bsa  (Sino Biological)


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    Name:
    Influenza A H7N9 A Shanghai 1 2013 Hemagglutinin HA Protein His Tag
    Description:
    A DNA sequence encoding the Influenza A virus A Shanghai 1 2013 H7N9 hemagglutinin Met1 Val524 was expressed with a C terminal polyhistidine tag
    Catalog Number:
    40104-V08B
    Price:
    None
    Category:
    recombinant protein
    Host:
    Baculovirus-Insect Cells
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    Structured Review

    Sino Biological bsa
    SDF-1α induces expression of active form of E-selectin ligands in EC. ( A ) Increased expression of E-selectin ligand, CD44, in luminal EC of ischemic hindlimb wounds injected with γmSDF-1α compared to PBS injected non-wounded hindlimb in NOD mice (n = 8 mice/group). ( A ) right : Co-expression (yellow) of CD44 (green) and CD31 (red) in vessels was detected by immunostaining. Representative images are shown (images of isotype-matched non-specific control Ab are not shown). Left : Quantification of CD44 expression in vessels. Data are presented as mean ± SD of ratio of CD44:CD31 signals from 5 random selected sections of high power field (LPF, X 20) of each wound sample. CD31 signal was established as “1” in each section and relative amount of CD44 signal was normalized accordingly. ( B ) Immunoblotting analysis of SDF-1α-induced expression of three E-selectin ligands in HMVEC at various time points <t>(γhSDF-1α:</t> 100 ng/ml). β-actin is used as loading control. Experiments were repeated three times and similar results were obtained. ( C ) Binding of FITC-conjugated HECA452 to HMVEC stimulated with γhSDF-1α or <t>BSA.</t> Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). ( D ) Binding of FITC-conjugated HECA452 to human EPC stimulated with γhSDF-1α or BSA (100 ng/ml). Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). Data are analyzed by 2-tailed Student’s t -test and presented as mean ± SEM of fluorescent signals based on triplicate wells in each condition and totally three independent experiments in ( C , D ).
    A DNA sequence encoding the Influenza A virus A Shanghai 1 2013 H7N9 hemagglutinin Met1 Val524 was expressed with a C terminal polyhistidine tag
    https://www.bioz.com/result/bsa/product/Sino Biological
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bsa - by Bioz Stars, 2021-06
    86/100 stars

    Images

    1) Product Images from "SDF-1α-induced dual pairs of E-selectin/ligand mediate endothelial progenitor cell homing to critical ischemia"

    Article Title: SDF-1α-induced dual pairs of E-selectin/ligand mediate endothelial progenitor cell homing to critical ischemia

    Journal: Scientific Reports

    doi: 10.1038/srep34416

    SDF-1α induces expression of active form of E-selectin ligands in EC. ( A ) Increased expression of E-selectin ligand, CD44, in luminal EC of ischemic hindlimb wounds injected with γmSDF-1α compared to PBS injected non-wounded hindlimb in NOD mice (n = 8 mice/group). ( A ) right : Co-expression (yellow) of CD44 (green) and CD31 (red) in vessels was detected by immunostaining. Representative images are shown (images of isotype-matched non-specific control Ab are not shown). Left : Quantification of CD44 expression in vessels. Data are presented as mean ± SD of ratio of CD44:CD31 signals from 5 random selected sections of high power field (LPF, X 20) of each wound sample. CD31 signal was established as “1” in each section and relative amount of CD44 signal was normalized accordingly. ( B ) Immunoblotting analysis of SDF-1α-induced expression of three E-selectin ligands in HMVEC at various time points (γhSDF-1α: 100 ng/ml). β-actin is used as loading control. Experiments were repeated three times and similar results were obtained. ( C ) Binding of FITC-conjugated HECA452 to HMVEC stimulated with γhSDF-1α or BSA. Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). ( D ) Binding of FITC-conjugated HECA452 to human EPC stimulated with γhSDF-1α or BSA (100 ng/ml). Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). Data are analyzed by 2-tailed Student’s t -test and presented as mean ± SEM of fluorescent signals based on triplicate wells in each condition and totally three independent experiments in ( C , D ).
    Figure Legend Snippet: SDF-1α induces expression of active form of E-selectin ligands in EC. ( A ) Increased expression of E-selectin ligand, CD44, in luminal EC of ischemic hindlimb wounds injected with γmSDF-1α compared to PBS injected non-wounded hindlimb in NOD mice (n = 8 mice/group). ( A ) right : Co-expression (yellow) of CD44 (green) and CD31 (red) in vessels was detected by immunostaining. Representative images are shown (images of isotype-matched non-specific control Ab are not shown). Left : Quantification of CD44 expression in vessels. Data are presented as mean ± SD of ratio of CD44:CD31 signals from 5 random selected sections of high power field (LPF, X 20) of each wound sample. CD31 signal was established as “1” in each section and relative amount of CD44 signal was normalized accordingly. ( B ) Immunoblotting analysis of SDF-1α-induced expression of three E-selectin ligands in HMVEC at various time points (γhSDF-1α: 100 ng/ml). β-actin is used as loading control. Experiments were repeated three times and similar results were obtained. ( C ) Binding of FITC-conjugated HECA452 to HMVEC stimulated with γhSDF-1α or BSA. Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). ( D ) Binding of FITC-conjugated HECA452 to human EPC stimulated with γhSDF-1α or BSA (100 ng/ml). Fluorescent signals were quantified ( top ). Representative fluorescent images were exhibited ( bottom ). Data are analyzed by 2-tailed Student’s t -test and presented as mean ± SEM of fluorescent signals based on triplicate wells in each condition and totally three independent experiments in ( C , D ).

    Techniques Used: Expressing, Injection, Mouse Assay, Immunostaining, Binding Assay

    SDF-1α induces E-selectin expression in EPC. ( A ) Levels of mSDF-1α in sera 4 h after wound bed injection of γmSDF-1α vs. PBS (n = 8 mice/group). ( B ) Measurement of levels of E-selectin in BM EPC by flow cytometry. BMC were incubated with Abs against CD34, KDR, and E-selectin or isotype-matched control Abs. EPC (CD34 + /KDR + ) were gated (P2), counted, and analyzed for levels of E-selectin (Q2-1). Bar graphs show % of EPC in BM mononuclear cells and relative levels of E-selectin in BM-EPC. Levels of E-selectin in EPC from mice injected with PBS were established as “1” and relative levels of E-selectin in EPC from mice injected with γmSDF-1α were normalized accordingly (n = 8 mice/group). ( C ) Measurement of % of EPC in peripheral blood MNC and relative levels of E-selectin in circulating EPC as described in ( B ) (n = 8 mice/group). ( D ) Immunoblotting analysis of E-selectin expression upon γhSDF-1α (100 ng/ml) stimulation in human EPC at various time points. β-actin served as a loading control. ( E ) Human EPC were stimulated with γhSDF-1α or BSA for 4 h, and total RNA was extracted. Expression of extracellular matrix and adhesion molecules were analyzed using RT2-PCRArray . Expression of E-selectin was upregulated upon γmSDF-1α stimulation. Levels of mRNA in BSA-treated EPC were established as “1” and compared to those in γmSDF-1α-treated EPC. Experiments were repeated three times in ( D ) and ( E ). Data are analyzed by 2-tailed Student’s t -test and presented as mean ± SEM.
    Figure Legend Snippet: SDF-1α induces E-selectin expression in EPC. ( A ) Levels of mSDF-1α in sera 4 h after wound bed injection of γmSDF-1α vs. PBS (n = 8 mice/group). ( B ) Measurement of levels of E-selectin in BM EPC by flow cytometry. BMC were incubated with Abs against CD34, KDR, and E-selectin or isotype-matched control Abs. EPC (CD34 + /KDR + ) were gated (P2), counted, and analyzed for levels of E-selectin (Q2-1). Bar graphs show % of EPC in BM mononuclear cells and relative levels of E-selectin in BM-EPC. Levels of E-selectin in EPC from mice injected with PBS were established as “1” and relative levels of E-selectin in EPC from mice injected with γmSDF-1α were normalized accordingly (n = 8 mice/group). ( C ) Measurement of % of EPC in peripheral blood MNC and relative levels of E-selectin in circulating EPC as described in ( B ) (n = 8 mice/group). ( D ) Immunoblotting analysis of E-selectin expression upon γhSDF-1α (100 ng/ml) stimulation in human EPC at various time points. β-actin served as a loading control. ( E ) Human EPC were stimulated with γhSDF-1α or BSA for 4 h, and total RNA was extracted. Expression of extracellular matrix and adhesion molecules were analyzed using RT2-PCRArray . Expression of E-selectin was upregulated upon γmSDF-1α stimulation. Levels of mRNA in BSA-treated EPC were established as “1” and compared to those in γmSDF-1α-treated EPC. Experiments were repeated three times in ( D ) and ( E ). Data are analyzed by 2-tailed Student’s t -test and presented as mean ± SEM.

    Techniques Used: Expressing, Injection, Mouse Assay, Flow Cytometry, Incubation

    2) Product Images from "Nanodiamond enhances immune responses in mice against recombinant HA/H7N9 protein"

    Article Title: Nanodiamond enhances immune responses in mice against recombinant HA/H7N9 protein

    Journal: Journal of Nanobiotechnology

    doi: 10.1186/s12951-017-0305-2

    Immunopotentiation following immunization with an H7:ND (1/12, w/w) conjugate. a Immunization scheme in mice. b Measurement of H7 specific IgG amount in mouse sera via ELISA. In total, 50 ng of purified H7 [Influenza antigen A/Anhui/1/2013 (H7N9), NIBSC] per well were coated at the plate. The sera were diluted 1:5000 and a monoclonal mouse anti- H7N9 haemagglutinin/HA antibody (SinoBiological InC.) at concentrations of 0.5, 0.75, 1, 1.25, 2.5, 5, 12.5, 25, 50, 100, 150 μg/mL was applied as a standard, then analysed via ELISA. Specific immune responses were measured at 450 nm after 1 and 2 booster immunizations with H7 (group 1), H7:ND (group 2) and PBS:ND (group 3). The responses were recalculated according the standard values as µg/mL anti H7N9 antibody in the sera. The BSA background was subtracted. A standard curve was built by the help of OD450 values corresponding to known amounts of H7N9 haemagglutinin/HA antibody. The amount of H7 specific IgG antibody in mouse sera was measured via the standard curve. Statistical analyses were performed using the t-test (SigmaPlot) and are presented. A single dot indicates the value of a single mouse serum. SD was included on a single dot that corresponds to an ELISA data variation of a single mouse serum with three replications. The bars indicate the average value of the test groups. P
    Figure Legend Snippet: Immunopotentiation following immunization with an H7:ND (1/12, w/w) conjugate. a Immunization scheme in mice. b Measurement of H7 specific IgG amount in mouse sera via ELISA. In total, 50 ng of purified H7 [Influenza antigen A/Anhui/1/2013 (H7N9), NIBSC] per well were coated at the plate. The sera were diluted 1:5000 and a monoclonal mouse anti- H7N9 haemagglutinin/HA antibody (SinoBiological InC.) at concentrations of 0.5, 0.75, 1, 1.25, 2.5, 5, 12.5, 25, 50, 100, 150 μg/mL was applied as a standard, then analysed via ELISA. Specific immune responses were measured at 450 nm after 1 and 2 booster immunizations with H7 (group 1), H7:ND (group 2) and PBS:ND (group 3). The responses were recalculated according the standard values as µg/mL anti H7N9 antibody in the sera. The BSA background was subtracted. A standard curve was built by the help of OD450 values corresponding to known amounts of H7N9 haemagglutinin/HA antibody. The amount of H7 specific IgG antibody in mouse sera was measured via the standard curve. Statistical analyses were performed using the t-test (SigmaPlot) and are presented. A single dot indicates the value of a single mouse serum. SD was included on a single dot that corresponds to an ELISA data variation of a single mouse serum with three replications. The bars indicate the average value of the test groups. P

    Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay, Purification

    3) Product Images from "Machine Learning-Guided Prediction of Antigen-Reactive In Silico Clonotypes Based on Changes in Clonal Abundance through Bio-Panning"

    Article Title: Machine Learning-Guided Prediction of Antigen-Reactive In Silico Clonotypes Based on Changes in Clonal Abundance through Bio-Panning

    Journal: Biomolecules

    doi: 10.3390/biom10030421

    Reactivity of phage-displayed scFv clones in phage ELISA. Binding reactivity of 15 unique clones identified from the AR library and 16 unique clones from the NR library are shown. Wells in microtiter plates were either coated with recombinant mouse c-Met or just blocked with 3% BSA in PBS. Phage clones, HRP-conjugated anti-M13 antibody, and HRP substrate solution were added sequentially with intermittent washing.
    Figure Legend Snippet: Reactivity of phage-displayed scFv clones in phage ELISA. Binding reactivity of 15 unique clones identified from the AR library and 16 unique clones from the NR library are shown. Wells in microtiter plates were either coated with recombinant mouse c-Met or just blocked with 3% BSA in PBS. Phage clones, HRP-conjugated anti-M13 antibody, and HRP substrate solution were added sequentially with intermittent washing.

    Techniques Used: Clone Assay, Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant

    4) Product Images from "A Recombinant Secondary Antibody Mimic as a Target-specific Signal Amplifier and an Antibody Immobilizer in Immunoassays"

    Article Title: A Recombinant Secondary Antibody Mimic as a Target-specific Signal Amplifier and an Antibody Immobilizer in Immunoassays

    Journal: Scientific Reports

    doi: 10.1038/srep24159

    HRP-GST-ABD mimics signal-amplifying secondary antibodies in indirect ELISA. ( A ) Scheme showing different combinations of primary antibodies with either HRP-conjugated secondary antibodies or HRP-GST-ABD. ( B – E ) BSA ( B , C ) or EpCAM ( D , E ) are immobilized on the surface of the ELISA plates and various concentrations of either rabbit anti-BSA ( B ) or mouse anti-BSA primary antibodies ( C ) or either rabbit anti-EpCAM ( D ) or mouse anti-EpCAM primary antibodies ( E ) are applied. Linear responses of each measurement are plotted as insets of each graph.
    Figure Legend Snippet: HRP-GST-ABD mimics signal-amplifying secondary antibodies in indirect ELISA. ( A ) Scheme showing different combinations of primary antibodies with either HRP-conjugated secondary antibodies or HRP-GST-ABD. ( B – E ) BSA ( B , C ) or EpCAM ( D , E ) are immobilized on the surface of the ELISA plates and various concentrations of either rabbit anti-BSA ( B ) or mouse anti-BSA primary antibodies ( C ) or either rabbit anti-EpCAM ( D ) or mouse anti-EpCAM primary antibodies ( E ) are applied. Linear responses of each measurement are plotted as insets of each graph.

    Techniques Used: Indirect ELISA, Enzyme-linked Immunosorbent Assay

    GST-ABD serves as an anchoring adaptor on the surface of GSH-coated plates for immobilizing antigen-capturing anti-bodies in an orientation-controlled manner in sandwich-type indirect ELISA. ( A ) Scheme showing the adaptation of GST-ABD as an anchoring adaptor for antigen-capturing antibodies. ( B , C ) GST-ABDs are spread on the surface of GSH-coated plates and saturated with capturing antibodies, either anti-BSA rabbit IgGs ( B ) or anti-EpCAM rabbit IgGs ( C ). Various amounts of BSA ( B ) or EpCAM ( C ) are added. Linear responses for each measurement are plotted as insets of each graph.
    Figure Legend Snippet: GST-ABD serves as an anchoring adaptor on the surface of GSH-coated plates for immobilizing antigen-capturing anti-bodies in an orientation-controlled manner in sandwich-type indirect ELISA. ( A ) Scheme showing the adaptation of GST-ABD as an anchoring adaptor for antigen-capturing antibodies. ( B , C ) GST-ABDs are spread on the surface of GSH-coated plates and saturated with capturing antibodies, either anti-BSA rabbit IgGs ( B ) or anti-EpCAM rabbit IgGs ( C ). Various amounts of BSA ( B ) or EpCAM ( C ) are added. Linear responses for each measurement are plotted as insets of each graph.

    Techniques Used: Indirect ELISA

    5) Product Images from "Serum-Dependence of Affinity-Mediated VEGF Release from Biomimetic Microspheres"

    Article Title: Serum-Dependence of Affinity-Mediated VEGF Release from Biomimetic Microspheres

    Journal: Biomacromolecules

    doi: 10.1021/bm500177c

    (A–H) Fractional cumulative release of VEGF measured from binding in 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF in various loading solutions containing albumin-only or serum. Release of bound VEGF from 0.4% microspheres (A–D) and 1.6% microspheres (E–H) was measured in albumin-only, 1.25 wt % BSA in PBS solution (A,E), 2 vol % serum in PBS (B,F), 10 vol % serum in PBS (C,G), and 25 vol % serum in PBS (D,H).
    Figure Legend Snippet: (A–H) Fractional cumulative release of VEGF measured from binding in 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF in various loading solutions containing albumin-only or serum. Release of bound VEGF from 0.4% microspheres (A–D) and 1.6% microspheres (E–H) was measured in albumin-only, 1.25 wt % BSA in PBS solution (A,E), 2 vol % serum in PBS (B,F), 10 vol % serum in PBS (C,G), and 25 vol % serum in PBS (D,H).

    Techniques Used: Binding Assay

    Modeling correlations to experimental release from microspheres. (A) Replot of VEGF released from Blank (red diamonds), 1.6% Scramble (blue diamonds), and 1.6% VBP (black diamonds) microspheres preincubated in 0.1 wt % BSA in PBS supplemented with 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF. Subsequent release was measured in 0.1 wt % BSA in PBS without VEGF supplementation. Data is fit to model of normalized VEGF flux from Blank microspheres exhibiting passive diffusion of VEGF from Blank microspheres (red dotted line; R 2 = 0.916), Scramble microspheres (blue dotted line; R 2 = 0.954) and from VBP microspheres (black dotted line; R 2 = 0.952). (B) Plot of normalized VEGF release from 1.6% VBP microspheres in albumin-only solution supplemented with 10 ng mL –1 sFlt-1 (red diamonds). VEGF release data in sFlt-1 is fit to model of normalized VEGF flux from 1.6% VBP microspheres releasing into solution containing no protein, sFlt-1 (red dotted line; R 2 = 0.98). Graph also contains a replot of normalized VEGF release data from 1.6% VBP microspheres in 25 vol % serum (blue diamonds) and modeling results for VEGF release into albumin-only solution (black dotted line). Experimental VEGF release data in 25 vol % serum is fit to model of normalized flux from 1.6% VBP microspheres releasing into solution containing physiologic concentrations of three serum proteins, sFlt-1, sKDR, and α2 M (blue dotted line; R 2 = 0.99).
    Figure Legend Snippet: Modeling correlations to experimental release from microspheres. (A) Replot of VEGF released from Blank (red diamonds), 1.6% Scramble (blue diamonds), and 1.6% VBP (black diamonds) microspheres preincubated in 0.1 wt % BSA in PBS supplemented with 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF. Subsequent release was measured in 0.1 wt % BSA in PBS without VEGF supplementation. Data is fit to model of normalized VEGF flux from Blank microspheres exhibiting passive diffusion of VEGF from Blank microspheres (red dotted line; R 2 = 0.916), Scramble microspheres (blue dotted line; R 2 = 0.954) and from VBP microspheres (black dotted line; R 2 = 0.952). (B) Plot of normalized VEGF release from 1.6% VBP microspheres in albumin-only solution supplemented with 10 ng mL –1 sFlt-1 (red diamonds). VEGF release data in sFlt-1 is fit to model of normalized VEGF flux from 1.6% VBP microspheres releasing into solution containing no protein, sFlt-1 (red dotted line; R 2 = 0.98). Graph also contains a replot of normalized VEGF release data from 1.6% VBP microspheres in 25 vol % serum (blue diamonds) and modeling results for VEGF release into albumin-only solution (black dotted line). Experimental VEGF release data in 25 vol % serum is fit to model of normalized flux from 1.6% VBP microspheres releasing into solution containing physiologic concentrations of three serum proteins, sFlt-1, sKDR, and α2 M (blue dotted line; R 2 = 0.99).

    Techniques Used: Diffusion-based Assay

    Influence of peptide concentration on VEGF release from microspheres. (A) Schematic of VEGF release from PEG microspheres in albumin-only (Serum-Free) solution. Top panel: Blank (no peptide) PEG microspheres imaged with phase contrast, under 20X objective with an Olympus IX51 inverted epifluorescence microscope. Schematic shows VEGF-bound state of a microsphere (in red), followed by a change in time and subsequent release of VEGF from the PEG microsphere. (B–E) Fractional cumulative VEGF release from PEG microspheres that were incubated in 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF in 0.1 wt % BSA in PBS at various peptide concentrations in % of norbornene groups functionalized with peptide. Graphs represent PEG microspheres containing 0.4% peptide (B), 0.8% peptide (C), 1.6% peptide (D) and 3.2% peptide (E). Fractional release was calculated by dividing the release at each time point by the cumulative amount of VEGF released at the final time point.
    Figure Legend Snippet: Influence of peptide concentration on VEGF release from microspheres. (A) Schematic of VEGF release from PEG microspheres in albumin-only (Serum-Free) solution. Top panel: Blank (no peptide) PEG microspheres imaged with phase contrast, under 20X objective with an Olympus IX51 inverted epifluorescence microscope. Schematic shows VEGF-bound state of a microsphere (in red), followed by a change in time and subsequent release of VEGF from the PEG microsphere. (B–E) Fractional cumulative VEGF release from PEG microspheres that were incubated in 9.9 ng mL –1 VEGF, 0.1 ng mL –1 [ 125 I]VEGF in 0.1 wt % BSA in PBS at various peptide concentrations in % of norbornene groups functionalized with peptide. Graphs represent PEG microspheres containing 0.4% peptide (B), 0.8% peptide (C), 1.6% peptide (D) and 3.2% peptide (E). Fractional release was calculated by dividing the release at each time point by the cumulative amount of VEGF released at the final time point.

    Techniques Used: Concentration Assay, Inverted Epifluorescence, Incubation

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: Simultaneous Targeting of Multiple Hemagglutinins to APCs for Induction of Broad Immunity against Influenza
    Article Snippet: .. ELISA 96-well plates (Costar 3590) were coated with one of the following recombinant influenza HA proteins: PR8 (11684-V08H; Sino Biological), A/Hong Kong/483/97 (H5N1) (11689-V08H; Sino Biological), A/northern shoveler/California/HKWF115/07 (H6N1) (MBS434125; MyBioSource, San Diego, CA, or 11723-V08H; Sino Biological), A/pintail duck/Alberta/114/1979 (H8N4) (11722-V08H; Sino Biological), A/Hong Kong/1073/99 (H9N2) (11229-V08H; Sino Biological), A/duck/Yangzhou/906/2002 (H11N2) (11705-V08H; Sino Biological), A/black-headed gull/Netherlands/1/00 (H13N8) (11721-V08H; Sino Biological), A/Shanghai/1/2013 (H7N9) (40104-V08B; Sino Biological), or A/Hong Kong/1/1968 (H3N2) (40116-V08B; Sino Biological). .. Alternatively, plates were coated with inactivated virus: PR8 (1:1600; Charles River, Wilmington, MA) or Cal07 (Pandemrix; 1:50; GlaxoSmithKline, Brentford, U.K.).

    Article Title: A DNA Vaccine That Targets Hemagglutinin to Antigen-Presenting Cells Protects Mice against H7 Influenza
    Article Snippet: Blood was harvested by puncture of the saphenous vein, and sera were isolated by centrifugation. .. ELISA plates (Costar 3590) were coated with 0.5 μg/ml recombinant HA [A/Shanghai/1/2013 (H7N9)] (40104-V08B; Sino Biological), blocked with 1% BSA, and incubated with serially diluted serum samples assayed individually (n = 6 to 12/group). .. HA-specific antibodies were detected with alkaline phosphatase conjugated goat anti-mouse IgG (A1418; Sigma-Aldrich), developed with phosphatase substrate (P4744; Sigma-Aldrich) and analyzed as previously described.

    Recombinant:

    Article Title: Simultaneous Targeting of Multiple Hemagglutinins to APCs for Induction of Broad Immunity against Influenza
    Article Snippet: .. ELISA 96-well plates (Costar 3590) were coated with one of the following recombinant influenza HA proteins: PR8 (11684-V08H; Sino Biological), A/Hong Kong/483/97 (H5N1) (11689-V08H; Sino Biological), A/northern shoveler/California/HKWF115/07 (H6N1) (MBS434125; MyBioSource, San Diego, CA, or 11723-V08H; Sino Biological), A/pintail duck/Alberta/114/1979 (H8N4) (11722-V08H; Sino Biological), A/Hong Kong/1073/99 (H9N2) (11229-V08H; Sino Biological), A/duck/Yangzhou/906/2002 (H11N2) (11705-V08H; Sino Biological), A/black-headed gull/Netherlands/1/00 (H13N8) (11721-V08H; Sino Biological), A/Shanghai/1/2013 (H7N9) (40104-V08B; Sino Biological), or A/Hong Kong/1/1968 (H3N2) (40116-V08B; Sino Biological). .. Alternatively, plates were coated with inactivated virus: PR8 (1:1600; Charles River, Wilmington, MA) or Cal07 (Pandemrix; 1:50; GlaxoSmithKline, Brentford, U.K.).

    Article Title: A DNA Vaccine That Targets Hemagglutinin to Antigen-Presenting Cells Protects Mice against H7 Influenza
    Article Snippet: Blood was harvested by puncture of the saphenous vein, and sera were isolated by centrifugation. .. ELISA plates (Costar 3590) were coated with 0.5 μg/ml recombinant HA [A/Shanghai/1/2013 (H7N9)] (40104-V08B; Sino Biological), blocked with 1% BSA, and incubated with serially diluted serum samples assayed individually (n = 6 to 12/group). .. HA-specific antibodies were detected with alkaline phosphatase conjugated goat anti-mouse IgG (A1418; Sigma-Aldrich), developed with phosphatase substrate (P4744; Sigma-Aldrich) and analyzed as previously described.

    Incubation:

    Article Title: A DNA Vaccine That Targets Hemagglutinin to Antigen-Presenting Cells Protects Mice against H7 Influenza
    Article Snippet: Blood was harvested by puncture of the saphenous vein, and sera were isolated by centrifugation. .. ELISA plates (Costar 3590) were coated with 0.5 μg/ml recombinant HA [A/Shanghai/1/2013 (H7N9)] (40104-V08B; Sino Biological), blocked with 1% BSA, and incubated with serially diluted serum samples assayed individually (n = 6 to 12/group). .. HA-specific antibodies were detected with alkaline phosphatase conjugated goat anti-mouse IgG (A1418; Sigma-Aldrich), developed with phosphatase substrate (P4744; Sigma-Aldrich) and analyzed as previously described.

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    Sino Biological sars cov 2 antigen s protein
    Detection of <t>SARS-CoV-2</t> pseudovirus. (A) T 1 s that measured during the reaction procedure between GPG-Ab and pseudovirus. (B) Detection sensitivity for pseudovirus. Error bars indicate SD. *P
    Sars Cov 2 Antigen S Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sars cov 2 antigen s protein/product/Sino Biological
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    99
    Sino Biological sars cov 2 s protein
    Anti-severe acute respiratory syndrome virus 2 <t>(SARS-CoV-2)</t> effects of aprotinin and SERPINA1/alpha-1 antitrypsin. ( A ) Concentration-dependent effects of aprotinin and SERPINA1/alpha-1 antitrypsin on SARS-CoV-2-induced cytopathogenic effect (CPE) formation determined 48 h post-infection in Caco2 cells infected at a multiplicity of infection (MOI) of 0.01 with the three different SARS-CoV-2 isolates. The viability of the Caco2 cells was 84.3 ± 2.7% relative to the untreated control in the presence of 20 µM of aprotinin. ( B ) Immunostaining for the SARS-CoV-2 S protein in aprotinin- and SERPINA1/alpha-1 antitrypsin-treated Caco2 cells infected at an MOI of 0.01 with the three different SARS-CoV-2 isolates as determined 48 h post-infection. The protease inhibitors were tested at four concentrations in 1:4 dilution steps ranging from 20 to 0.3125 µM. A quantification is provided in Figure S1 . ( C ) Copy numbers of genomic RNA in Caco2 cells infected with different SARS-CoV-2 isolates (MOI of 0.01) in response to treatment with aprotinin or SERPINA1/alpha-1 antitrypsin as determined 48 h post-infection. FFM1, 1/Human/2020/Frankfurt; FFM2, 2/Human/2020/Frankfurt; FFM6, 6/Human/2020/Frankfurt.
    Sars Cov 2 S Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sars cov 2 s protein/product/Sino Biological
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sars cov 2 s protein - by Bioz Stars, 2021-06
    99/100 stars
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    94
    Sino Biological recombinant sars cov 2 s protein
    Site-specific N-glycosylation of recombinant <t>SARS-CoV-2</t> S proteins. (A and B) The number of intact N-glycopeptides and N-glycans in recombinant SARS-CoV-2 S proteins expressed in insect cells (A) or human cells (B). (C and D) The numbers of the N-glycosites containing one representative N-glycan and its deduced structure from the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (C) and human cells (D). (E and F) Different types and numbers of N-glycan compositions on each N-glycosite of the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (E) or human cells (F). The size of the pies represents the number of N-glycan compositions.
    Recombinant Sars Cov 2 S Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Detection of SARS-CoV-2 pseudovirus. (A) T 1 s that measured during the reaction procedure between GPG-Ab and pseudovirus. (B) Detection sensitivity for pseudovirus. Error bars indicate SD. *P

    Journal: Sensors and Actuators. B, Chemical

    Article Title: Magnetic graphene quantum dots facilitate closed-tube one-step detection of SARS-CoV-2 with ultra-low field NMR relaxometry

    doi: 10.1016/j.snb.2021.129786

    Figure Lengend Snippet: Detection of SARS-CoV-2 pseudovirus. (A) T 1 s that measured during the reaction procedure between GPG-Ab and pseudovirus. (B) Detection sensitivity for pseudovirus. Error bars indicate SD. *P

    Article Snippet: The SARS-CoV-2 antigen S protein was purchased from Sino Biological Inc. (Beijing, China).

    Techniques:

    Antibody response following LUNAR-COV19 vaccination (A) BALB/c and C57BL/6J mice were i.m. immunized with 0.2 μg, 2 μg, or 10 μg of LUNAR-COV19 or conventional mRNA control (n = 5/group). Blood sampling was conducted at baseline and days 10, 19, 30, 40, 50, and 60 post-vaccination for BALB/c and days 10, 20, and 30 for C57BL/6J. (B–E) IgM (B and C) and IgG (D and E) against the SARS-CoV-2 Spike protein over time, assessed with insect cell-derived whole Spike protein in a Luminex immuno-assay (measured as MFI). (F and G) IgG endpoint titers to mammalian-derived whole Spike protein and S1, S2, and RBD proteins to mammalian-derived whole Spike protein at day 30 post-vaccination were assessed in BALB/c (F) and C57BL/6J (G). (H) Avidity of SARS-CoV-2 Spike protein-specific IgG at day 30 post-immunization was measured with 8 M urea washes. (I) Neutralizing antibody (PRNT 50 titers) at day 30 post-vaccination against a clinically isolated live SARS-CoV-2 virus measured in both BALB/c and C57BL/6J. Gray dashed lines depict the serum dilution range (i.e., from 1:20 to 1:320) tested by PRNT. (J and K) PRNT 50 (J) and PRNT 70 (K) of SARS-CoV-2 neutralization at day 30 and day 60 post-vaccination in BALB/c and convalescent sera from COVID-19 patients. (L) Correlation analysis of Spike-specific IgG endpoint titers against SARS-CoV-2 neutralization (PRNT 50 ). Antibody data were compared between groups with a two-tailed Mann-Whitney U test; ∗0.05

    Journal: Molecular Therapy

    Article Title: A single dose of self-transcribing and replicating RNA-based SARS-CoV-2 vaccine produces protective adaptive immunity in mice

    doi: 10.1016/j.ymthe.2021.04.001

    Figure Lengend Snippet: Antibody response following LUNAR-COV19 vaccination (A) BALB/c and C57BL/6J mice were i.m. immunized with 0.2 μg, 2 μg, or 10 μg of LUNAR-COV19 or conventional mRNA control (n = 5/group). Blood sampling was conducted at baseline and days 10, 19, 30, 40, 50, and 60 post-vaccination for BALB/c and days 10, 20, and 30 for C57BL/6J. (B–E) IgM (B and C) and IgG (D and E) against the SARS-CoV-2 Spike protein over time, assessed with insect cell-derived whole Spike protein in a Luminex immuno-assay (measured as MFI). (F and G) IgG endpoint titers to mammalian-derived whole Spike protein and S1, S2, and RBD proteins to mammalian-derived whole Spike protein at day 30 post-vaccination were assessed in BALB/c (F) and C57BL/6J (G). (H) Avidity of SARS-CoV-2 Spike protein-specific IgG at day 30 post-immunization was measured with 8 M urea washes. (I) Neutralizing antibody (PRNT 50 titers) at day 30 post-vaccination against a clinically isolated live SARS-CoV-2 virus measured in both BALB/c and C57BL/6J. Gray dashed lines depict the serum dilution range (i.e., from 1:20 to 1:320) tested by PRNT. (J and K) PRNT 50 (J) and PRNT 70 (K) of SARS-CoV-2 neutralization at day 30 and day 60 post-vaccination in BALB/c and convalescent sera from COVID-19 patients. (L) Correlation analysis of Spike-specific IgG endpoint titers against SARS-CoV-2 neutralization (PRNT 50 ). Antibody data were compared between groups with a two-tailed Mann-Whitney U test; ∗0.05

    Article Snippet: Similar Luminex immuno-assays have been previously described for antibody detection against SARS-CoV-2 antigens., Briefly, MAGPIX Luminex beads were covalently conjugated to insect-derived HIS-tagged SARS-CoV-2 whole S protein (Sino Biological) with the ABC coupling kit (Thermo) as per manufacturer’s instructions.

    Techniques: Mouse Assay, Sampling, Derivative Assay, Luminex, Immuno Assay, Plaque Reduction Neutralization Test, Isolation, Neutralization, Two Tailed Test, MANN-WHITNEY

    LUNAR-COV19 elicits Th1-biased immune responses (A and B) SARS-CoV-2 spike-specific IgG subclasses and the ratio of IgG2a / c/IgG1 at 30 days post-vaccination with LUNAR-COV19 compared with conventional mRNA control in BALB/c (A) and C57BL/6J (B) mice (n = 5/group). (C and D) Th2 cytokine and Th1/Th2 skew in CD4 T cells at day 7 post-vaccination in C57BL/6J mice measured by ICS as percentage of IL-4+ CD4 T cells (C) and ratio of IFNγ + /IL-4 + CD4 + T cells (D). Antibody titers and T cell data were compared between groups with a two-tailed Mann-Whitney U test; ∗0.05

    Journal: Molecular Therapy

    Article Title: A single dose of self-transcribing and replicating RNA-based SARS-CoV-2 vaccine produces protective adaptive immunity in mice

    doi: 10.1016/j.ymthe.2021.04.001

    Figure Lengend Snippet: LUNAR-COV19 elicits Th1-biased immune responses (A and B) SARS-CoV-2 spike-specific IgG subclasses and the ratio of IgG2a / c/IgG1 at 30 days post-vaccination with LUNAR-COV19 compared with conventional mRNA control in BALB/c (A) and C57BL/6J (B) mice (n = 5/group). (C and D) Th2 cytokine and Th1/Th2 skew in CD4 T cells at day 7 post-vaccination in C57BL/6J mice measured by ICS as percentage of IL-4+ CD4 T cells (C) and ratio of IFNγ + /IL-4 + CD4 + T cells (D). Antibody titers and T cell data were compared between groups with a two-tailed Mann-Whitney U test; ∗0.05

    Article Snippet: Similar Luminex immuno-assays have been previously described for antibody detection against SARS-CoV-2 antigens., Briefly, MAGPIX Luminex beads were covalently conjugated to insect-derived HIS-tagged SARS-CoV-2 whole S protein (Sino Biological) with the ABC coupling kit (Thermo) as per manufacturer’s instructions.

    Techniques: Mouse Assay, Two Tailed Test, MANN-WHITNEY

    Cellular immune responses following vaccination with LUNAR-COV19 C57BL/6 mice (n = 5 per group) were immunized i.m. with 0.2 μg, 2.0 μg, or 10.0 μg of LUNAR-COV19 or conventional mRNA control and sacrificed at day 7 post-vaccination, and spleens were analyzed for cellular T cell responses by flow cytometry and ELISpot. (A–C) CD8 + (A and B) and CD4 + (C) T effector cells were assessed in vaccinated animals with surface staining for T cell markers and flow cytometry. (D–F) IFNγ + CD8 + T cells (D and E) and ratio of IFNγ + IL-4 + CD4 + T cells (F) in spleens of immunized mice were assessed after ex vivo stimulation with PMA/IO and intracellular staining. (G and H) SARS-CoV-2 Spike protein-specific responses to pooled Spike protein peptides were assessed with IFNγ ELISpot assays after vaccination with conventional mRNA controls or LUNAR-COV19. Percentage of CD8+ cells, CD4+ cells, and IFNγ- and IL-4-producing T cells were compared between groups with two-tailed Mann-Whitney U test; ∗0.05

    Journal: Molecular Therapy

    Article Title: A single dose of self-transcribing and replicating RNA-based SARS-CoV-2 vaccine produces protective adaptive immunity in mice

    doi: 10.1016/j.ymthe.2021.04.001

    Figure Lengend Snippet: Cellular immune responses following vaccination with LUNAR-COV19 C57BL/6 mice (n = 5 per group) were immunized i.m. with 0.2 μg, 2.0 μg, or 10.0 μg of LUNAR-COV19 or conventional mRNA control and sacrificed at day 7 post-vaccination, and spleens were analyzed for cellular T cell responses by flow cytometry and ELISpot. (A–C) CD8 + (A and B) and CD4 + (C) T effector cells were assessed in vaccinated animals with surface staining for T cell markers and flow cytometry. (D–F) IFNγ + CD8 + T cells (D and E) and ratio of IFNγ + IL-4 + CD4 + T cells (F) in spleens of immunized mice were assessed after ex vivo stimulation with PMA/IO and intracellular staining. (G and H) SARS-CoV-2 Spike protein-specific responses to pooled Spike protein peptides were assessed with IFNγ ELISpot assays after vaccination with conventional mRNA controls or LUNAR-COV19. Percentage of CD8+ cells, CD4+ cells, and IFNγ- and IL-4-producing T cells were compared between groups with two-tailed Mann-Whitney U test; ∗0.05

    Article Snippet: Similar Luminex immuno-assays have been previously described for antibody detection against SARS-CoV-2 antigens., Briefly, MAGPIX Luminex beads were covalently conjugated to insect-derived HIS-tagged SARS-CoV-2 whole S protein (Sino Biological) with the ABC coupling kit (Thermo) as per manufacturer’s instructions.

    Techniques: Mouse Assay, Flow Cytometry, Enzyme-linked Immunospot, Staining, Ex Vivo, Two Tailed Test, MANN-WHITNEY

    Design and expression of a SARS-COV-2 vaccine with conventional mRNA and self-transcribing and replicating RNA (STARR) platforms (A) Schematic diagram of the SARS-CoV-2 self-replicating STARR RNA (LUNAR-COV19) and conventional mRNA vaccine constructs. The STARR construct encodes for the four non-structural proteins, ns1–ns4, from Venezuelan equine encephalitis virus (VEEV) and the unmodified full-length pre-fusion spike protein of SARS-CoV-2. The mRNA construct also codes for the same SARS-CoV-2 full-length spike protein. (B) Physical characteristics and RNA trapping efficiency of the LNPs encapsulating conventional mRNA and LUNAR-COV19 vaccines. (C) Western blot detection of SARS-CoV-2 Spike protein following transfection of Hep3b cells with LUNAR-COV19 and conventional mRNA. (D) In vivo comparison of protein expression following i.m. administration of LNPs containing luciferase-expressing STARR RNA or conventional mRNA. BALB/c mice (n = 3/group) were injected i.m. with 0.2 μg, 2.0 μg, or 10.0 μg of STARR RNA or conventional mRNA formulated with the same LNPs. Luciferase expression was measured by in vivo bioluminescence on days 1, 3, and 7 post-i.m. administration. Results are shown as mean with standard deviation error bars. S1, S domain 1; S2, S domain 2; TM, transmembrane domain; CP, cytoplasmic domain; aka, also known as.

    Journal: Molecular Therapy

    Article Title: A single dose of self-transcribing and replicating RNA-based SARS-CoV-2 vaccine produces protective adaptive immunity in mice

    doi: 10.1016/j.ymthe.2021.04.001

    Figure Lengend Snippet: Design and expression of a SARS-COV-2 vaccine with conventional mRNA and self-transcribing and replicating RNA (STARR) platforms (A) Schematic diagram of the SARS-CoV-2 self-replicating STARR RNA (LUNAR-COV19) and conventional mRNA vaccine constructs. The STARR construct encodes for the four non-structural proteins, ns1–ns4, from Venezuelan equine encephalitis virus (VEEV) and the unmodified full-length pre-fusion spike protein of SARS-CoV-2. The mRNA construct also codes for the same SARS-CoV-2 full-length spike protein. (B) Physical characteristics and RNA trapping efficiency of the LNPs encapsulating conventional mRNA and LUNAR-COV19 vaccines. (C) Western blot detection of SARS-CoV-2 Spike protein following transfection of Hep3b cells with LUNAR-COV19 and conventional mRNA. (D) In vivo comparison of protein expression following i.m. administration of LNPs containing luciferase-expressing STARR RNA or conventional mRNA. BALB/c mice (n = 3/group) were injected i.m. with 0.2 μg, 2.0 μg, or 10.0 μg of STARR RNA or conventional mRNA formulated with the same LNPs. Luciferase expression was measured by in vivo bioluminescence on days 1, 3, and 7 post-i.m. administration. Results are shown as mean with standard deviation error bars. S1, S domain 1; S2, S domain 2; TM, transmembrane domain; CP, cytoplasmic domain; aka, also known as.

    Article Snippet: Similar Luminex immuno-assays have been previously described for antibody detection against SARS-CoV-2 antigens., Briefly, MAGPIX Luminex beads were covalently conjugated to insect-derived HIS-tagged SARS-CoV-2 whole S protein (Sino Biological) with the ABC coupling kit (Thermo) as per manufacturer’s instructions.

    Techniques: Expressing, Construct, Western Blot, Transfection, In Vivo, Luciferase, Mouse Assay, Injection, Standard Deviation

    Single dose of LUNAR-COV19 protects hACE2 mice against a lethal challenge of SARS-CoV-2 virus (A) hACE2 transgenic mice were immunized with a single dose of either PBS or 2 μg or 10 μg of LUNAR-COV19 (n = 5 per group), then challenged with live SARS-CoV-2 at 30 days post-vaccination, and either assessed for survival (with daily weights and clinical scores) or sacrificed at day 5 post-challenge for measurement of lung and brain tissue viral loads. (B) Live SARS-CoV-2 neutralizing antibody titers (PRNT 70 ) measured at 28 days post-vaccination. (C–E) Weight (C), clinical score (D), and survival (E) were estimated after challenge with a lethal dose (5 × 10 5 TCID 50 ) of live SARS-CoV-2 virus. (F and G) Viral RNA (F) and infectious virus (G) in the lungs and brain of challenged mice were measured with qRT-PCR and plaque assay, respectively. (H) The role of B cell and T cell depletion in LUNAR-COV19-vaccinated mice was studied after challenge with SARS-CoV-2 virus. (I) At 5 dpi, viral RNA was assessed in both mouse lungs and brain. Study design schematic diagrams were created with BioRender.com . PRNT 70 and viral titers (RNA and plaque titers) were compared across groups with the non-parametric Mann-Whitney U test. Weights and clinical scores at different time points were compared between PBS and 10 μg LUNAR-COV19-immunized mice with multiple t tests. ∗0.05

    Journal: Molecular Therapy

    Article Title: A single dose of self-transcribing and replicating RNA-based SARS-CoV-2 vaccine produces protective adaptive immunity in mice

    doi: 10.1016/j.ymthe.2021.04.001

    Figure Lengend Snippet: Single dose of LUNAR-COV19 protects hACE2 mice against a lethal challenge of SARS-CoV-2 virus (A) hACE2 transgenic mice were immunized with a single dose of either PBS or 2 μg or 10 μg of LUNAR-COV19 (n = 5 per group), then challenged with live SARS-CoV-2 at 30 days post-vaccination, and either assessed for survival (with daily weights and clinical scores) or sacrificed at day 5 post-challenge for measurement of lung and brain tissue viral loads. (B) Live SARS-CoV-2 neutralizing antibody titers (PRNT 70 ) measured at 28 days post-vaccination. (C–E) Weight (C), clinical score (D), and survival (E) were estimated after challenge with a lethal dose (5 × 10 5 TCID 50 ) of live SARS-CoV-2 virus. (F and G) Viral RNA (F) and infectious virus (G) in the lungs and brain of challenged mice were measured with qRT-PCR and plaque assay, respectively. (H) The role of B cell and T cell depletion in LUNAR-COV19-vaccinated mice was studied after challenge with SARS-CoV-2 virus. (I) At 5 dpi, viral RNA was assessed in both mouse lungs and brain. Study design schematic diagrams were created with BioRender.com . PRNT 70 and viral titers (RNA and plaque titers) were compared across groups with the non-parametric Mann-Whitney U test. Weights and clinical scores at different time points were compared between PBS and 10 μg LUNAR-COV19-immunized mice with multiple t tests. ∗0.05

    Article Snippet: Similar Luminex immuno-assays have been previously described for antibody detection against SARS-CoV-2 antigens., Briefly, MAGPIX Luminex beads were covalently conjugated to insect-derived HIS-tagged SARS-CoV-2 whole S protein (Sino Biological) with the ABC coupling kit (Thermo) as per manufacturer’s instructions.

    Techniques: Mouse Assay, Transgenic Assay, Plaque Reduction Neutralization Test, Quantitative RT-PCR, Plaque Assay, MANN-WHITNEY

    Anti-severe acute respiratory syndrome virus 2 (SARS-CoV-2) effects of aprotinin and SERPINA1/alpha-1 antitrypsin. ( A ) Concentration-dependent effects of aprotinin and SERPINA1/alpha-1 antitrypsin on SARS-CoV-2-induced cytopathogenic effect (CPE) formation determined 48 h post-infection in Caco2 cells infected at a multiplicity of infection (MOI) of 0.01 with the three different SARS-CoV-2 isolates. The viability of the Caco2 cells was 84.3 ± 2.7% relative to the untreated control in the presence of 20 µM of aprotinin. ( B ) Immunostaining for the SARS-CoV-2 S protein in aprotinin- and SERPINA1/alpha-1 antitrypsin-treated Caco2 cells infected at an MOI of 0.01 with the three different SARS-CoV-2 isolates as determined 48 h post-infection. The protease inhibitors were tested at four concentrations in 1:4 dilution steps ranging from 20 to 0.3125 µM. A quantification is provided in Figure S1 . ( C ) Copy numbers of genomic RNA in Caco2 cells infected with different SARS-CoV-2 isolates (MOI of 0.01) in response to treatment with aprotinin or SERPINA1/alpha-1 antitrypsin as determined 48 h post-infection. FFM1, 1/Human/2020/Frankfurt; FFM2, 2/Human/2020/Frankfurt; FFM6, 6/Human/2020/Frankfurt.

    Journal: Cells

    Article Title: Aprotinin Inhibits SARS-CoV-2 Replication

    doi: 10.3390/cells9112377

    Figure Lengend Snippet: Anti-severe acute respiratory syndrome virus 2 (SARS-CoV-2) effects of aprotinin and SERPINA1/alpha-1 antitrypsin. ( A ) Concentration-dependent effects of aprotinin and SERPINA1/alpha-1 antitrypsin on SARS-CoV-2-induced cytopathogenic effect (CPE) formation determined 48 h post-infection in Caco2 cells infected at a multiplicity of infection (MOI) of 0.01 with the three different SARS-CoV-2 isolates. The viability of the Caco2 cells was 84.3 ± 2.7% relative to the untreated control in the presence of 20 µM of aprotinin. ( B ) Immunostaining for the SARS-CoV-2 S protein in aprotinin- and SERPINA1/alpha-1 antitrypsin-treated Caco2 cells infected at an MOI of 0.01 with the three different SARS-CoV-2 isolates as determined 48 h post-infection. The protease inhibitors were tested at four concentrations in 1:4 dilution steps ranging from 20 to 0.3125 µM. A quantification is provided in Figure S1 . ( C ) Copy numbers of genomic RNA in Caco2 cells infected with different SARS-CoV-2 isolates (MOI of 0.01) in response to treatment with aprotinin or SERPINA1/alpha-1 antitrypsin as determined 48 h post-infection. FFM1, 1/Human/2020/Frankfurt; FFM2, 2/Human/2020/Frankfurt; FFM6, 6/Human/2020/Frankfurt.

    Article Snippet: Similar effects were observed by cell staining for SARS-CoV-2 S protein ( B and , ).

    Techniques: Concentration Assay, Infection, Immunostaining

    Site-specific N-glycosylation of recombinant SARS-CoV-2 S proteins. (A and B) The number of intact N-glycopeptides and N-glycans in recombinant SARS-CoV-2 S proteins expressed in insect cells (A) or human cells (B). (C and D) The numbers of the N-glycosites containing one representative N-glycan and its deduced structure from the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (C) and human cells (D). (E and F) Different types and numbers of N-glycan compositions on each N-glycosite of the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (E) or human cells (F). The size of the pies represents the number of N-glycan compositions.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

    doi: 10.1074/mcp.RA120.002295

    Figure Lengend Snippet: Site-specific N-glycosylation of recombinant SARS-CoV-2 S proteins. (A and B) The number of intact N-glycopeptides and N-glycans in recombinant SARS-CoV-2 S proteins expressed in insect cells (A) or human cells (B). (C and D) The numbers of the N-glycosites containing one representative N-glycan and its deduced structure from the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (C) and human cells (D). (E and F) Different types and numbers of N-glycan compositions on each N-glycosite of the recombinant SARS-CoV-2 S protein or subunit expressed in insect cells (E) or human cells (F). The size of the pies represents the number of N-glycan compositions.

    Article Snippet: The recombinant SARS-CoV-2 S protein (S1+S2 ECD and RBD) expressed in insect cells (High Five) and S protein (S1 and RBD) expressed in human embryonic kidney cells (HEK293) were purchased from Sino Biological (Beijing, China).

    Techniques: Recombinant

    Workflow for site-specific N-glycosylation characterization of recombinant SARS-CoV-2 S proteins using two complementary proteases for digestion and an integrated N-glycoproteomic analysis.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

    doi: 10.1074/mcp.RA120.002295

    Figure Lengend Snippet: Workflow for site-specific N-glycosylation characterization of recombinant SARS-CoV-2 S proteins using two complementary proteases for digestion and an integrated N-glycoproteomic analysis.

    Article Snippet: The recombinant SARS-CoV-2 S protein (S1+S2 ECD and RBD) expressed in insect cells (High Five) and S protein (S1 and RBD) expressed in human embryonic kidney cells (HEK293) were purchased from Sino Biological (Beijing, China).

    Techniques: Recombinant

    N-glycosites characterization of SARS-CoV-2 S proteins. (A and B) N-glycosites of the recombinant SARS-CoV-2 S protein or subunits expressed in insect cells (A) and human cells (B). PSS: putative signal sequence; RBD: receptor-binding domain; S1/S2: S1/S2 protease cleavage site; Oval: potential N-glycosite; Yellow oval: ambiguously assigned N-glycosite; Red oval: unambiguously assigned N-glycosite; Blue arrow: unambiguously assigned N-glycosite using trypsin digestion; Green arrow: unambiguously assigned N-glycosite using Glu-C digestion; Yellow arrow: unambiguously assigned N-glycosite using the combination of trypsin and Glu-C digestion. The unambiguously glycosite was determined by at least twice identification within each digestion list in Table S1 and Table S2 . (C) N-glycosites were demonstrated in the three-dimensional structure of the SARS-CoV-2 S protein trimers (PDB code: 6VSB). RBDs, yellow; N-glycosites, blue.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

    doi: 10.1074/mcp.RA120.002295

    Figure Lengend Snippet: N-glycosites characterization of SARS-CoV-2 S proteins. (A and B) N-glycosites of the recombinant SARS-CoV-2 S protein or subunits expressed in insect cells (A) and human cells (B). PSS: putative signal sequence; RBD: receptor-binding domain; S1/S2: S1/S2 protease cleavage site; Oval: potential N-glycosite; Yellow oval: ambiguously assigned N-glycosite; Red oval: unambiguously assigned N-glycosite; Blue arrow: unambiguously assigned N-glycosite using trypsin digestion; Green arrow: unambiguously assigned N-glycosite using Glu-C digestion; Yellow arrow: unambiguously assigned N-glycosite using the combination of trypsin and Glu-C digestion. The unambiguously glycosite was determined by at least twice identification within each digestion list in Table S1 and Table S2 . (C) N-glycosites were demonstrated in the three-dimensional structure of the SARS-CoV-2 S protein trimers (PDB code: 6VSB). RBDs, yellow; N-glycosites, blue.

    Article Snippet: The recombinant SARS-CoV-2 S protein (S1+S2 ECD and RBD) expressed in insect cells (High Five) and S protein (S1 and RBD) expressed in human embryonic kidney cells (HEK293) were purchased from Sino Biological (Beijing, China).

    Techniques: Recombinant, Sequencing, Binding Assay