|Detection of B7‑2/CD86 in Mouse Splenocytes by Flow Cytometry. Mouse splenocytes either untreated (light orange filled histogram) or treated with 1 μg/mL LPS for 3 days (dark orange filled histogram) were stained with Rat Anti-Mouse B7‑2/CD86 PerCP‑conjugated Monoclonal Antibody (Catalog # FAB741C) or isotype control antibody (Catalog # IC006C, open histogram). View our protocol for Staining Membrane-associated Proteins.|
B7-1 and B7-2, together with their receptors CD28 and CTLA-4, constitute one of the dominant costimulatory pathways that regulate T- and B-cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down‑regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through Interferon gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. Mouse B7-2 is a 309 amino acid (aa) protein containing a putative 23 aa signal peptide, a 221 aa extracellular domain, a 21 aa transmembrane domain, and a 44 aa cytoplasmic domain. Mouse B7-2 and B7-1 share 28% amino acid identity. Mouse and human B7-2 share 50% amino acid identity. However, it has been observed that both human and mouse B7‑1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.
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