vero76 cells Search Results


vero 76  (ATCC)
99
ATCC vero 76
Vero 76, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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suit2-007 cells  (Marburg GmbH)
90
Marburg GmbH suit2-007 cells
Suit2 007 Cells, supplied by Marburg GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero cells vero 76 kclb no. 21587  (Korean Cell Line Bank)
90
Korean Cell Line Bank vero cells vero 76 kclb no. 21587
Vero Cells Vero 76 Kclb No. 21587, supplied by Korean Cell Line Bank, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero-76 cells  (Merck KGaA)
90
Merck KGaA vero-76 cells
Vero 76 Cells, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero 76 cells  (Corning Life Sciences)
90
Corning Life Sciences vero 76 cells
(A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded <t>Vero</t> <t>76</t> cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.
Vero 76 Cells, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero 76 cells - by Bioz Stars, 2026-03
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vero cell line vero76  (JCRB Cell Bank)
90
JCRB Cell Bank vero cell line vero76
(A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded <t>Vero</t> <t>76</t> cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.
Vero Cell Line Vero76, supplied by JCRB Cell Bank, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero cells vero 76  (National Centre for Cell Science)
90
National Centre for Cell Science vero cells vero 76
(A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded <t>Vero</t> <t>76</t> cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.
Vero Cells Vero 76, supplied by National Centre for Cell Science, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vero 76 cells grown on the coverslips of mattek glass bottom dishes  (MatTek)
90
MatTek vero 76 cells grown on the coverslips of mattek glass bottom dishes
(A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded <t>Vero</t> <t>76</t> cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.
Vero 76 Cells Grown On The Coverslips Of Mattek Glass Bottom Dishes, supplied by MatTek, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


(A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded Vero 76 cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.

Journal: bioRxiv

Article Title: The Sequence Basis for Selectivity of Ephrin-B2 Ligand for Eph Receptors and Pathogenic Henipavirus G Glycoproteins

doi: 10.1101/2023.04.26.538420

Figure Lengend Snippet: (A) Magnified views of the G-H binding loop bound to Eph receptor (magenta) and NiV-G (green) are shown. The difference of the conservation scores for the NiV-G-High sorts from the two EFNB2 deep mutational scans are mapped onto the RBD of EFNB2 and colored as in . (B) Expi293F cells expressing full-length NiV-G fused at the C-terminus to sfGFP were incubated with increasing concentrations of sEFNB2-Fc protein. Binding of sEFNB2-Fc to membrane-displayed NiV-G-sfGFP was measured by flow cytometry. Data are mean ± SEM, N = 3 biological replicates. (C) Mixtures of rCedV-GFP chimeric viruses pre-incubated with increasing concentrations of sEFNB2-Fc protein were added to pre-seeded Vero 76 cells. Neutralizing activity of sEFNB2-Fc was measured by counting the reduction in GFP fluorescent foci. Data are mean ± SD, N = 2 independent experiments, each performed in technical triplicate. (D) Proposed mechanism by which the Q130L and V167L mutations affect the conformational selectivity of the G-H binding loop. In wild-type EFNB2, the G-H binding loop is dynamic and in equilibrium between conformations for binding both Eph receptors (magenta) and NiV-G (green). The side chain of EFNB2-Q130 is fully exposed to solvent in the ‘open’ loop structure bound to Eph receptors but is packed against neighboring side chains in the ‘closed’ loop structure bound by NiV-G. In EFNB2-D62Q-Q130L-V167L, the conformational equilibrium shifts to favor the ‘closed’ state, which minimizes interactions between solvent and the hydrophobic Q130L substitution. Additionally, a leucine substitution at EFNB2-V167 acts as a cavity-filling mutation and increases the hydrophobic packing around EFNB2-F129 in the ‘closed’ state.

Article Snippet: Vero 76 cells were seeded at a density of 2 × 10 4 cells/well in black walled clear bottom 96-well plates (Corning Life Sciences). sEFNB2-Fc proteins were serially diluted 3-fold for 7-point dose response curves.

Techniques: Binding Assay, Expressing, Incubation, Protein Binding, Membrane, Flow Cytometry, Activity Assay, Solvent, Mutagenesis