CD152 [CTLA-4] (mouse):Fc (mouse) (rec.) (non-lytic)

The extracellular domain of mouse CD152 [CTLA-4] (aa 1-160) is fused to the N-terminus of the Fc region of a mutant mouse IgG2a. Lyophilized from 0.2µm-filtered solution in PBS. Blocks the binding of mouse CD80 (B7-1) and CD86 (B7-2) to their receptors (by binding CD80 and CD86 with high affinity) and thereby prevents their T cell regulatory actions by inhibiting the CD28 signaling competitively. Shows the biological functions of the CD152 moiety and exerts a prolonged circulating half-life caused by the modified Fc domain. Useful for investigating the T cell co-stimulation. CD152 [CTLA-4] and CD28, together with their ligands B7-1 and B7-2, constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD152 and CD28 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD152 and CD28 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD152 and CD28 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. CD152 was originally identified as a gene that was specifically expressed by cytotoxic T lymphocytes. However, CD152 transcripts have since been found in both Th1 and Th2, and CD4 and CD8 T cell clones. Whereas, CD28 expression is constitutive on the surfaces of 95% of CD4 T cells and 50% of CD8 T cells and is down regulated upon T cell activation, CD152 expression is upregulated rapidly following T cell activation and peaks approximately 24 hours following activation. Although both CD152 and CD28 can bind to the same ligands, CD152 binds to B71 and B72 with 20-100-fold higher affinity than CD28.