human cd86 his Search Results


human cd86 / b7-2 protein (his tag), biotinylated  (Sino Biological)
N/A
A DNA sequence encoding the extracellular domain (Met1-His239) of human B7-2 (NP_008820.2) was fused with a polyhistidine tag at the C-terminus. The purified protein was biotinylated in vitro.
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cd86  (R&D Systems)
90
R&D Systems cd86
A. The ability of CTLA-4 mAbs to block binding of CD80 or <t>CD86</t> was measured using a plate-based ELISA method. CTLA-4 was used to coat the plate, then after the antibody samples were incubated, His-tagged CD80 or CD86 was added, and the amount of ligand able to bind to CTLA-4 was measured. Blocking mAbs that prevent CD80 or CD86 from binding to CTLA-4 reduce the absorbance signal due to lack of CD80 or CD86 binding to CTLA-4. Weak-blocking mAbs still allow CD80 or CD86 to bind, preventing the loss of all absorbance signal. B. Plots show the ability of GIGA-564 to block the interaction between CTLA-4 and the B7 ligands CD80 and CD86 compared to ipilimumab and CTLA-4.28, as assessed by ELISA as described in (A). Absorbance values were normalized to an anti-PD-1 control (pembrolizumab) and displayed as the average of two technical replicates. C-D. The key residues mediating CTLA-4 binding were identified for GIGA-564 and ipilimumab by shotgun mutagenesis of CTLA-4, followed by staining and flow cytometry assessment of binding. C. Shown is the crystal structure (Protein Database [PDB] 1I8L) of the complex between CD80 (blue) and CTLA-4 (gray) on which the CTLA-4 epitope residues shared between ipilimumab and GIGA-564 were colored orange and the key differentiating residue R70 was colored red (visualized with Pymol). Additionally, G142 was identified as a secondary residue for the epitope of ipilimumab but not GIGA-564. D. Table showing key amino acids on CTLA-4 of interest for these epitopes; those found by mutational analysis to be important for binding of CTLA-4 to CD80 or CD86 in a cell-based assay are marked in gray to indicate the epitope residues for those proteins .
Cd86, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+cd86+his/Recombinant+Human+B7-2%2FCD86+His+Tag+Protein%2C+CF/bio_rxiv__2021__07__12__452090-228-11-12
Average 90 stars, based on 1 article reviews
cd86 - by Bioz Stars, 2026-11
90/100 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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recombinant human cd86, fc-his tagged  (Creative BioMart)
N/A
Recombinant Human CD86 extracellular domain (Met 1-His 239) (NP_008820.2), fused with the polyhistidine-tagged Fc region of human IgG1 at the C-terminus, was produced in Human Cell.http://www.creativebiomart.net/description_3644_12.htm
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recombinant human cd86 b7-2 protein, c-his-avi  (Bioss)
N/A
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human cd86 b7 2 protein his fc tag biotinylated  (Sino Biological)
N/A
A DNA sequence encoding the human CD86 NP 008820 2 Met1 His239 was expressed with the C terminal His tagged Fc region of human IgG1 at the C terminus The purified protein was biotinylated in
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human cd86/b7-2 transcript variant 2 gene orf cdna clone expression plasmid, n-his tag  (Sino Biological)
N/A
Full length Clone DNA of Human CD86 molecule (CD86), transcript variant 2 with N terminal His tag.
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recombinant human cd86 b7-2 protein, c-his-avi (hek293), biotin conjugated  (Bioss)
N/A
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recombinant human b7-2/cd86 his protein  (Novus Biologicals)
N/A
Recombinant Human B7-2/CD86 His Protein
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human cd86 protein (his & avi tag), biotinylated  (Sino Biological)
N/A
A DNA sequence encoding the human CD86 (NP_008820.4) (Met1-His239) was expressed with a C-terminal polyhistidine tag followed by an AVI tag. The expressed protein was biotinylated in vivo by the Biotin-Protein ligase (BirA enzyme) which
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b7-2-cd86 protein, human, recombinant (his & avi), biotinylated  (TargetMol)
N/A
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A. The ability of CTLA-4 mAbs to block binding of CD80 or CD86 was measured using a plate-based ELISA method. CTLA-4 was used to coat the plate, then after the antibody samples were incubated, His-tagged CD80 or CD86 was added, and the amount of ligand able to bind to CTLA-4 was measured. Blocking mAbs that prevent CD80 or CD86 from binding to CTLA-4 reduce the absorbance signal due to lack of CD80 or CD86 binding to CTLA-4. Weak-blocking mAbs still allow CD80 or CD86 to bind, preventing the loss of all absorbance signal. B. Plots show the ability of GIGA-564 to block the interaction between CTLA-4 and the B7 ligands CD80 and CD86 compared to ipilimumab and CTLA-4.28, as assessed by ELISA as described in (A). Absorbance values were normalized to an anti-PD-1 control (pembrolizumab) and displayed as the average of two technical replicates. C-D. The key residues mediating CTLA-4 binding were identified for GIGA-564 and ipilimumab by shotgun mutagenesis of CTLA-4, followed by staining and flow cytometry assessment of binding. C. Shown is the crystal structure (Protein Database [PDB] 1I8L) of the complex between CD80 (blue) and CTLA-4 (gray) on which the CTLA-4 epitope residues shared between ipilimumab and GIGA-564 were colored orange and the key differentiating residue R70 was colored red (visualized with Pymol). Additionally, G142 was identified as a secondary residue for the epitope of ipilimumab but not GIGA-564. D. Table showing key amino acids on CTLA-4 of interest for these epitopes; those found by mutational analysis to be important for binding of CTLA-4 to CD80 or CD86 in a cell-based assay are marked in gray to indicate the epitope residues for those proteins .

Journal: bioRxiv

Article Title: Lack of blocking activity in anti-CTLA-4 antibodies reduces toxicity, but not anti-tumor efficacy

doi: 10.1101/2021.07.12.452090

Figure Lengend Snippet: A. The ability of CTLA-4 mAbs to block binding of CD80 or CD86 was measured using a plate-based ELISA method. CTLA-4 was used to coat the plate, then after the antibody samples were incubated, His-tagged CD80 or CD86 was added, and the amount of ligand able to bind to CTLA-4 was measured. Blocking mAbs that prevent CD80 or CD86 from binding to CTLA-4 reduce the absorbance signal due to lack of CD80 or CD86 binding to CTLA-4. Weak-blocking mAbs still allow CD80 or CD86 to bind, preventing the loss of all absorbance signal. B. Plots show the ability of GIGA-564 to block the interaction between CTLA-4 and the B7 ligands CD80 and CD86 compared to ipilimumab and CTLA-4.28, as assessed by ELISA as described in (A). Absorbance values were normalized to an anti-PD-1 control (pembrolizumab) and displayed as the average of two technical replicates. C-D. The key residues mediating CTLA-4 binding were identified for GIGA-564 and ipilimumab by shotgun mutagenesis of CTLA-4, followed by staining and flow cytometry assessment of binding. C. Shown is the crystal structure (Protein Database [PDB] 1I8L) of the complex between CD80 (blue) and CTLA-4 (gray) on which the CTLA-4 epitope residues shared between ipilimumab and GIGA-564 were colored orange and the key differentiating residue R70 was colored red (visualized with Pymol). Additionally, G142 was identified as a secondary residue for the epitope of ipilimumab but not GIGA-564. D. Table showing key amino acids on CTLA-4 of interest for these epitopes; those found by mutational analysis to be important for binding of CTLA-4 to CD80 or CD86 in a cell-based assay are marked in gray to indicate the epitope residues for those proteins .

Article Snippet: Recombinant human His-tagged CD80 (R&D Systems 9050-B1, Minneapolis, MN, USA) or CD86 (R&D Systems 9090-B2, Minneapolis, MN, USA) was then added to the plates at 1 μg/mL.

Techniques: Blocking Assay, Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation, Control, Mutagenesis, Staining, Flow Cytometry, Residue, Cell Based Assay

Top panel: Ipilimumab blocks CTLA-4 interaction with CD80/CD86, which allows antigen presenting cells (APCs) to co-stimulate peripheral Tregs enhancing their proliferation. GIGA-564 weakly blocks CTLA-4 interaction with CD80/CD86 and thus induces less Treg proliferation. Bottom panel: Ipilimumab and GIGA-564 bind CTLA-4 on intratumoral Tregs to induce Treg killing via interactions with Fc receptor (FcR) on effector cells. GIGA-564 induces stronger FcR signaling and thus more efficiently depletes intratumoral Tregs than ipilimumab.

Journal: bioRxiv

Article Title: Lack of blocking activity in anti-CTLA-4 antibodies reduces toxicity, but not anti-tumor efficacy

doi: 10.1101/2021.07.12.452090

Figure Lengend Snippet: Top panel: Ipilimumab blocks CTLA-4 interaction with CD80/CD86, which allows antigen presenting cells (APCs) to co-stimulate peripheral Tregs enhancing their proliferation. GIGA-564 weakly blocks CTLA-4 interaction with CD80/CD86 and thus induces less Treg proliferation. Bottom panel: Ipilimumab and GIGA-564 bind CTLA-4 on intratumoral Tregs to induce Treg killing via interactions with Fc receptor (FcR) on effector cells. GIGA-564 induces stronger FcR signaling and thus more efficiently depletes intratumoral Tregs than ipilimumab.

Article Snippet: Recombinant human His-tagged CD80 (R&D Systems 9050-B1, Minneapolis, MN, USA) or CD86 (R&D Systems 9090-B2, Minneapolis, MN, USA) was then added to the plates at 1 μg/mL.

Techniques: