insect cells  (Sino Biological)


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    Sino Biological insect cells
    Insect Cells, supplied by Sino Biological, used in various techniques. Bioz Stars score: 86/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/insect cells/product/Sino Biological
    Average 86 stars, based on 32 article reviews
    Price from $9.99 to $1999.99
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    Sino Biological h7n9
    Detection limit of FICT assay for target antigen. FICT employing Europium-conjugated antibodies were tested for the limit of detection (LOD) against <t>H7N9</t> rHA1 ( A ). The data ( n = 3) are shown as mean ± SD. Linear regression is shown with the dotted line. The arrow indicates the antigen concentration of LOD. Raw fluorescence peaks from the test line (TL) and control line (CL) in FICT are shown in the bottom panel.
    H7n9, supplied by Sino Biological, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sino Biological sino biological insect derived sars cov 2 rbd
    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the <t>SARS-CoV-2</t> spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.
    Sino Biological Insect Derived Sars Cov 2 Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sino Biological sars cov 2 nucleocapsid stainingafter staining
    Repurposed library screening for COVID-19 using phenomics A . Syk, c-Met and PI3K inhibitors rescue the severe COVID-19 specific cytokine storm high-dimensional phenoprint (perturbed state) to the healthy phenoprint (target state). B . Example images of target and perturbed cell populations for the cytokine storm and SARS-CoV2 viral models. C . Infection of HRCE yielded a phenoprint against the mock-infected target population with an assay z-factor of 0.43 for the separation in on-perturbation score for the mock and infected populations. D-F . Projections of compound response in the context of the perturbation vector generated in <t>SARS-CoV-2-infected</t> HRCE, Vero, and Calu3 cells. Off-perturbation values clipped at 50 for visualization. G . Compound impact on endothelial barrier function as quantified by ECIS assay. Values are normalized from 0 (cytokine storm cocktail-treated wells) to 100 (mock-treated wells). Data was averaged over a 12-minute window at hour 12 of ECIS measurement to visualize concentration response curves for the indicated compounds. H . Infection rate as determined by SARS-CoV-2 nucleocapsid antibody staining of infected HRCEs treated with the denoted compounds. I . Plot of efficacious molecules by hit-scores in SARS-CoV-2 HRCE assay vs cytokine storm assay. Orange circles denote molecules registered in interventional COVID-19 clinical trials at the time of submission. Dotted lines presented as a visual guide depicting a hit score of 0.6.
    Sars Cov 2 Nucleocapsid Stainingafter Staining, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Detection limit of FICT assay for target antigen. FICT employing Europium-conjugated antibodies were tested for the limit of detection (LOD) against H7N9 rHA1 ( A ). The data ( n = 3) are shown as mean ± SD. Linear regression is shown with the dotted line. The arrow indicates the antigen concentration of LOD. Raw fluorescence peaks from the test line (TL) and control line (CL) in FICT are shown in the bottom panel.

    Journal: Scientific Reports

    Article Title: Improvement of a rapid diagnostic application of monoclonal antibodies against avian influenza H7 subtype virus using Europium nanoparticles

    doi: 10.1038/s41598-017-08328-9

    Figure Lengend Snippet: Detection limit of FICT assay for target antigen. FICT employing Europium-conjugated antibodies were tested for the limit of detection (LOD) against H7N9 rHA1 ( A ). The data ( n = 3) are shown as mean ± SD. Linear regression is shown with the dotted line. The arrow indicates the antigen concentration of LOD. Raw fluorescence peaks from the test line (TL) and control line (CL) in FICT are shown in the bottom panel.

    Article Snippet: Recombinant hemagglutinin 1 (rHA1) of H7N9 (A/Anhui/1/2013) and rHA1 of H5N1 (A/Vietnam/1/2003) were purchased from Sino Biological Inc. (Beijing, China).

    Techniques: Concentration Assay, Fluorescence

    Development of H7 subtype-specific antibodies. The fusions were performed using mouse spleen cells inoculated with H7N9 virus rHA1. Ten hybridomas were produced. The secreted antibodies from each hybridoma were tested for recombinant antigen (H7N9 HA1 ( A ) and different influenza subtype virus ( B ) by indirect ELISA. Pre-immune, serum from a healthy mouse; P.C., positive control antibody (anti-influenza A nucleoprotein antibody).

    Journal: Scientific Reports

    Article Title: Improvement of a rapid diagnostic application of monoclonal antibodies against avian influenza H7 subtype virus using Europium nanoparticles

    doi: 10.1038/s41598-017-08328-9

    Figure Lengend Snippet: Development of H7 subtype-specific antibodies. The fusions were performed using mouse spleen cells inoculated with H7N9 virus rHA1. Ten hybridomas were produced. The secreted antibodies from each hybridoma were tested for recombinant antigen (H7N9 HA1 ( A ) and different influenza subtype virus ( B ) by indirect ELISA. Pre-immune, serum from a healthy mouse; P.C., positive control antibody (anti-influenza A nucleoprotein antibody).

    Article Snippet: Recombinant hemagglutinin 1 (rHA1) of H7N9 (A/Anhui/1/2013) and rHA1 of H5N1 (A/Vietnam/1/2003) were purchased from Sino Biological Inc. (Beijing, China).

    Techniques: Produced, Recombinant, Indirect ELISA, Positive Control

    Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Superimposition of the initial structure (red) and final structure (blue) after 500 ns of simulation of the SARS-CoV-2 spike protein bound to (A) control α1 helix and (B) designed peptide modification 15.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Spike protein (RBD) of SARS-CoV-2 (yellow) and modification 15 (blue) complex from PATCHDOCK prediction. (A) Detailing of the polar interactions between the substituted Glu residue and Lys417. (B) Detailing of the polar interactions determined by acetylated Lys in modification 15. The nonpolar hydrogens were hidden for visualization purpose.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with viral RBD containing the mutation E484K. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from modification 15 (right Y -axis).

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification, Mutagenesis

    RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: RMSD fluctuations of the original 22-mer hACE2 α1 helix (A), NYBSP-4 stapled control (B), modification 15 (C), and modification 11 (D) spike protein of SARS-CoV-2 complexes. The 500 ns MD simulations were monitored with the first frame as a reference. RMSD based on carbon α of the protein (black) (left Y -axis) and ligand RMSD (right Y -axis). Lig fit Prot in blue, and Lig fit Lig in red.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Detailing of the aspartic acid 30 substitution by glutamic acid in modification 15. Spike protein (RBD) of SARS-CoV-2 (yellow). Modification 15 (blue) and hACE2 control (cyan) overlaid. The nonpolar hydrogens were hidden for visualization purpose.

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).

    Journal: The Journal of Physical Chemistry. B

    Article Title: Targeting SARS-CoV-2 Receptor Binding Domain with Stapled Peptides: An In Silico Study

    doi: 10.1021/acs.jpcb.1c02398

    Figure Lengend Snippet: Most persistent interactions ( > 10% of simulation time) from modification 11 (A) and modification 15 (B) with SARS-CoV-2 RBD. Interacting residues from RBD of SARS-CoV-2 (left Y -axis) and from the studied stapled peptides (right Y -axis).

    Article Snippet: Bio-layer interferometry on the top designed peptide showed that the structure presented a dissociation constant, K D , of 1.3 μM for the Sino Biological insect-derived SARS-CoV-2-RBD (the binding of the 23-mer sequence derived from the hACE2 was not reported), a value around 100 times higher compared to the results published by Wrapp et al. for the binding of the hACE2 full length and the spike protein, which determined a K D of ∼14.7 nM.

    Techniques: Modification

    Repurposed library screening for COVID-19 using phenomics A . Syk, c-Met and PI3K inhibitors rescue the severe COVID-19 specific cytokine storm high-dimensional phenoprint (perturbed state) to the healthy phenoprint (target state). B . Example images of target and perturbed cell populations for the cytokine storm and SARS-CoV2 viral models. C . Infection of HRCE yielded a phenoprint against the mock-infected target population with an assay z-factor of 0.43 for the separation in on-perturbation score for the mock and infected populations. D-F . Projections of compound response in the context of the perturbation vector generated in SARS-CoV-2-infected HRCE, Vero, and Calu3 cells. Off-perturbation values clipped at 50 for visualization. G . Compound impact on endothelial barrier function as quantified by ECIS assay. Values are normalized from 0 (cytokine storm cocktail-treated wells) to 100 (mock-treated wells). Data was averaged over a 12-minute window at hour 12 of ECIS measurement to visualize concentration response curves for the indicated compounds. H . Infection rate as determined by SARS-CoV-2 nucleocapsid antibody staining of infected HRCEs treated with the denoted compounds. I . Plot of efficacious molecules by hit-scores in SARS-CoV-2 HRCE assay vs cytokine storm assay. Orange circles denote molecules registered in interventional COVID-19 clinical trials at the time of submission. Dotted lines presented as a visual guide depicting a hit score of 0.6.

    Journal: bioRxiv

    Article Title: Functional immune mapping with deep-learning enabled phenomics applied to immunomodulatory and COVID-19 drug discovery

    doi: 10.1101/2020.08.02.233064

    Figure Lengend Snippet: Repurposed library screening for COVID-19 using phenomics A . Syk, c-Met and PI3K inhibitors rescue the severe COVID-19 specific cytokine storm high-dimensional phenoprint (perturbed state) to the healthy phenoprint (target state). B . Example images of target and perturbed cell populations for the cytokine storm and SARS-CoV2 viral models. C . Infection of HRCE yielded a phenoprint against the mock-infected target population with an assay z-factor of 0.43 for the separation in on-perturbation score for the mock and infected populations. D-F . Projections of compound response in the context of the perturbation vector generated in SARS-CoV-2-infected HRCE, Vero, and Calu3 cells. Off-perturbation values clipped at 50 for visualization. G . Compound impact on endothelial barrier function as quantified by ECIS assay. Values are normalized from 0 (cytokine storm cocktail-treated wells) to 100 (mock-treated wells). Data was averaged over a 12-minute window at hour 12 of ECIS measurement to visualize concentration response curves for the indicated compounds. H . Infection rate as determined by SARS-CoV-2 nucleocapsid antibody staining of infected HRCEs treated with the denoted compounds. I . Plot of efficacious molecules by hit-scores in SARS-CoV-2 HRCE assay vs cytokine storm assay. Orange circles denote molecules registered in interventional COVID-19 clinical trials at the time of submission. Dotted lines presented as a visual guide depicting a hit score of 0.6.

    Article Snippet: SARS-CoV-2 Nucleocapsid stainingAfter staining and imaging to establish high dimensional phenotypes, plates were rinsed once with Wash Buffer (1xHBSS + 0.02% sodium azide) before incubating with primary antibody raised against SARS-CoV-2 nucleocapsid protein for 60 mins at RT (Sino Biological catno.

    Techniques: Library Screening, Infection, Plasmid Preparation, Generated, Electric Cell-substrate Impedance Sensing, Concentration Assay, Staining

    SARS-CoV-2 infection model A . Quantification of active SARS-CoV-2 production over time in the indicated cell types using TCID50 measurement on Vero cells (n=2). B . Representative images of HRCE, Calu3 and Vero cells immunostained with SARS-CoV-2 nucleocapsid protein (pink) and modified cell paint dyes C . Infection rates of each tested cell type as analyzed by nucleocapsid immunostaining. Of note, HRCE donors displayed significant variation in infectability and only a minority of donors exhibited infection rates high enough for screening. Antibody stains were performed after the principal analysis concluded, and are therefore not represented in the primary dataset used for phenoprint evaluation and compound screening. D . Infection of HRCE yielded a phenoprint against the mock-infected target population with an assay z-factor of 0.43 and was selected for further investigation. Vero and Calu3 cells also demonstrated screenable phenoprints. E . Quantification of percentage of cells infected using nucleocapsid protein immunostaining in Calu3 cells at 96 hours post infection for key compounds F . Consistency of hit scores for selected compounds across HRCE donors and between cell types. G . Projections of compound response of JAK inhibitor and control compounds onto the perturbation vector generated in SARS-CoV-2-infected HRCE. H . Quantification of percent of cells infected using nucleocapsid protein immunostaining in HRCE cells at 96 hours post infection for JAK inhibitors

    Journal: bioRxiv

    Article Title: Functional immune mapping with deep-learning enabled phenomics applied to immunomodulatory and COVID-19 drug discovery

    doi: 10.1101/2020.08.02.233064

    Figure Lengend Snippet: SARS-CoV-2 infection model A . Quantification of active SARS-CoV-2 production over time in the indicated cell types using TCID50 measurement on Vero cells (n=2). B . Representative images of HRCE, Calu3 and Vero cells immunostained with SARS-CoV-2 nucleocapsid protein (pink) and modified cell paint dyes C . Infection rates of each tested cell type as analyzed by nucleocapsid immunostaining. Of note, HRCE donors displayed significant variation in infectability and only a minority of donors exhibited infection rates high enough for screening. Antibody stains were performed after the principal analysis concluded, and are therefore not represented in the primary dataset used for phenoprint evaluation and compound screening. D . Infection of HRCE yielded a phenoprint against the mock-infected target population with an assay z-factor of 0.43 and was selected for further investigation. Vero and Calu3 cells also demonstrated screenable phenoprints. E . Quantification of percentage of cells infected using nucleocapsid protein immunostaining in Calu3 cells at 96 hours post infection for key compounds F . Consistency of hit scores for selected compounds across HRCE donors and between cell types. G . Projections of compound response of JAK inhibitor and control compounds onto the perturbation vector generated in SARS-CoV-2-infected HRCE. H . Quantification of percent of cells infected using nucleocapsid protein immunostaining in HRCE cells at 96 hours post infection for JAK inhibitors

    Article Snippet: SARS-CoV-2 Nucleocapsid stainingAfter staining and imaging to establish high dimensional phenotypes, plates were rinsed once with Wash Buffer (1xHBSS + 0.02% sodium azide) before incubating with primary antibody raised against SARS-CoV-2 nucleocapsid protein for 60 mins at RT (Sino Biological catno.

    Techniques: Infection, Modification, Immunostaining, Plasmid Preparation, Generated

    SPR analysis and molecular dynamics analysis of the ACE2 binding compound Evans blue. (A) Graphical representation showing Evans blue identification in the SPR screen. The circled spot is Evans blue (Compounds Australia sample no. SN01005402; molecular weight, 962 g/mol). (B) Sensor gram of the multicycle interaction between Evans blue and ACE2. (C) Competition assay between Evans blue and the RBD-1 peptide for ACE2. The blue line is the peptide injection for the whole injection (injections A, B, and A)–peptide control. Gray line is the Evans blue (injections A, B, and A)–compound-only control. Orange is the peptide (Both A injections) and compound (Evans blue; injection B)–competition curve. (D) Molecular docking results of the highest-affinity ligand Evans blue (also called T-1824) in complex with human ACE2. Evans blue has a K D of 1.6 nM by SPR. Shown in green is the secondary ribbon structure of the S1 RBD of the SARS-CoV-2.

    Journal: mBio

    Article Title: Multidisciplinary Approaches Identify Compounds that Bind to Human ACE2 or SARS-CoV-2 Spike Protein as Candidates to Block SARS-CoV-2–ACE2 Receptor Interactions

    doi: 10.1128/mBio.03681-20

    Figure Lengend Snippet: SPR analysis and molecular dynamics analysis of the ACE2 binding compound Evans blue. (A) Graphical representation showing Evans blue identification in the SPR screen. The circled spot is Evans blue (Compounds Australia sample no. SN01005402; molecular weight, 962 g/mol). (B) Sensor gram of the multicycle interaction between Evans blue and ACE2. (C) Competition assay between Evans blue and the RBD-1 peptide for ACE2. The blue line is the peptide injection for the whole injection (injections A, B, and A)–peptide control. Gray line is the Evans blue (injections A, B, and A)–compound-only control. Orange is the peptide (Both A injections) and compound (Evans blue; injection B)–competition curve. (D) Molecular docking results of the highest-affinity ligand Evans blue (also called T-1824) in complex with human ACE2. Evans blue has a K D of 1.6 nM by SPR. Shown in green is the secondary ribbon structure of the S1 RBD of the SARS-CoV-2.

    Article Snippet: The intracellular SARS-CoV-2 nucleocapsid was immunostained by incubating cells with a 1:2,000 dilution of primary mouse anti-SARS-CoV-2 nucleocapsid antibody (reference no. [ref.] 40143-MM08; SinoBiological) in PBS/5% skim-milk for 30 min at 37°C, and a 1:6,000 dilution of secondary goat anti-mouse IgG(H+L)-horseradish peroxidase (HRP)-conjugated antibody (ref. 170-6516; Bio-Rad) in PBS/5% skim-milk for 30 min at 37°C.

    Techniques: SPR Assay, Binding Assay, Molecular Weight, Competitive Binding Assay, Injection

    The structure of the human ACE2-S1 domain (RBD) of the SARS-CoV spike protein initially used to select regions for the molecular docking screen. The structure was determined using PDB 2AJF ( 53 ). (A) SARS-CoV S spike protein bound to ACE2 with marked ACE2 active site and SARS-CoV S protein interacting site. (B) For molecular docking screening experiments, SARS-CoV S spike protein was removed, and a rectangular box (50 Å by 60 Å by 40 Å) was centered around HIS-34. (C) For molecular docking screening experiments, the structure of the SARS-CoV-2 chimeric receptor-binding domain SARS-CoV-2 (PDB 6VW1 ) was used with 2.68-Å resolution ( 28 ). (D) The human ACE2 protein was removed, and a rectangular box (50 Å by 60 Å by 50 Å) was centered around GLN-493.

    Journal: mBio

    Article Title: Multidisciplinary Approaches Identify Compounds that Bind to Human ACE2 or SARS-CoV-2 Spike Protein as Candidates to Block SARS-CoV-2–ACE2 Receptor Interactions

    doi: 10.1128/mBio.03681-20

    Figure Lengend Snippet: The structure of the human ACE2-S1 domain (RBD) of the SARS-CoV spike protein initially used to select regions for the molecular docking screen. The structure was determined using PDB 2AJF ( 53 ). (A) SARS-CoV S spike protein bound to ACE2 with marked ACE2 active site and SARS-CoV S protein interacting site. (B) For molecular docking screening experiments, SARS-CoV S spike protein was removed, and a rectangular box (50 Å by 60 Å by 40 Å) was centered around HIS-34. (C) For molecular docking screening experiments, the structure of the SARS-CoV-2 chimeric receptor-binding domain SARS-CoV-2 (PDB 6VW1 ) was used with 2.68-Å resolution ( 28 ). (D) The human ACE2 protein was removed, and a rectangular box (50 Å by 60 Å by 50 Å) was centered around GLN-493.

    Article Snippet: The intracellular SARS-CoV-2 nucleocapsid was immunostained by incubating cells with a 1:2,000 dilution of primary mouse anti-SARS-CoV-2 nucleocapsid antibody (reference no. [ref.] 40143-MM08; SinoBiological) in PBS/5% skim-milk for 30 min at 37°C, and a 1:6,000 dilution of secondary goat anti-mouse IgG(H+L)-horseradish peroxidase (HRP)-conjugated antibody (ref. 170-6516; Bio-Rad) in PBS/5% skim-milk for 30 min at 37°C.

    Techniques: Binding Assay

    Screening of approved drugs against SARS-CoV-2 in vitro infection of Vero-E6 cells. Confluent Vero-E6 cells were incubated with virus and compound dilutions for 48 h at 37°C, after which infection was measured with in situ ELISA using a primary SARS-CoV-2 nucleocapsid antibody. Bars represent the average ± standard deviation (SD) of duplicate measurements. Black stars denote obvious compound-induced cytotoxicity.

    Journal: mBio

    Article Title: Multidisciplinary Approaches Identify Compounds that Bind to Human ACE2 or SARS-CoV-2 Spike Protein as Candidates to Block SARS-CoV-2–ACE2 Receptor Interactions

    doi: 10.1128/mBio.03681-20

    Figure Lengend Snippet: Screening of approved drugs against SARS-CoV-2 in vitro infection of Vero-E6 cells. Confluent Vero-E6 cells were incubated with virus and compound dilutions for 48 h at 37°C, after which infection was measured with in situ ELISA using a primary SARS-CoV-2 nucleocapsid antibody. Bars represent the average ± standard deviation (SD) of duplicate measurements. Black stars denote obvious compound-induced cytotoxicity.

    Article Snippet: The intracellular SARS-CoV-2 nucleocapsid was immunostained by incubating cells with a 1:2,000 dilution of primary mouse anti-SARS-CoV-2 nucleocapsid antibody (reference no. [ref.] 40143-MM08; SinoBiological) in PBS/5% skim-milk for 30 min at 37°C, and a 1:6,000 dilution of secondary goat anti-mouse IgG(H+L)-horseradish peroxidase (HRP)-conjugated antibody (ref. 170-6516; Bio-Rad) in PBS/5% skim-milk for 30 min at 37°C.

    Techniques: In Vitro, Infection, Incubation, In Situ, Enzyme-linked Immunosorbent Assay, Standard Deviation