Journal: Cancers

Article Title: Isolation of Two Novel Human Anti-CTLA-4 mAbs with Intriguing Biological Properties on Tumor and NK Cells

doi: 10.3390/cancers12082204

Figure Lengend Snippet: Binding of the novel anti-CTLA-4 mAbs to CD28-Fc and to cynomologous CTLA-4-Fc. Cross-reactivity of ID-1 and ID-8 mAbs to CD28-Fc ( A ) or to monkey CTLA-4-Fc proteins ( B ). Ipilimumab was used in parallel assays as a control.

Article Snippet: The following recombinant proteins were used: Recombinant Human CTLA-4 Fc Chimera; Recombinant Human B7-1/CD80 Fc Chimera Protein; Recombinant Human B7-2/CD86 Fc Chimera Protein; Recombinant Human CD28 Fc protein; Recombinant Cynomolgus Monkey CTLA-4 Fc Chimera Protein; Recombinant Human IgG1 Fc Protein (all from R & D Systems, Minneapolis, MN, USA); Human CTLA-4 Protein (His & Fc Tag); CTLA-4 Protein, Mouse, Recombinant (Fc Tag) (both from Sino Biological, Wayne, PA, USA).

Techniques: Binding Assay, Control

Journal: Journal of biomedical science

Article Title: The homodimer interfaces of costimulatory receptors B7 and CD28 control their engagement and pro-inflammatory signaling.

doi: 10.1186/s12929-023-00941-3

Figure Lengend Snippet: Fig. 5 B7-1 and B7-2 dimer interface mimetic peptides attenuate engagement of CD28 by the cognate B7 costimulatory receptor. A In cartoon model of the extracellular domain of costimulatory receptor B7-1 (CD80) (green; 1dr9.pdb), a double beta-barrel, amino acid residues forming pB1-8 are modeled in sticks, with 2 residues making homodimer interface contacts shown in yellow. B, C pB1-8 selectively attenuates intercellular B7-1/CD28 engagement (B) but not B7-2/CD28 engagement (C). Receptor engagement was assayed by flow cytometry as in Fig. 3K for B7-1/CD28 engagement and as in Fig. 3D for B7-2/CD28 engagement. D In the extracellular domain of B7-1, amino acid residues forming pB1-78 are modeled in sticks, with 4 residues making homodimer interface contacts shown in yellow and orange. E, F pB1-78 selectively attenuates intercellular B7-1/ CD28 engagement (E) but not B7-2/CD28 engagement (F). G, H pB2-7 selectively attenuates intercellular B7-2/CD28 engagement (H) but not B7-1/ CD28 engagement (G). Data are mean and SEM of three independent experiments (contour plots: Additional file 1: Fig. S6). Intercellular receptor engagement was compared using the one-tailed unpaired student’s t-test; *p < 0.05, **p < 0.005, ***p < 0.001, ****p < 0.0001; n.s, not significant

Article Snippet: Recombinant human B7-2 (CD86) Fc chimera and human CD28 Fc chimera expressed in mouse myeloma NS0 cells (R&D Systems) comprise the extracellular 20–239 and 19–152 amino acid domain, respectively, of the mature human ligands fused to C-terminal human IgG1 Fc and are homodimers, disulfide-linked in the Fc domain.

Techniques: Flow Cytometry, One-tailed Test