h5n1  (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 h5n1
    ( a ) Impedance spectra of proposed biosensor with various targets (100 nM), including H1N1 (black line), <t>H5N1</t> (red line), hemoglobin (blue line), myoglobin (green line), and CRP (purple line) in 5 mM [Fe(CN) 6 ] 3−/4− solution in 10 mM HEPES (pH 7.04) containing 1 M KCl. ( b ) Change in charge-transfer resistance based on selectivity test (error bars: standard deviation). CRP, C-reactive protein; HEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid.
    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
    https://www.bioz.com/result/h5n1/product/Sino Biological
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    h5n1 - by Bioz Stars, 2021-09
    94/100 stars

    Images

    1) Product Images from "Fabrication of Electrochemical Influenza Virus (H1N1) Biosensor Composed of Multifunctional DNA Four-Way Junction and Molybdenum Disulfide Hybrid Material"

    Article Title: Fabrication of Electrochemical Influenza Virus (H1N1) Biosensor Composed of Multifunctional DNA Four-Way Junction and Molybdenum Disulfide Hybrid Material

    Journal: Materials

    doi: 10.3390/ma14020343

    ( a ) Impedance spectra of proposed biosensor with various targets (100 nM), including H1N1 (black line), H5N1 (red line), hemoglobin (blue line), myoglobin (green line), and CRP (purple line) in 5 mM [Fe(CN) 6 ] 3−/4− solution in 10 mM HEPES (pH 7.04) containing 1 M KCl. ( b ) Change in charge-transfer resistance based on selectivity test (error bars: standard deviation). CRP, C-reactive protein; HEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid.
    Figure Legend Snippet: ( a ) Impedance spectra of proposed biosensor with various targets (100 nM), including H1N1 (black line), H5N1 (red line), hemoglobin (blue line), myoglobin (green line), and CRP (purple line) in 5 mM [Fe(CN) 6 ] 3−/4− solution in 10 mM HEPES (pH 7.04) containing 1 M KCl. ( b ) Change in charge-transfer resistance based on selectivity test (error bars: standard deviation). CRP, C-reactive protein; HEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid.

    Techniques Used: Standard Deviation

    2) Product Images from "Highly specific and rapid glycan based amperometric detection of influenza viruses specific and rapid glycan based amperometric detection of influenza viruses †Electronic supplementary information (ESI) available: Synthesis and characterization of all compounds and intermediates are provided. See DOI: 10.1039/c6sc03720hClick here for additional data file."

    Article Title: Highly specific and rapid glycan based amperometric detection of influenza viruses specific and rapid glycan based amperometric detection of influenza viruses †Electronic supplementary information (ESI) available: Synthesis and characterization of all compounds and intermediates are provided. See DOI: 10.1039/c6sc03720hClick here for additional data file.

    Journal: Chemical Science

    doi: 10.1039/c6sc03720h

    Detection of NA using (A) natural substrates Sα2,3Gal and Sα2,6Gal or (B) new substrates (4,7di-OMe)Sα2,3Gal and (4,7di-OMe)Sα2,6Gal. 50 U of different enzymes [(1) H5N1 NA (A/Anhui/1/2005), (2) H3N2 NA (A/Babol/36/2005), (3) NA from Streptococcus pneumoniae specific for α2-3 linkages, (4) NA from Salmonella typhimurium specific for α2-3 linkages, (5) NA from Clostridium perfringens specific for α2-3, α2-6 and α2-8 linkages and (6) NA from Arthrobacter ureafaciens specific for α2-3, α2-6, α2-8 and α2-9 linkages] was incubated with Sα2,3Gal or Sα2,6Gal at 37 °C for 1 h. (C) Detection of influenza and S. pneumoniae . Different substrate [(Sα2,3Gal:Sα2,6Gal; (4,7di-OMe)Sα2,3Gal or (4,7di-OMe)Sα2,6Gal)] was incubated with different pathogens [H1N1 (A/Brisbane/59/2007); H3N2 (A/Victoria/361/2011); SP1 (serotype 1, ATCC 6301) or SP2 (serotype 1, ATCC6305)] at 37 °C for 1 h. (D) Monitoring antiviral efficacy. 10 ng of Zanamivir was premixed with different pathogens [(H3N2 A/Victoria/361/2011, VZ ), SP2 (serotype 1, ATCC 6305, SZ ), or H3N2 A/Victoria/361/2011 and SP2 ( VSZ )] for 30 min before the addition of Sα2,3Gal. Also shown is data obtained without the addition of Zanamivir to the pathogens [(H3N2 A/Victoria/361/2011, V ), SP2 (serotype 1, ATCC 6305, SP2 ), or A/Victoria/361/2011 and SP2 ( VS )]. The current was measured using Accu-Chek Aviva strips (Roche Diagnostics) with the 10 s average current recorded 5 s following substrate introduction at a working potential of –0.15 V. The y axis, Δ I , represents the difference in current before and after the addition of the substrate. All experiments were performed in triplicate independently on different days to demonstrate scientific rigor.
    Figure Legend Snippet: Detection of NA using (A) natural substrates Sα2,3Gal and Sα2,6Gal or (B) new substrates (4,7di-OMe)Sα2,3Gal and (4,7di-OMe)Sα2,6Gal. 50 U of different enzymes [(1) H5N1 NA (A/Anhui/1/2005), (2) H3N2 NA (A/Babol/36/2005), (3) NA from Streptococcus pneumoniae specific for α2-3 linkages, (4) NA from Salmonella typhimurium specific for α2-3 linkages, (5) NA from Clostridium perfringens specific for α2-3, α2-6 and α2-8 linkages and (6) NA from Arthrobacter ureafaciens specific for α2-3, α2-6, α2-8 and α2-9 linkages] was incubated with Sα2,3Gal or Sα2,6Gal at 37 °C for 1 h. (C) Detection of influenza and S. pneumoniae . Different substrate [(Sα2,3Gal:Sα2,6Gal; (4,7di-OMe)Sα2,3Gal or (4,7di-OMe)Sα2,6Gal)] was incubated with different pathogens [H1N1 (A/Brisbane/59/2007); H3N2 (A/Victoria/361/2011); SP1 (serotype 1, ATCC 6301) or SP2 (serotype 1, ATCC6305)] at 37 °C for 1 h. (D) Monitoring antiviral efficacy. 10 ng of Zanamivir was premixed with different pathogens [(H3N2 A/Victoria/361/2011, VZ ), SP2 (serotype 1, ATCC 6305, SZ ), or H3N2 A/Victoria/361/2011 and SP2 ( VSZ )] for 30 min before the addition of Sα2,3Gal. Also shown is data obtained without the addition of Zanamivir to the pathogens [(H3N2 A/Victoria/361/2011, V ), SP2 (serotype 1, ATCC 6305, SP2 ), or A/Victoria/361/2011 and SP2 ( VS )]. The current was measured using Accu-Chek Aviva strips (Roche Diagnostics) with the 10 s average current recorded 5 s following substrate introduction at a working potential of –0.15 V. The y axis, Δ I , represents the difference in current before and after the addition of the substrate. All experiments were performed in triplicate independently on different days to demonstrate scientific rigor.

    Techniques Used: Incubation

    3) Product Images from "Isolation of Recombinant Phage Antibodies Targeting the Hemagglutinin Cleavage Site of Highly Pathogenic Avian Influenza Virus"

    Article Title: Isolation of Recombinant Phage Antibodies Targeting the Hemagglutinin Cleavage Site of Highly Pathogenic Avian Influenza Virus

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0061158

    Detection of (A) HA331 peptide and (B) recombinant H5N1 HA protein by open sandwich phage ELISAs. The antigen-dependency of the V H /V L interaction was measured with the pDong system.
    Figure Legend Snippet: Detection of (A) HA331 peptide and (B) recombinant H5N1 HA protein by open sandwich phage ELISAs. The antigen-dependency of the V H /V L interaction was measured with the pDong system.

    Techniques Used: Recombinant

    Fab fragment-mediated immunofluorescent staining of Madin-Darby canine kidney (MDCK) cells infected with H5N1 Mongolia virus or Vac (low pathogenic) virus. An anti-H5N1 antibody 9F2E3F3 was also used for staining.
    Figure Legend Snippet: Fab fragment-mediated immunofluorescent staining of Madin-Darby canine kidney (MDCK) cells infected with H5N1 Mongolia virus or Vac (low pathogenic) virus. An anti-H5N1 antibody 9F2E3F3 was also used for staining.

    Techniques Used: Staining, Infection

    Characterization of soluble Fab fragments. (A) SDS-PAGE of purified Fab fragments. Upper and lower bands correspond to Fd and L chains, respectively. M: Molecular weight standards. (B) ELISA for evaluating binding to H5N1 HA protein. H5N1-HA: recombinant HA from H5N1 A/Vietnam/1194/2004.
    Figure Legend Snippet: Characterization of soluble Fab fragments. (A) SDS-PAGE of purified Fab fragments. Upper and lower bands correspond to Fd and L chains, respectively. M: Molecular weight standards. (B) ELISA for evaluating binding to H5N1 HA protein. H5N1-HA: recombinant HA from H5N1 A/Vietnam/1194/2004.

    Techniques Used: SDS Page, Purification, Molecular Weight, Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant

    Binding specificity of the clones. (A) ELISA to determine binding to several other HA proteins. H5N1-HA(An): A/Anhui/1/05(H5N1) HA; H5N1-HA(Tu): A/Turkey/1/2005(H5N1) HA; H7N7-HA(Ne): A/Netherlands/219/03(H7N7) HA. (B) ELISA to determine epitope sequence. The inhibitory effect of 7-mer partial peptide sequences shown on the binding of Fab-phages to SAv-HA331 peptide was investigated. The peptide NSPQRER showed maximal inhibitory effect. (C) The cleavage site peptide sequence of HA proteins used. The presumptive peripheral and core epitope sequences are shown in brown and red, respectively. H6 is shown as a reference.
    Figure Legend Snippet: Binding specificity of the clones. (A) ELISA to determine binding to several other HA proteins. H5N1-HA(An): A/Anhui/1/05(H5N1) HA; H5N1-HA(Tu): A/Turkey/1/2005(H5N1) HA; H7N7-HA(Ne): A/Netherlands/219/03(H7N7) HA. (B) ELISA to determine epitope sequence. The inhibitory effect of 7-mer partial peptide sequences shown on the binding of Fab-phages to SAv-HA331 peptide was investigated. The peptide NSPQRER showed maximal inhibitory effect. (C) The cleavage site peptide sequence of HA proteins used. The presumptive peripheral and core epitope sequences are shown in brown and red, respectively. H6 is shown as a reference.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Sequencing

    Selection of anti-HPAI HA antibodies. (A) The structure of BSA-MBS-HA331 used for mice immunization. (B) Flow chart for the development of monoclonal Fabs. The RNA extracted from the spleen cells of immunized mice was used for RT-PCR, which produced V H and V L cDNAs. These fragments were used to make the pDong1 phagemid library that was subsequently used for biopanning the phage libraries. (C) ELISA of the binding of positive Fab-phages to HA 331 peptide and HA proteins. HA331: cleavage site peptide; MBS: m-maleimidobenzoic acid N-hydroxysuccinimide ester; BSA: bovine serum albumin; H1N1-HA: recombinant A/California/04/2009 H1N1 HA; H5N1-HA: recombinant A/Vietnam/1194/2004 H5N1 HA.
    Figure Legend Snippet: Selection of anti-HPAI HA antibodies. (A) The structure of BSA-MBS-HA331 used for mice immunization. (B) Flow chart for the development of monoclonal Fabs. The RNA extracted from the spleen cells of immunized mice was used for RT-PCR, which produced V H and V L cDNAs. These fragments were used to make the pDong1 phagemid library that was subsequently used for biopanning the phage libraries. (C) ELISA of the binding of positive Fab-phages to HA 331 peptide and HA proteins. HA331: cleavage site peptide; MBS: m-maleimidobenzoic acid N-hydroxysuccinimide ester; BSA: bovine serum albumin; H1N1-HA: recombinant A/California/04/2009 H1N1 HA; H5N1-HA: recombinant A/Vietnam/1194/2004 H5N1 HA.

    Techniques Used: Selection, Mouse Assay, Reverse Transcription Polymerase Chain Reaction, Produced, Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant

    4) Product Images from "Highly specific and rapid glycan based amperometric detection of influenza viruses Highly specific and rapid glycan based amperometric detection of influenza viruses †Electronic supplementary information (ESI) available: Synthesis and characterization of all compounds and intermediates are provided. See DOI: 10.1039/c6sc03720hClick here for additional data file."

    Article Title: Highly specific and rapid glycan based amperometric detection of influenza viruses Highly specific and rapid glycan based amperometric detection of influenza viruses †Electronic supplementary information (ESI) available: Synthesis and characterization of all compounds and intermediates are provided. See DOI: 10.1039/c6sc03720hClick here for additional data file.

    Journal: Chemical Science

    doi: 10.1039/c6sc03720h

    Detection of NA using (A) natural substrates Sα2,3Gal and Sα2,6Gal or (B) new substrates (4,7di-OMe)Sα2,3Gal and (4,7di-OMe)Sα2,6Gal. 50 U of different enzymes [(1) H5N1 NA (A/Anhui/1/2005), (2) H3N2 NA (A/Babol/36/2005), (3) NA from Streptococcus pneumoniae specific for α2-3 linkages, (4) NA from Salmonella typhimurium specific for α2-3 linkages, (5) NA from Clostridium perfringens specific for α2-3, α2-6 and α2-8 linkages and (6) NA from Arthrobacter ureafaciens specific for α2-3, α2-6, α2-8 and α2-9 linkages] was incubated with Sα2,3Gal or Sα2,6Gal at 37 °C for 1 h. (C) Detection of influenza and S. pneumoniae . Different substrate [(Sα2,3Gal:Sα2,6Gal; (4,7di-OMe)Sα2,3Gal or (4,7di-OMe)Sα2,6Gal)] was incubated with different pathogens [H1N1 (A/Brisbane/59/2007); H3N2 (A/Victoria/361/2011); SP1 (serotype 1, ATCC 6301) or SP2 (serotype 1, ATCC6305)] at 37 °C for 1 h. (D) Monitoring antiviral efficacy. 10 ng of Zanamivir was premixed with different pathogens [(H3N2 A/Victoria/361/2011, VZ ), SP2 (serotype 1, ATCC 6305, SZ ), or H3N2 A/Victoria/361/2011 and SP2 ( VSZ )] for 30 min before the addition of Sα2,3Gal. Also shown is data obtained without the addition of Zanamivir to the pathogens [(H3N2 A/Victoria/361/2011, V ), SP2 (serotype 1, ATCC 6305, SP2 ), or A/Victoria/361/2011 and SP2 ( VS )]. The current was measured using Accu-Chek Aviva strips (Roche Diagnostics) with the 10 s average current recorded 5 s following substrate introduction at a working potential of –0.15 V. The y axis, Δ I , represents the difference in current before and after the addition of the substrate. All experiments were performed in triplicate independently on different days to demonstrate scientific rigor.
    Figure Legend Snippet: Detection of NA using (A) natural substrates Sα2,3Gal and Sα2,6Gal or (B) new substrates (4,7di-OMe)Sα2,3Gal and (4,7di-OMe)Sα2,6Gal. 50 U of different enzymes [(1) H5N1 NA (A/Anhui/1/2005), (2) H3N2 NA (A/Babol/36/2005), (3) NA from Streptococcus pneumoniae specific for α2-3 linkages, (4) NA from Salmonella typhimurium specific for α2-3 linkages, (5) NA from Clostridium perfringens specific for α2-3, α2-6 and α2-8 linkages and (6) NA from Arthrobacter ureafaciens specific for α2-3, α2-6, α2-8 and α2-9 linkages] was incubated with Sα2,3Gal or Sα2,6Gal at 37 °C for 1 h. (C) Detection of influenza and S. pneumoniae . Different substrate [(Sα2,3Gal:Sα2,6Gal; (4,7di-OMe)Sα2,3Gal or (4,7di-OMe)Sα2,6Gal)] was incubated with different pathogens [H1N1 (A/Brisbane/59/2007); H3N2 (A/Victoria/361/2011); SP1 (serotype 1, ATCC 6301) or SP2 (serotype 1, ATCC6305)] at 37 °C for 1 h. (D) Monitoring antiviral efficacy. 10 ng of Zanamivir was premixed with different pathogens [(H3N2 A/Victoria/361/2011, VZ ), SP2 (serotype 1, ATCC 6305, SZ ), or H3N2 A/Victoria/361/2011 and SP2 ( VSZ )] for 30 min before the addition of Sα2,3Gal. Also shown is data obtained without the addition of Zanamivir to the pathogens [(H3N2 A/Victoria/361/2011, V ), SP2 (serotype 1, ATCC 6305, SP2 ), or A/Victoria/361/2011 and SP2 ( VS )]. The current was measured using Accu-Chek Aviva strips (Roche Diagnostics) with the 10 s average current recorded 5 s following substrate introduction at a working potential of –0.15 V. The y axis, Δ I , represents the difference in current before and after the addition of the substrate. All experiments were performed in triplicate independently on different days to demonstrate scientific rigor.

    Techniques Used: Incubation

    5) Product Images from "Selection of Therapeutic H5N1 Monoclonal Antibodies Following IgVH Repertoire Analysis in Mice"

    Article Title: Selection of Therapeutic H5N1 Monoclonal Antibodies Following IgVH Repertoire Analysis in Mice

    Journal: Antiviral research

    doi: 10.1016/j.antiviral.2016.04.001

    MAb-mediated protection against a lethal challenge of H5N1 virus in mice
    Figure Legend Snippet: MAb-mediated protection against a lethal challenge of H5N1 virus in mice

    Techniques Used: Mouse Assay

    Related Articles

    Recombinant:

    Article Title: Auto-affitech: an automated ligand binding affinity evaluation platform using digital microfluidics with a bidirectional magnetic separation method.
    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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    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
    https://www.bioz.com/result/ha rabbit igg/product/Sino Biological
    Average 92 stars, based on 1 article reviews
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    86
    Sino Biological anti h5n1 virus
    Receptor binding affinity of recombinant <t>H5N1</t> viruses. The two types of serially diluted biotinylated sialylglycopolymers (Neu5Acα2-3Galb1-4GlcNAcb–PAA-biotin (3′SLN–PAA) and Neu5Acα2-6GalNAca–PAA-biotin (6′SLN–PAA)) were incubated with the same concentration (10 5 EID 50 ) of recombinant viruses. After development with horseradish peroxidase (HRP)-conjugated streptavidin and 3,3’5,5’-Tetramethylbenzidine (TMB) substrate, the reaction was stopped by adding stop solution, and the absorbance at 450 nm was measured. ( a ) Receptor binding affinity of recombinant viruses to 3′SLN–PAA and ( b ) Receptor binding affinity of recombinant viruses to 6′SLN–PAA. The absorbance data are the average of three independent experiments, # significant difference of rH5N1 and rH5N1-N144S-I223V compared to the other viruses, * significant difference compare to rH5N1–N144S ( p
    Anti H5n1 Virus, supplied by Sino Biological, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    86
    Sino Biological a anhui 1 2005 ah05 h5n1
    In vivo efficacy of TH/NE DDV+EP immunization. (A to I) Time course of weight change (upper panels) and survival rate (lower panels), followed by homologous NE03 H7N7 (A), intrasubtypic CAM05 <t>H5N1</t> (B), intrasubtypic SZ06 H5N1 (C), or heterosubtypic WSN33
    A Anhui 1 2005 Ah05 H5n1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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

    Receptor binding affinity of recombinant H5N1 viruses. The two types of serially diluted biotinylated sialylglycopolymers (Neu5Acα2-3Galb1-4GlcNAcb–PAA-biotin (3′SLN–PAA) and Neu5Acα2-6GalNAca–PAA-biotin (6′SLN–PAA)) were incubated with the same concentration (10 5 EID 50 ) of recombinant viruses. After development with horseradish peroxidase (HRP)-conjugated streptavidin and 3,3’5,5’-Tetramethylbenzidine (TMB) substrate, the reaction was stopped by adding stop solution, and the absorbance at 450 nm was measured. ( a ) Receptor binding affinity of recombinant viruses to 3′SLN–PAA and ( b ) Receptor binding affinity of recombinant viruses to 6′SLN–PAA. The absorbance data are the average of three independent experiments, # significant difference of rH5N1 and rH5N1-N144S-I223V compared to the other viruses, * significant difference compare to rH5N1–N144S ( p

    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: Receptor binding affinity of recombinant H5N1 viruses. The two types of serially diluted biotinylated sialylglycopolymers (Neu5Acα2-3Galb1-4GlcNAcb–PAA-biotin (3′SLN–PAA) and Neu5Acα2-6GalNAca–PAA-biotin (6′SLN–PAA)) were incubated with the same concentration (10 5 EID 50 ) of recombinant viruses. After development with horseradish peroxidase (HRP)-conjugated streptavidin and 3,3’5,5’-Tetramethylbenzidine (TMB) substrate, the reaction was stopped by adding stop solution, and the absorbance at 450 nm was measured. ( a ) Receptor binding affinity of recombinant viruses to 3′SLN–PAA and ( b ) Receptor binding affinity of recombinant viruses to 6′SLN–PAA. The absorbance data are the average of three independent experiments, # significant difference of rH5N1 and rH5N1-N144S-I223V compared to the other viruses, * significant difference compare to rH5N1–N144S ( p

    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: Binding Assay, Recombinant, Incubation, Concentration Assay

    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

    Growth kinetics of recombinant H5N1 viruses in MDCK and A549 cells. Each recombinant virus was diluted to 10 5 50% chicken embryo infection dose (EID 50 )/0.1 mL, and 0.5 mL of diluents were inoculated into confluent ( a ) MDCK and ( b ) A549 cells in 6-well plates for 1 h. After 1 h, the inoculated virus was removed, and 1 mL of fresh medium was added. During 72 h of incubation, the supernatant was harvested at 0, 24, 48, and 72 hpi, and 50% tissue culture infectious dose (TCID 50 )/0.1 mL of each time point was measured in MDCK cells. The TCID 50 /0.1 mL values are the average of three independent experiments. #, *, significant differences of rH5N1-N144S-I223V (#) and rPR8 (*) in comparison with other viruses ( p

    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: Growth kinetics of recombinant H5N1 viruses in MDCK and A549 cells. Each recombinant virus was diluted to 10 5 50% chicken embryo infection dose (EID 50 )/0.1 mL, and 0.5 mL of diluents were inoculated into confluent ( a ) MDCK and ( b ) A549 cells in 6-well plates for 1 h. After 1 h, the inoculated virus was removed, and 1 mL of fresh medium was added. During 72 h of incubation, the supernatant was harvested at 0, 24, 48, and 72 hpi, and 50% tissue culture infectious dose (TCID 50 )/0.1 mL of each time point was measured in MDCK cells. The TCID 50 /0.1 mL values are the average of three independent experiments. #, *, significant differences of rH5N1-N144S-I223V (#) and rPR8 (*) in comparison with other viruses ( p

    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: Recombinant, Infection, Incubation

    Heat stability of recombinant H5N1 viruses. Each of the recombinant viruses was diluted to a 2 4 HA titer, and aliquots were incubated at 60 °C for 0, 5, 15, and 30 min. After heat treatment, the HA titer of each aliquot was measured by HA assay with 1% chicken RBCs.

    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: Heat stability of recombinant H5N1 viruses. Each of the recombinant viruses was diluted to a 2 4 HA titer, and aliquots were incubated at 60 °C for 0, 5, 15, and 30 min. After heat treatment, the HA titer of each aliquot was measured by HA assay with 1% chicken RBCs.

    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: Recombinant, Incubation, Hemagglutination Assay

    Mouse pathogenicity of recombinant H5N1 viruses. ( a ) Mortality and ( b ) weight loss of mouse experimental groups infected with recombinant H5N1 viruses. Five six-week-old female BALB/c mice per group were inoculated with 10 6 EID 50 of virus or an equivalent volume PBS (mock) intranasally. Weight loss was monitored for 2 weeks, and mice with more than 20% weight loss were euthanized. The weight loss was calculated based on the body weight measured at 0 dpi, and the data are the average of each group; * significant difference of the rH5N1-I223V and rH5N1-N144S groups compared to the mock groups ( p

    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: Mouse pathogenicity of recombinant H5N1 viruses. ( a ) Mortality and ( b ) weight loss of mouse experimental groups infected with recombinant H5N1 viruses. Five six-week-old female BALB/c mice per group were inoculated with 10 6 EID 50 of virus or an equivalent volume PBS (mock) intranasally. Weight loss was monitored for 2 weeks, and mice with more than 20% weight loss were euthanized. The weight loss was calculated based on the body weight measured at 0 dpi, and the data are the average of each group; * significant difference of the rH5N1-I223V and rH5N1-N144S groups compared to the mock groups ( p

    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: Recombinant, Infection, Mouse Assay

    In vivo efficacy of TH/NE DDV+EP immunization. (A to I) Time course of weight change (upper panels) and survival rate (lower panels), followed by homologous NE03 H7N7 (A), intrasubtypic CAM05 H5N1 (B), intrasubtypic SZ06 H5N1 (C), or heterosubtypic WSN33

    Journal: Journal of Virology

    Article Title: A Bivalent Heterologous DNA Virus-Like-Particle Prime-Boost Vaccine Elicits Broad Protection against both Group 1 and 2 Influenza A Viruses

    doi: 10.1128/JVI.02052-16

    Figure Lengend Snippet: In vivo efficacy of TH/NE DDV+EP immunization. (A to I) Time course of weight change (upper panels) and survival rate (lower panels), followed by homologous NE03 H7N7 (A), intrasubtypic CAM05 H5N1 (B), intrasubtypic SZ06 H5N1 (C), or heterosubtypic WSN33

    Article Snippet: To measure the total IgG, IgG1, and IgG2a antibody responses in TH/NE DDV+EP serum samples against divergent influenza HA, 96-well EIA/RIA flat-bottom plates (Corning) were coated with 100 ng of soluble ectodomain of HA proteins from WSN33 H1N1, HK68 H3N2, A/Anhui/1/2005 (AH05) H5N1, NE03 H7N7, or A/Hong Kong/1073/1999 (HK99) H9N2 (Sino Biological, Inc.) per well at 4°C overnight.

    Techniques: In Vivo

    In vivo efficacy of passive immunization with immune sera or with immune sera and/or T cells . (A to E) Time course of weight change (upper panel) and survival rate (lower panel), followed by homologous NE03 H7N7 (A), intrasubtypic CAM05 H5N1 (B), or heterosubtypic

    Journal: Journal of Virology

    Article Title: A Bivalent Heterologous DNA Virus-Like-Particle Prime-Boost Vaccine Elicits Broad Protection against both Group 1 and 2 Influenza A Viruses

    doi: 10.1128/JVI.02052-16

    Figure Lengend Snippet: In vivo efficacy of passive immunization with immune sera or with immune sera and/or T cells . (A to E) Time course of weight change (upper panel) and survival rate (lower panel), followed by homologous NE03 H7N7 (A), intrasubtypic CAM05 H5N1 (B), or heterosubtypic

    Article Snippet: To measure the total IgG, IgG1, and IgG2a antibody responses in TH/NE DDV+EP serum samples against divergent influenza HA, 96-well EIA/RIA flat-bottom plates (Corning) were coated with 100 ng of soluble ectodomain of HA proteins from WSN33 H1N1, HK68 H3N2, A/Anhui/1/2005 (AH05) H5N1, NE03 H7N7, or A/Hong Kong/1073/1999 (HK99) H9N2 (Sino Biological, Inc.) per well at 4°C overnight.

    Techniques: In Vivo

    Neutralization measured by plaque reduction assay. (A) Comparison of percentages of plaques between TH/NE DDV+EP sera versus control DDV+EP sera at a 1:40 dilution against homologous NE03 H7N7 and intrasubtypic CAM05 H5N1 and SZ06 H5N1 strains. (B) Comparison

    Journal: Journal of Virology

    Article Title: A Bivalent Heterologous DNA Virus-Like-Particle Prime-Boost Vaccine Elicits Broad Protection against both Group 1 and 2 Influenza A Viruses

    doi: 10.1128/JVI.02052-16

    Figure Lengend Snippet: Neutralization measured by plaque reduction assay. (A) Comparison of percentages of plaques between TH/NE DDV+EP sera versus control DDV+EP sera at a 1:40 dilution against homologous NE03 H7N7 and intrasubtypic CAM05 H5N1 and SZ06 H5N1 strains. (B) Comparison

    Article Snippet: To measure the total IgG, IgG1, and IgG2a antibody responses in TH/NE DDV+EP serum samples against divergent influenza HA, 96-well EIA/RIA flat-bottom plates (Corning) were coated with 100 ng of soluble ectodomain of HA proteins from WSN33 H1N1, HK68 H3N2, A/Anhui/1/2005 (AH05) H5N1, NE03 H7N7, or A/Hong Kong/1073/1999 (HK99) H9N2 (Sino Biological, Inc.) per well at 4°C overnight.

    Techniques: Neutralization