influenza a h5n1 ha protein  (Sino Biological)


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    Name:
    Influenza A H5N1 Hemagglutinin HA Protein
    Description:
    A DNA sequence encoding the extracellular domain of hemagglutinin Influenza A virus A Viet Nam 1203 2004 H5N1 AAW80717 1 Met 1 Gln 531 with cleavage site mutated RERRRKKR→TETR HA1 HA2 uncleaved was fused with the C terminal polyhistidine tagged Fc region of mouse IgG1 at the C terminus
    Catalog Number:
    10003-V06H3
    Price:
    None
    Category:
    recombinant protein
    Host:
    HEK293 Cells
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    Structured Review

    Sino Biological influenza a h5n1 ha protein
    (a) Upconversion emission spectra of the UCNP aptasensor in the presence of various concentrations of <t>H5N1</t> HA (0, 0.1, 0.2, 0.4, 1, 2, 4, 8, 10, 15, 20, 25, 30 ng mL –1 ) under optimal experimental conditions, where F 0 represents the fluorescence intensity of the UCNP-Apt–GO complex (0.05 mg mL –1 UCNP-Apt and 0.1 mg mL –1 GO) and F is the fluorescence intensity of the complex plus different concentrations of HA. (b) Relationship between relative fluorescence intensity ( F – F 0 )/ F 0 at 541 nm against the H5N1 HA concentration. Inset: linear part of the plot ranging from 0.01 to 15 ng mL –1 in borate buffer. (c) Specific selectivity evaluation of the proposed method for HA (20 ng mL –1 ) against other proteins (100 ng mL –1 ). (d) Relationship curve of relative fluorescence intensity for added standard HA from human serum samples. It shows the linear response with HA concentrations from 0.2 to 12 ng mL –1 , under the experimental conditions the same as an aqueous buffer. Error bars: SD, n = 3.
    A DNA sequence encoding the extracellular domain of hemagglutinin Influenza A virus A Viet Nam 1203 2004 H5N1 AAW80717 1 Met 1 Gln 531 with cleavage site mutated RERRRKKR→TETR HA1 HA2 uncleaved was fused with the C terminal polyhistidine tagged Fc region of mouse IgG1 at the C terminus
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    Average 94 stars, based on 1 article reviews
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    Images

    1) Product Images from "Upconversion Fluorescence Resonance Energy Transfer Aptasensors for H5N1 Influenza Virus Detection"

    Article Title: Upconversion Fluorescence Resonance Energy Transfer Aptasensors for H5N1 Influenza Virus Detection

    Journal: ACS Omega

    doi: 10.1021/acsomega.1c01491

    (a) Upconversion emission spectra of the UCNP aptasensor in the presence of various concentrations of H5N1 HA (0, 0.1, 0.2, 0.4, 1, 2, 4, 8, 10, 15, 20, 25, 30 ng mL –1 ) under optimal experimental conditions, where F 0 represents the fluorescence intensity of the UCNP-Apt–GO complex (0.05 mg mL –1 UCNP-Apt and 0.1 mg mL –1 GO) and F is the fluorescence intensity of the complex plus different concentrations of HA. (b) Relationship between relative fluorescence intensity ( F – F 0 )/ F 0 at 541 nm against the H5N1 HA concentration. Inset: linear part of the plot ranging from 0.01 to 15 ng mL –1 in borate buffer. (c) Specific selectivity evaluation of the proposed method for HA (20 ng mL –1 ) against other proteins (100 ng mL –1 ). (d) Relationship curve of relative fluorescence intensity for added standard HA from human serum samples. It shows the linear response with HA concentrations from 0.2 to 12 ng mL –1 , under the experimental conditions the same as an aqueous buffer. Error bars: SD, n = 3.
    Figure Legend Snippet: (a) Upconversion emission spectra of the UCNP aptasensor in the presence of various concentrations of H5N1 HA (0, 0.1, 0.2, 0.4, 1, 2, 4, 8, 10, 15, 20, 25, 30 ng mL –1 ) under optimal experimental conditions, where F 0 represents the fluorescence intensity of the UCNP-Apt–GO complex (0.05 mg mL –1 UCNP-Apt and 0.1 mg mL –1 GO) and F is the fluorescence intensity of the complex plus different concentrations of HA. (b) Relationship between relative fluorescence intensity ( F – F 0 )/ F 0 at 541 nm against the H5N1 HA concentration. Inset: linear part of the plot ranging from 0.01 to 15 ng mL –1 in borate buffer. (c) Specific selectivity evaluation of the proposed method for HA (20 ng mL –1 ) against other proteins (100 ng mL –1 ). (d) Relationship curve of relative fluorescence intensity for added standard HA from human serum samples. It shows the linear response with HA concentrations from 0.2 to 12 ng mL –1 , under the experimental conditions the same as an aqueous buffer. Error bars: SD, n = 3.

    Techniques Used: Fluorescence, Concentration Assay

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    Article Snippet: .. The dissociation constant (Kd) is a crucial parameter for characterizing binding affinity in molecular recognition, including antigen-antibody, DNA-protein, and receptor-ligand interactions. ..

    Article Title: Aerosolized Exposure to H5N1 Influenza Virus Causes Less Severe Disease Than Infection via Combined Intrabronchial, Oral, and Nasal Inoculation in Cynomolgus Macaques
    Article Snippet: .. The animals were negative for antibodies to simian type D retrovirus and simian T-cell lymphotropic virus, and they were selected for the absence of antibodies directed to influenza A/Vietnam/1203/04 (H5N1) recombinant hemagglutinin (HA) protein (Sino Biological Inc). ..

    Article Title: Rapid, Sensitive, and Selective Detection of H5 Hemagglutinin from Avian Influenza Virus Using an Immunowall Device
    Article Snippet: .. Mouse anti-H5N1 HA monoclonal antibody, recombinant H5N1 HA, recombinant H1N1 HA, recombinant H3N2 HA, recombinant H7N9 HA, and rabbit anti-avian influenza A HA polyclonal antibody were purchased from Sino Biological, Inc. (Beijing, China). ..

    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). ..

    Article Title: An oligothiophene compound neutralized influenza A viruses by interfering with hemagglutinin.
    Article Snippet: .. Surface plasmon resonance (SPR)The HA of influenza A/Thailand/Kan353/2004(H5N1) and the HA of A/Vietnam/1194/2004(H5N1) were 99.82% identical, so we used HA and HA2 recombinant protein of influenza A/Vietnam/1194/2004(H5N1) bought from Sino Biological Inc. in this experiment. ..

    Article Title: Highly Sensitive and Automated Surface Enhanced Raman Scattering-based Immunoassay for H5N1 Detection with Digital Microfluidics.
    Article Snippet: .. Digital microfluidics (DMF) is a powerful platform for a broad range of applications, especially immunoassays having multiple steps, due to the advantages of low reagent consumption and high automatization. ..

    other:

    Article Title: Upconversion Fluorescence Resonance Energy Transfer Aptasensors for H5N1 Influenza Virus Detection
    Article Snippet: Influenza A H5N1 HA protein was purchased from Sino Biological Inc. (Beijing, China).

    Article Title: Fabrication of Electrochemical Influenza Virus (H1N1) Biosensor Composed of Multifunctional DNA Four-Way Junction and Molybdenum Disulfide Hybrid Material
    Article Snippet: Materials The influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA Protein (His Tag) and influenza A H5N1 (A/VietNam/1203/2004) Hemagglutinin/HA Protein (His Tag and fragment crystallizable (Fc) Tag) were purchased from Sino Biological (Beijing, China).

    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). ..

    SPR Assay:

    Article Title: An oligothiophene compound neutralized influenza A viruses by interfering with hemagglutinin.
    Article Snippet: .. Surface plasmon resonance (SPR)The HA of influenza A/Thailand/Kan353/2004(H5N1) and the HA of A/Vietnam/1194/2004(H5N1) were 99.82% identical, so we used HA and HA2 recombinant protein of influenza A/Vietnam/1194/2004(H5N1) bought from Sino Biological Inc. in this experiment. ..

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  • 92
    Sino Biological ha rabbit igg
    Verification of 144N-glycosylation by Western blotting. Recombinant viruses untreated and treated with PNGase F enzyme were denatured and separated by SDS-PAGE. Transferred membranes were incubated with rabbit anti-influenza A <t>H5N1</t> (A/Vietnam/1194/2004) HA <t>IgG,</t> followed by goat anti-rabbit IgG HRP-conjugated secondary antibody. Then, HRP was developed by TMB substrate. HA proteins of rH5N1 and rH5N1-I223V had 144N-glycan, and they had higher molecular weight than rH5N1-N144S and rH5N1-N144S-I223V in the absence of PNGase F enzyme treatment (−). However, the difference disappeared after treatment of PNGase F enzyme (+).
    Ha Rabbit Igg, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Sino Biological influenza a h1n1
    (A) Schematic illustration siallylactose immobilization. (B) Result of label-free <t>influenza</t> A virus subtype <t>H1N1</t> detection using QCM measurement. Frequency shifts were detected following the application of influenza A H1N1 solution on 6SL or 3SL immobilized QCM sensor surfaces (experiments were performed in triplicate). Virus solutions of 1/32, 1/16, 1/8, 1/4, 1/2 and 1 HAU were injected at 5-min intervals (position of arrows). (C) The plotted data were converted from Fig. 3 B. All plots were sampled after 5 min from injection. (D) Schematic illustration of the influenza A virus subtype H1N1 detection experiment. (E) An example of real-time measurements of transition in potential vs. Ag/AgCl reference electrode as potential changes. An average of six cooperative measurement lines were shown as measurement data. Solutions of 1/1280, 1/320, 1/80, 1/20, 1/5 and 4/5 HAU were applied on 6SL modified gold electrodes at 10-min intervals (position of arrows). The original measurement lines are shown in Supporting Information (Fig. S4) . (F) Data plots of relative potential changes 10 min after virus introduction. All plots were converted from the original real-time potential measurements ( Fig. 2 E). The potential measurement of virus binding on 6SL or 3SL surface were performed in duplicate. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
    Influenza A H1n1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Sino Biological anti h7n9 hemagglutinin ha antibody rabbit pab
    Biological and chemical modifications of <t>H7N9</t> VLPs. (A) SDS-PAGE and western blot analysis of biologically modified H7N9 VLPs. Lane 1–3 represent 320 ng, 180 ng and 90 ng of αGal (-) VLP based on HA content, respectively. Lane 4–6 are 130 ng, 90, and 40 ng of αGal (+) VLP, respectively. (B) SDS-PAGE and western blot analysis of chemically modified H7N9 VLPs. S: protein standards; 1: αGal (-) H7N9 VLP; 2: intermediate of αGal (-) H7N9 VLP reacted with GO; 3: H7N9 conjugated with αGal linker a11; 4: H7N9 conjugated with αGal linker aN11; 5: H7N9 VLPs conjugated with control linker sp11. (C) Electron microscopy of H7N9 VLPs. (D) Electron microscopy of H7N9 VLPs stained with gold particles. Negative: VLPs were only stained with immunogold donkey anti-rabbit secondary antibody; Positive: VLPs were stained with anti-HA7 rabbit polyclonal antibody, followed by staining with immunogold donkey anti-rabbit secondary antibody. Sp11 is the aminooxy spacer control linker without αGal antigen; a11 is one type of αGal (Galα1,3-Galβ1,4-Glc) aminooxy linker; aN11 is the other type of αGal (Galα1,3-Galβ1,4-GlcNAc) aminooxy linker.
    Anti H7n9 Hemagglutinin Ha Antibody Rabbit Pab, 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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    Image Search Results


    Verification of 144N-glycosylation by Western blotting. Recombinant viruses untreated and treated with PNGase F enzyme were denatured and separated by SDS-PAGE. Transferred membranes were incubated with rabbit anti-influenza A H5N1 (A/Vietnam/1194/2004) HA IgG, followed by goat anti-rabbit IgG HRP-conjugated secondary antibody. Then, HRP was developed by TMB substrate. HA proteins of rH5N1 and rH5N1-I223V had 144N-glycan, and they had higher molecular weight than rH5N1-N144S and rH5N1-N144S-I223V in the absence of PNGase F enzyme treatment (−). However, the difference disappeared after treatment of PNGase F enzyme (+).

    Journal: Viruses

    Article Title: Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

    doi: 10.3390/v11100923

    Figure Lengend Snippet: Verification of 144N-glycosylation by Western blotting. Recombinant viruses untreated and treated with PNGase F enzyme were denatured and separated by SDS-PAGE. Transferred membranes were incubated with rabbit anti-influenza A H5N1 (A/Vietnam/1194/2004) HA IgG, followed by goat anti-rabbit IgG HRP-conjugated secondary antibody. Then, HRP was developed by TMB substrate. HA proteins of rH5N1 and rH5N1-I223V had 144N-glycan, and they had higher molecular weight than rH5N1-N144S and rH5N1-N144S-I223V in the absence of PNGase F enzyme treatment (−). However, the difference disappeared after treatment of PNGase F enzyme (+).

    Article Snippet: The proteins were transferred to a nitrocellulose membrane (Life Technologies Co.), and the membrane was incubated with anti-H5N1 virus (A/Vietnam/1194/2004), HA rabbit IgG (Sino Biological Inc., Beijing, China), followed by incubation with horseradish peroxidase conjugated-goat anti-rabbit IgG (Bethyl Laboratories Inc., Montgomery, AL, USA).

    Techniques: Western Blot, Recombinant, SDS Page, Incubation, Molecular Weight

    Expression of viral proteins in infected MDCK cells. MDCK cells were infected with viruses at an MOI of 5. The infected cells were collected at 12 h postinfection, lysed in SDS loading buffer, and further analyzed by Western blotting (A and B). (A) Protein bands of HA, NP, and M1 proteins detected by Western blotting. The intensity of each band was measured by using ImageJ software, and relative intensity ratios of HA, NP, and M1 compared with that of GAPDH were calculated (B). The infected cells were digested with trypsin to obtain a single cell suspension at 12 h postinfection. The samples were stained with rabbit monoclonal antibody to influenza A virus H5N1 HA protein and Alexa Fluor 488-conjugated goat anti-rabbit IgG (H+L) secondary antibody and then detected on a FACSAria II (BD Biosciences). (C) Mean fluorescence intensity of HA protein was analyzed with FlowJo X 10.0.7r2 (Tree Star, San Carlos, CA). Data are presented as means ± SD ( n = 3). **, P

    Journal: Journal of Virology

    Article Title: Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune Response

    doi: 10.1128/JVI.02215-16

    Figure Lengend Snippet: Expression of viral proteins in infected MDCK cells. MDCK cells were infected with viruses at an MOI of 5. The infected cells were collected at 12 h postinfection, lysed in SDS loading buffer, and further analyzed by Western blotting (A and B). (A) Protein bands of HA, NP, and M1 proteins detected by Western blotting. The intensity of each band was measured by using ImageJ software, and relative intensity ratios of HA, NP, and M1 compared with that of GAPDH were calculated (B). The infected cells were digested with trypsin to obtain a single cell suspension at 12 h postinfection. The samples were stained with rabbit monoclonal antibody to influenza A virus H5N1 HA protein and Alexa Fluor 488-conjugated goat anti-rabbit IgG (H+L) secondary antibody and then detected on a FACSAria II (BD Biosciences). (C) Mean fluorescence intensity of HA protein was analyzed with FlowJo X 10.0.7r2 (Tree Star, San Carlos, CA). Data are presented as means ± SD ( n = 3). **, P

    Article Snippet: The samples were stained with a rabbit monoclonal antibody to influenza A virus H5N1 HA protein (11048-RM07; Sino Biological Inc.) and with Alexa Fluor 488-conjugated goat anti-rabbit IgG (H+L) secondary antibody (A-11034; Thermo Fisher Scientific).

    Techniques: Expressing, Infection, Western Blot, Software, Staining, Fluorescence

    (A) Schematic illustration siallylactose immobilization. (B) Result of label-free influenza A virus subtype H1N1 detection using QCM measurement. Frequency shifts were detected following the application of influenza A H1N1 solution on 6SL or 3SL immobilized QCM sensor surfaces (experiments were performed in triplicate). Virus solutions of 1/32, 1/16, 1/8, 1/4, 1/2 and 1 HAU were injected at 5-min intervals (position of arrows). (C) The plotted data were converted from Fig. 3 B. All plots were sampled after 5 min from injection. (D) Schematic illustration of the influenza A virus subtype H1N1 detection experiment. (E) An example of real-time measurements of transition in potential vs. Ag/AgCl reference electrode as potential changes. An average of six cooperative measurement lines were shown as measurement data. Solutions of 1/1280, 1/320, 1/80, 1/20, 1/5 and 4/5 HAU were applied on 6SL modified gold electrodes at 10-min intervals (position of arrows). The original measurement lines are shown in Supporting Information (Fig. S4) . (F) Data plots of relative potential changes 10 min after virus introduction. All plots were converted from the original real-time potential measurements ( Fig. 2 E). The potential measurement of virus binding on 6SL or 3SL surface were performed in duplicate. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Journal: Biosensors & Bioelectronics

    Article Title: Direct and label-free influenza virus detection based on multisite binding to sialic acid receptors

    doi: 10.1016/j.bios.2017.02.023

    Figure Lengend Snippet: (A) Schematic illustration siallylactose immobilization. (B) Result of label-free influenza A virus subtype H1N1 detection using QCM measurement. Frequency shifts were detected following the application of influenza A H1N1 solution on 6SL or 3SL immobilized QCM sensor surfaces (experiments were performed in triplicate). Virus solutions of 1/32, 1/16, 1/8, 1/4, 1/2 and 1 HAU were injected at 5-min intervals (position of arrows). (C) The plotted data were converted from Fig. 3 B. All plots were sampled after 5 min from injection. (D) Schematic illustration of the influenza A virus subtype H1N1 detection experiment. (E) An example of real-time measurements of transition in potential vs. Ag/AgCl reference electrode as potential changes. An average of six cooperative measurement lines were shown as measurement data. Solutions of 1/1280, 1/320, 1/80, 1/20, 1/5 and 4/5 HAU were applied on 6SL modified gold electrodes at 10-min intervals (position of arrows). The original measurement lines are shown in Supporting Information (Fig. S4) . (F) Data plots of relative potential changes 10 min after virus introduction. All plots were converted from the original real-time potential measurements ( Fig. 2 E). The potential measurement of virus binding on 6SL or 3SL surface were performed in duplicate. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Influenza A H1N1 (A/California/04/2009) hemagglutinin and influenza A virus subtype H5N1 (A/Vietnam/1194/2004) hemagglutinin were purchased from Sino Biological Inc. (Beijing, China).

    Techniques: Injection, Modification, Binding Assay

    Characterization of influenza A virus subtype H1N1. (A) Determination of HA titer by hemagglutination assay. A 16- to 2048-fold dilution series (2 −4 to 2 −11 ) of virus solution was prepared using 0.01% gelatin DPBS solution. Then, 50 μL of each dilution was added to a 96-well round-bottom plate. Fifty microliters of 0.5% chicken red blood cell suspension was mixed with each virus solution (n=3). Top panel: 96-well plate just after mixing. Lower panel: 96-well plate after 30 min. The blood cells were precipitated from 1/512 dilution of virus solution, giving an HA titer of the original virus of 256. (B) The size distribution, mean size of particle diameter and zeta potential of virus (32 HAU).

    Journal: Biosensors & Bioelectronics

    Article Title: Direct and label-free influenza virus detection based on multisite binding to sialic acid receptors

    doi: 10.1016/j.bios.2017.02.023

    Figure Lengend Snippet: Characterization of influenza A virus subtype H1N1. (A) Determination of HA titer by hemagglutination assay. A 16- to 2048-fold dilution series (2 −4 to 2 −11 ) of virus solution was prepared using 0.01% gelatin DPBS solution. Then, 50 μL of each dilution was added to a 96-well round-bottom plate. Fifty microliters of 0.5% chicken red blood cell suspension was mixed with each virus solution (n=3). Top panel: 96-well plate just after mixing. Lower panel: 96-well plate after 30 min. The blood cells were precipitated from 1/512 dilution of virus solution, giving an HA titer of the original virus of 256. (B) The size distribution, mean size of particle diameter and zeta potential of virus (32 HAU).

    Article Snippet: Influenza A H1N1 (A/California/04/2009) hemagglutinin and influenza A virus subtype H5N1 (A/Vietnam/1194/2004) hemagglutinin were purchased from Sino Biological Inc. (Beijing, China).

    Techniques: Hemagglutination Assay

    Biological and chemical modifications of H7N9 VLPs. (A) SDS-PAGE and western blot analysis of biologically modified H7N9 VLPs. Lane 1–3 represent 320 ng, 180 ng and 90 ng of αGal (-) VLP based on HA content, respectively. Lane 4–6 are 130 ng, 90, and 40 ng of αGal (+) VLP, respectively. (B) SDS-PAGE and western blot analysis of chemically modified H7N9 VLPs. S: protein standards; 1: αGal (-) H7N9 VLP; 2: intermediate of αGal (-) H7N9 VLP reacted with GO; 3: H7N9 conjugated with αGal linker a11; 4: H7N9 conjugated with αGal linker aN11; 5: H7N9 VLPs conjugated with control linker sp11. (C) Electron microscopy of H7N9 VLPs. (D) Electron microscopy of H7N9 VLPs stained with gold particles. Negative: VLPs were only stained with immunogold donkey anti-rabbit secondary antibody; Positive: VLPs were stained with anti-HA7 rabbit polyclonal antibody, followed by staining with immunogold donkey anti-rabbit secondary antibody. Sp11 is the aminooxy spacer control linker without αGal antigen; a11 is one type of αGal (Galα1,3-Galβ1,4-Glc) aminooxy linker; aN11 is the other type of αGal (Galα1,3-Galβ1,4-GlcNAc) aminooxy linker.

    Journal: PLoS ONE

    Article Title: Addition of αGal HyperAcute™ technology to recombinant avian influenza vaccines induces strong low-dose antibody responses

    doi: 10.1371/journal.pone.0182683

    Figure Lengend Snippet: Biological and chemical modifications of H7N9 VLPs. (A) SDS-PAGE and western blot analysis of biologically modified H7N9 VLPs. Lane 1–3 represent 320 ng, 180 ng and 90 ng of αGal (-) VLP based on HA content, respectively. Lane 4–6 are 130 ng, 90, and 40 ng of αGal (+) VLP, respectively. (B) SDS-PAGE and western blot analysis of chemically modified H7N9 VLPs. S: protein standards; 1: αGal (-) H7N9 VLP; 2: intermediate of αGal (-) H7N9 VLP reacted with GO; 3: H7N9 conjugated with αGal linker a11; 4: H7N9 conjugated with αGal linker aN11; 5: H7N9 VLPs conjugated with control linker sp11. (C) Electron microscopy of H7N9 VLPs. (D) Electron microscopy of H7N9 VLPs stained with gold particles. Negative: VLPs were only stained with immunogold donkey anti-rabbit secondary antibody; Positive: VLPs were stained with anti-HA7 rabbit polyclonal antibody, followed by staining with immunogold donkey anti-rabbit secondary antibody. Sp11 is the aminooxy spacer control linker without αGal antigen; a11 is one type of αGal (Galα1,3-Galβ1,4-Glc) aminooxy linker; aN11 is the other type of αGal (Galα1,3-Galβ1,4-GlcNAc) aminooxy linker.

    Article Snippet: Following a 30-minute incubation in a glass petri dish incubation chamber, the grid was stained in a 40 μL drop of rabbit polyclonal anti-HA7 antibody (Sino Biological Inc., 40103-RP02, 1: 500 dilution in blocking buffer) or blocking buffer alone to serve as a negative control.

    Techniques: SDS Page, Western Blot, Modification, Electron Microscopy, Staining