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ace2 inhibition assay kit  (BPS Bioscience)


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    BPS Bioscience ace2 inhibition assay kit
    <t>RBD-ACE2</t> interaction <t>inhibition</t> assays. ( a ) Schematic illustration of ELISA experiment to evaluate the ability of the A13 or Nat1 to prevent the interaction of SARS-CoV-2 S1 protein RBD to human receptor ACE2. First the plates were incubated with immobilized RBD. They were then inoculated with peptides prior to the addition of recombinant human receptor ACE2. ( b ) Inhibition of RBD-ACE2 binding via A13 or Nat1. The level of RBD-ACE2 binding was measured by chemiluminescence. The negative control with no peptide representing RBD-ACE2 interaction was set to 1.00 (3.2 × 10 4 RLU) and other values were normalized to this number. To the same extent, at the concentration of 0.1 µg/mL, both peptides reduced ACE2 binding compared to the control. At 1.0 µg/mL, inhibition was further enhanced. The negative control peptide did not exhibit a notable inhibition. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001).
    Ace2 Inhibition Assay Kit, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ace2 inhibition assay kit/product/BPS Bioscience
    Average 93 stars, based on 16 article reviews
    ace2 inhibition assay kit - by Bioz Stars, 2026-05
    93/100 stars

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    1) Product Images from "Artificial Intelligence Reveals Nature: Functional Parallels Between a Designed and a Natural Peptide"

    Article Title: Artificial Intelligence Reveals Nature: Functional Parallels Between a Designed and a Natural Peptide

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms262110607

    RBD-ACE2 interaction inhibition assays. ( a ) Schematic illustration of ELISA experiment to evaluate the ability of the A13 or Nat1 to prevent the interaction of SARS-CoV-2 S1 protein RBD to human receptor ACE2. First the plates were incubated with immobilized RBD. They were then inoculated with peptides prior to the addition of recombinant human receptor ACE2. ( b ) Inhibition of RBD-ACE2 binding via A13 or Nat1. The level of RBD-ACE2 binding was measured by chemiluminescence. The negative control with no peptide representing RBD-ACE2 interaction was set to 1.00 (3.2 × 10 4 RLU) and other values were normalized to this number. To the same extent, at the concentration of 0.1 µg/mL, both peptides reduced ACE2 binding compared to the control. At 1.0 µg/mL, inhibition was further enhanced. The negative control peptide did not exhibit a notable inhibition. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001).
    Figure Legend Snippet: RBD-ACE2 interaction inhibition assays. ( a ) Schematic illustration of ELISA experiment to evaluate the ability of the A13 or Nat1 to prevent the interaction of SARS-CoV-2 S1 protein RBD to human receptor ACE2. First the plates were incubated with immobilized RBD. They were then inoculated with peptides prior to the addition of recombinant human receptor ACE2. ( b ) Inhibition of RBD-ACE2 binding via A13 or Nat1. The level of RBD-ACE2 binding was measured by chemiluminescence. The negative control with no peptide representing RBD-ACE2 interaction was set to 1.00 (3.2 × 10 4 RLU) and other values were normalized to this number. To the same extent, at the concentration of 0.1 µg/mL, both peptides reduced ACE2 binding compared to the control. At 1.0 µg/mL, inhibition was further enhanced. The negative control peptide did not exhibit a notable inhibition. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001).

    Techniques Used: Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, Recombinant, Binding Assay, Negative Control, Concentration Assay, Control, Standard Deviation, Two Tailed Test

    NanoLuc bioreporter assays. ( a ) A schematic illustration for the NanoLuc bioreporter assay to determine SARS-CoV-2 S1 RBD—ACE2 inhibition by A13 or Nat1. ( b ) NanoLuc bioreporter assay indicates that both peptides reduce luciferase complementation to the same extent. The signal value for no peptide control was set to 1.00 (6.30 × 10 5 RLU) and all other values were normalized to it. In cell lysates, A13 and Nat1 both reduced luminescence, indicating inhibition of RBD-ACE2 binding. The negative control peptide had no significant effect. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).
    Figure Legend Snippet: NanoLuc bioreporter assays. ( a ) A schematic illustration for the NanoLuc bioreporter assay to determine SARS-CoV-2 S1 RBD—ACE2 inhibition by A13 or Nat1. ( b ) NanoLuc bioreporter assay indicates that both peptides reduce luciferase complementation to the same extent. The signal value for no peptide control was set to 1.00 (6.30 × 10 5 RLU) and all other values were normalized to it. In cell lysates, A13 and Nat1 both reduced luminescence, indicating inhibition of RBD-ACE2 binding. The negative control peptide had no significant effect. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Techniques Used: Inhibition, Luciferase, Control, Binding Assay, Negative Control, Standard Deviation, Two Tailed Test

    Pseudovirus infectivity assays. ( a ) A schematic illustration for pseudovirus infectivity assay to determine the inhibition ability of the peptides to prevent psuedovirus to enter the cell. ( b ) Pseudovirus infectivity assays indicates that both peptides exhibit similar effects on pseudovirus infected cells. The signal value for pseudovirus infection with no peptide was set to 1.00 and corresponding values were normalized to it. Cells were incubated with pseudovirus in the absence/presence of A13 or Nat1, and infection was measured using a luciferase reporter. Both peptides reduce pseudovirus entry into ACE2-expressing cells. Neither peptide shows any visible effects on the non-peptide sample. Data represents the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).
    Figure Legend Snippet: Pseudovirus infectivity assays. ( a ) A schematic illustration for pseudovirus infectivity assay to determine the inhibition ability of the peptides to prevent psuedovirus to enter the cell. ( b ) Pseudovirus infectivity assays indicates that both peptides exhibit similar effects on pseudovirus infected cells. The signal value for pseudovirus infection with no peptide was set to 1.00 and corresponding values were normalized to it. Cells were incubated with pseudovirus in the absence/presence of A13 or Nat1, and infection was measured using a luciferase reporter. Both peptides reduce pseudovirus entry into ACE2-expressing cells. Neither peptide shows any visible effects on the non-peptide sample. Data represents the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Techniques Used: Infection, Inhibition, Incubation, Luciferase, Expressing, Standard Deviation, Two Tailed Test



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    RBD-ACE2 interaction inhibition assays. ( a ) Schematic illustration of ELISA experiment to evaluate the ability of the A13 or Nat1 to prevent the interaction of SARS-CoV-2 S1 protein RBD to human receptor ACE2. First the plates were incubated with immobilized RBD. They were then inoculated with peptides prior to the addition of recombinant human receptor ACE2. ( b ) Inhibition of RBD-ACE2 binding via A13 or Nat1. The level of RBD-ACE2 binding was measured by chemiluminescence. The negative control with no peptide representing RBD-ACE2 interaction was set to 1.00 (3.2 × 10 4 RLU) and other values were normalized to this number. To the same extent, at the concentration of 0.1 µg/mL, both peptides reduced ACE2 binding compared to the control. At 1.0 µg/mL, inhibition was further enhanced. The negative control peptide did not exhibit a notable inhibition. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001).

    Journal: International Journal of Molecular Sciences

    Article Title: Artificial Intelligence Reveals Nature: Functional Parallels Between a Designed and a Natural Peptide

    doi: 10.3390/ijms262110607

    Figure Lengend Snippet: RBD-ACE2 interaction inhibition assays. ( a ) Schematic illustration of ELISA experiment to evaluate the ability of the A13 or Nat1 to prevent the interaction of SARS-CoV-2 S1 protein RBD to human receptor ACE2. First the plates were incubated with immobilized RBD. They were then inoculated with peptides prior to the addition of recombinant human receptor ACE2. ( b ) Inhibition of RBD-ACE2 binding via A13 or Nat1. The level of RBD-ACE2 binding was measured by chemiluminescence. The negative control with no peptide representing RBD-ACE2 interaction was set to 1.00 (3.2 × 10 4 RLU) and other values were normalized to this number. To the same extent, at the concentration of 0.1 µg/mL, both peptides reduced ACE2 binding compared to the control. At 1.0 µg/mL, inhibition was further enhanced. The negative control peptide did not exhibit a notable inhibition. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001).

    Article Snippet: The ability of the peptides to block the interaction between the RBD and ACE2 was assessed using a commercial ACE2 inhibition assay kit (BPS Bioscience, San Diego, CA, United States, CAT# 79931).

    Techniques: Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, Recombinant, Binding Assay, Negative Control, Concentration Assay, Control, Standard Deviation, Two Tailed Test

    NanoLuc bioreporter assays. ( a ) A schematic illustration for the NanoLuc bioreporter assay to determine SARS-CoV-2 S1 RBD—ACE2 inhibition by A13 or Nat1. ( b ) NanoLuc bioreporter assay indicates that both peptides reduce luciferase complementation to the same extent. The signal value for no peptide control was set to 1.00 (6.30 × 10 5 RLU) and all other values were normalized to it. In cell lysates, A13 and Nat1 both reduced luminescence, indicating inhibition of RBD-ACE2 binding. The negative control peptide had no significant effect. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Journal: International Journal of Molecular Sciences

    Article Title: Artificial Intelligence Reveals Nature: Functional Parallels Between a Designed and a Natural Peptide

    doi: 10.3390/ijms262110607

    Figure Lengend Snippet: NanoLuc bioreporter assays. ( a ) A schematic illustration for the NanoLuc bioreporter assay to determine SARS-CoV-2 S1 RBD—ACE2 inhibition by A13 or Nat1. ( b ) NanoLuc bioreporter assay indicates that both peptides reduce luciferase complementation to the same extent. The signal value for no peptide control was set to 1.00 (6.30 × 10 5 RLU) and all other values were normalized to it. In cell lysates, A13 and Nat1 both reduced luminescence, indicating inhibition of RBD-ACE2 binding. The negative control peptide had no significant effect. Data represent the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Article Snippet: The ability of the peptides to block the interaction between the RBD and ACE2 was assessed using a commercial ACE2 inhibition assay kit (BPS Bioscience, San Diego, CA, United States, CAT# 79931).

    Techniques: Inhibition, Luciferase, Control, Binding Assay, Negative Control, Standard Deviation, Two Tailed Test

    Pseudovirus infectivity assays. ( a ) A schematic illustration for pseudovirus infectivity assay to determine the inhibition ability of the peptides to prevent psuedovirus to enter the cell. ( b ) Pseudovirus infectivity assays indicates that both peptides exhibit similar effects on pseudovirus infected cells. The signal value for pseudovirus infection with no peptide was set to 1.00 and corresponding values were normalized to it. Cells were incubated with pseudovirus in the absence/presence of A13 or Nat1, and infection was measured using a luciferase reporter. Both peptides reduce pseudovirus entry into ACE2-expressing cells. Neither peptide shows any visible effects on the non-peptide sample. Data represents the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Journal: International Journal of Molecular Sciences

    Article Title: Artificial Intelligence Reveals Nature: Functional Parallels Between a Designed and a Natural Peptide

    doi: 10.3390/ijms262110607

    Figure Lengend Snippet: Pseudovirus infectivity assays. ( a ) A schematic illustration for pseudovirus infectivity assay to determine the inhibition ability of the peptides to prevent psuedovirus to enter the cell. ( b ) Pseudovirus infectivity assays indicates that both peptides exhibit similar effects on pseudovirus infected cells. The signal value for pseudovirus infection with no peptide was set to 1.00 and corresponding values were normalized to it. Cells were incubated with pseudovirus in the absence/presence of A13 or Nat1, and infection was measured using a luciferase reporter. Both peptides reduce pseudovirus entry into ACE2-expressing cells. Neither peptide shows any visible effects on the non-peptide sample. Data represents the mean value from at least three independent experiments. Error bars represent standard deviation. Statistical significance was determined using the nonparametric two-tailed Student’s t -test (**** p ≤ 0.0001, ** p ≤ 0.01).

    Article Snippet: The ability of the peptides to block the interaction between the RBD and ACE2 was assessed using a commercial ACE2 inhibition assay kit (BPS Bioscience, San Diego, CA, United States, CAT# 79931).

    Techniques: Infection, Inhibition, Incubation, Luciferase, Expressing, Standard Deviation, Two Tailed Test