recombinant human cd86 protein Search Results


recombinant human cd28 fc protein  (R&D Systems)
94
R&D Systems recombinant human cd28 fc protein
Binding of the novel anti-CTLA-4 mAbs to <t>CD28-Fc</t> and to cynomologous CTLA-4-Fc. Cross-reactivity of ID-1 and ID-8 mAbs to <t>CD28-Fc</t> ( A ) or to monkey CTLA-4-Fc proteins ( B ). Ipilimumab was used in parallel assays as a control.
Recombinant Human Cd28 Fc Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/recombinant human cd28 fc protein/product/R&D Systems
Average 94 stars, based on 1 article reviews
recombinant human cd28 fc protein - by Bioz Stars, 2026-05
94/100 stars
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recombinant human b7 2 cd86 fc chimera  (R&D Systems)
93
R&D Systems recombinant human b7 2 cd86 fc chimera
Fig. 5 B7-1 <t>and</t> <t>B7-2</t> 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
Recombinant Human B7 2 Cd86 Fc Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/recombinant human b7 2 cd86 fc chimera/product/R&D Systems
Average 93 stars, based on 1 article reviews
recombinant human b7 2 cd86 fc chimera - by Bioz Stars, 2026-05
93/100 stars
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b7 2 his tag  (R&D Systems)
91
R&D Systems b7 2 his tag
Fig. 5 B7-1 <t>and</t> <t>B7-2</t> 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
B7 2 His Tag, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/b7 2 his tag/product/R&D Systems
Average 91 stars, based on 1 article reviews
b7 2 his tag - by Bioz Stars, 2026-05
91/100 stars
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cd86 fc proteins  (R&D Systems)
92
R&D Systems cd86 fc proteins
Fig. 5 B7-1 <t>and</t> <t>B7-2</t> 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
Cd86 Fc Proteins, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/cd86 fc proteins/product/R&D Systems
Average 92 stars, based on 1 article reviews
cd86 fc proteins - by Bioz Stars, 2026-05
92/100 stars
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recombinant human b7 2 cd86 his tag protein cf  (R&D Systems)
N/A
The Recombinant Human B7 2 CD86 His Tag Protein from R D Systems is derived from HEK293 The Recombinant Human B7 2 CD86 His Tag Protein has been validated for the following applications Bioactivity
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b7-2-cd86 protein, human, recombinant  (TargetMol)
N/A
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recombinant human cd86 b7-2 protein, c-his-avi  (Bioss)
N/A
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recombinant human cd86/b7-2 protein (val185ile  (Elabscience Biotechnology)
N/A
The protein is the receptor that involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. It may play a critical role in the early events of T-cell
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recombinant human cd86 protein  (Elabscience Biotechnology)
N/A
CD86, also known as B-lymphocyte activation antigen B7-2 (referred to as B70), is a member of the cell surface immunoglobulin superfamily. B7-2 exists predominantly as a monomer on cell surfaces and interacts with an two
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human cd86 recombinant protein fc tag lyophilized  (Innovative Research Inc)
N/A
Human CD86 Recombinant Protein Fc Tag Lyophilized from Innovative Research has been recombinantly produced in CHO cells. This is a Lyophilized protein buffered in Lyophilized from 0.2um-filtered solution in PBS. Reconstitute with 100 and#956;l sterile
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recombinant human b7 2 cd86 fc chimera protein cf  (R&D Systems)
N/A
The Recombinant Human B7 2 CD86 Fc Chimera Protein from R D Systems is derived from NS0 The Recombinant Human B7 2 CD86 Fc Chimera Protein has been validated for the following applications Bioactivity
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Image Search Results


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.

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

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

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