MOG 37-46

MOG 37-46 (100 μM; 2 h) binds to H-2Db on RMA-S cells with relatively low but detectable affinity^[1].
MOG37-46 (1-100 μM; 5 h-2 weeks) is the dominant CD8⁺ T cell epitope recognized by in vitro expanded lymph node-derived CD8⁺ T cells expanded with MOG35-55 peptide^[2].
MOG37-46 (100 μM; 5 h) is the dominant CD8⁺ T cell epitope recognized by in vitro expanded lymph node-derived CD8⁺ T cells expanded with recombinant MOG protein, inducing IFNγ production in a higher percentage of cells than MOG44-54^[2].
MOG37-46 (10-100 μM; 2 weeks) is recognized by in vitro expanded MOG37-46 reactive CD8⁺ T cell lines expanded with MOG37-46 peptide, which exhibit low functional avidity, requiring 100 μM MOG37-46 peptide for peak IFNγ production, which is 1000-fold higher than the concentration needed for viral antigen reactive CD8⁺ T cells^[2].
MOG37-46 (10-100 μM; 5 h-2 weeks) is recognized by in vitro expanded MOG37-46 reactive CD8⁺ T cell lines expanded with MOG37-46 peptide, which are polyclonal, pro-inflammatory effector cells, producing IFNγ, TNFα, and IL-2 in response to 100 μM MOG37-46 peptide^[2].
MOG 37-46 resides within the biologically relevant head-to-tail dimer interface of the mouse MOG extracellular domain, as determined via 1.8-Å resolution X-ray crystallography^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.