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s1 antibody candidates  (ACROBiosystems)

 
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    ACROBiosystems s1 antibody candidates
    Identification of high-affinity mAbs <t>against</t> <t>SARS-CoV-2</t> <t>S1</t> subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars
    S1 Antibody Candidates, supplied by ACROBiosystems, used in various techniques. Bioz Stars score: 90/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/s1 antibody candidates/product/ACROBiosystems
    Average 90 stars, based on 18 article reviews
    s1 antibody candidates - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries"

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    Journal: mAbs

    doi: 10.1080/19420862.2021.2002236

    Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars
    Figure Legend Snippet: Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars

    Techniques Used: Binding Assay, Software, Enzyme-linked Immunosorbent Assay, Inhibition, Flow Cytometry, Expressing, Fluorescence, Standard Deviation

    Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). circular dendrogram figure constructed using interactive tree of life (iTOL).
    Figure Legend Snippet: Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). circular dendrogram figure constructed using interactive tree of life (iTOL).

    Techniques Used: Sequencing, Binding Assay, Inhibition, Competitive Binding Assay, Generated, Construct

    Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only
    Figure Legend Snippet: Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only

    Techniques Used: Binding Assay, High Throughput Screening Assay

    Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations
    Figure Legend Snippet: Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations

    Techniques Used: Binding Assay, Negative Staining, Electron Microscopy



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    ACROBiosystems s1 antibody candidates
    Identification of high-affinity mAbs <t>against</t> <t>SARS-CoV-2</t> <t>S1</t> subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars
    S1 Antibody Candidates, supplied by ACROBiosystems, 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/result/s1 antibody candidates/product/ACROBiosystems
    Average 90 stars, based on 1 article reviews
    s1 antibody candidates - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars

    Article Snippet: We next investigated the cross-competition of the S1 antibody candidates and existing SARS-CoV-2 antibodies, including CR3022 and SAD-S35 (Acro Biosystems), with S1 using high-throughput SPR (HT-SPR).

    Techniques: Binding Assay, Software, Enzyme-linked Immunosorbent Assay, Inhibition, Flow Cytometry, Expressing, Fluorescence, Standard Deviation

    Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). circular dendrogram figure constructed using interactive tree of life (iTOL).

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). circular dendrogram figure constructed using interactive tree of life (iTOL).

    Article Snippet: We next investigated the cross-competition of the S1 antibody candidates and existing SARS-CoV-2 antibodies, including CR3022 and SAD-S35 (Acro Biosystems), with S1 using high-throughput SPR (HT-SPR).

    Techniques: Sequencing, Binding Assay, Inhibition, Competitive Binding Assay, Generated, Construct

    Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only

    Article Snippet: We next investigated the cross-competition of the S1 antibody candidates and existing SARS-CoV-2 antibodies, including CR3022 and SAD-S35 (Acro Biosystems), with S1 using high-throughput SPR (HT-SPR).

    Techniques: Binding Assay, High Throughput Screening Assay

    Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations

    Article Snippet: We next investigated the cross-competition of the S1 antibody candidates and existing SARS-CoV-2 antibodies, including CR3022 and SAD-S35 (Acro Biosystems), with S1 using high-throughput SPR (HT-SPR).

    Techniques: Binding Assay, Negative Staining, Electron Microscopy