donor cells could preclude allograft rejection, we coated crude islet allograft preparations in vitro for 1 h with a murine CTLA4/Fc fusion protein. Murine CTLA4/Fc blocks the proliferative response in
The Journal of experimental medicine, 174(3), 561-569 (1991-09-01)
Functional interactions between T and B lymphocytes are necessary for optimal activation of an immune response. Recently, the T lymphocyte receptor CD28 was shown to bind the B7 counter-receptor on activated B lymphocytes, and subsequently to costimulate interleukin 2 production
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