fcγriv  (Sino Biological)


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    Name:
    FCGR4 cDNA ORF Clone Mouse C DYKDDDDK tag
    Description:
    Full length Clone DNA of Mouse Fc receptor IgG low affinity IV with C terminal Flag tag
    Catalog Number:
    mg50036-cf
    Product Aliases:
    4833442P21Rik cDNA ORF Clone Mouse, CD16-2 cDNA ORF Clone Mouse, FcgammaRIV cDNA ORF Clone Mouse, Fcgr3a cDNA ORF Clone Mouse, FcgRIV cDNA ORF Clone Mouse, Fcrl3 cDNA ORF Clone Mouse
    Price:
    195.0
    Applications:
    Stable or Transient mammalian expression
    Size:
    1Unit
    Category:
    cDNA Clone
    Molecule Name:
    FCGR4,Fcrl3,
    Buy from Supplier


    Structured Review

    Sino Biological fcγriv
    FCGR4 cDNA ORF Clone Mouse C DYKDDDDK tag
    Full length Clone DNA of Mouse Fc receptor IgG low affinity IV with C terminal Flag tag
    https://www.bioz.com/result/fcγriv/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fcγriv - by Bioz Stars, 2021-02
    92/100 stars

    Images

    1) Product Images from "Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection"

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2019.02920

    Characterization of the isolated FcγRIV-specific VHH. (A) The predicted amino acid residue sequence of FcγRIV-VHH-7m, isolated after panning on recombinant mouse FcγRIV protein of a VHH library derived from a llama immunized with immature mouse dendritic cells. Above the sequences the Kabat numbering is indicated. CDR1, −2, and −3 are boxed. (B) Flow cytometric analysis showing binding of FcgRIV-VHH-7m and M2e-VHH-23m to HEK 293T cells transiently transfected with expression vectors coding for mouse FcγRI, FγRIIb, FcγRIII, and FcγRIV along with the common γ-chain for the activating FcγRs and a GFP expression plasmid. The lower graph depicts binding to Mf4/4 cells. The cells were incubated with fourfold serial dilution of Alexa Fluor™ 647 labeled FcγRIV-VHH-7m or M2e-VHH-23m, starting at a concentration of 0.2 μM, binding of the VHHs to the GFP positive cells was analyzed. Data points represent averages of triplicates and error bars standard deviations.
    Figure Legend Snippet: Characterization of the isolated FcγRIV-specific VHH. (A) The predicted amino acid residue sequence of FcγRIV-VHH-7m, isolated after panning on recombinant mouse FcγRIV protein of a VHH library derived from a llama immunized with immature mouse dendritic cells. Above the sequences the Kabat numbering is indicated. CDR1, −2, and −3 are boxed. (B) Flow cytometric analysis showing binding of FcgRIV-VHH-7m and M2e-VHH-23m to HEK 293T cells transiently transfected with expression vectors coding for mouse FcγRI, FγRIIb, FcγRIII, and FcγRIV along with the common γ-chain for the activating FcγRs and a GFP expression plasmid. The lower graph depicts binding to Mf4/4 cells. The cells were incubated with fourfold serial dilution of Alexa Fluor™ 647 labeled FcγRIV-VHH-7m or M2e-VHH-23m, starting at a concentration of 0.2 μM, binding of the VHHs to the GFP positive cells was analyzed. Data points represent averages of triplicates and error bars standard deviations.

    Techniques Used: Isolation, Sequencing, Recombinant, Derivative Assay, Flow Cytometry, Binding Assay, Transfection, Expressing, Plasmid Preparation, Incubation, Serial Dilution, Labeling, Concentration Assay

    Bispecific fusion construct of a FcγRIV- and M2e-specific VHH protects mice against a potentially lethal influenza A virus infection. (A) Groups of 16 (bispecific VHHs) or 14 (PBS) BALB/c mice were intranasally treated with 50 μg of the bispecific VHHs or PBS 4 h before and 24 h after challenge with 2xLD 50 of A/X47 (H3N2) influenza virus. Body weight change (left) and survival (right) were monitored for 14 days. The mean relative changes in body weight together with their standard errors, are represented. The difference in body weight loss between FcγRIV VHH-M2e VHH and the negative-control groups was statistically significant (*** P
    Figure Legend Snippet: Bispecific fusion construct of a FcγRIV- and M2e-specific VHH protects mice against a potentially lethal influenza A virus infection. (A) Groups of 16 (bispecific VHHs) or 14 (PBS) BALB/c mice were intranasally treated with 50 μg of the bispecific VHHs or PBS 4 h before and 24 h after challenge with 2xLD 50 of A/X47 (H3N2) influenza virus. Body weight change (left) and survival (right) were monitored for 14 days. The mean relative changes in body weight together with their standard errors, are represented. The difference in body weight loss between FcγRIV VHH-M2e VHH and the negative-control groups was statistically significant (*** P

    Techniques Used: Construct, Mouse Assay, Infection, Negative Control

    Bispecific fusion construct of anti-mouse FcγRIV VHH with M2e-VHH-23m selectively activates FcγRIV in vitro . (A) Schematic representation of the bispecific VHHs and ELISA on human H3N2 M2e peptide and recombinant FcγRIV protein is shown on the right. Wells of microtiter plates were coated with 100 ng peptide or protein. Dilution series of the bispecific VHH fusion constructs were added to the coated plates. Binding was detected with a mouse anti-His tag MAb, followed by a secondary sheep anti-mouse IgG Ab conjugated to HRP for the peptide ELISA. In the ELISA with coated recombinant FcγRIV protein, binding was detected with a HRP-conjugated rabbit anti-camelid VHH antibody. (B) Serial dilutions of the bispecific VHH fusion construct or monoclonal antibodies were added to HEK293T cells stably transfected with an influenza M2 expression plasmid. Thirty minutes later, FcγR-ζ BW5147 reporter cells were added to the HEK293T cells. After overnight incubation produced mIL-2 was measured in a sandwich-ELISA, which served as an indicator for the magnitude of FcγR activation. (C) MDCK cells were infected with A/Puerto Rico/8/1934 (H1N1) virus for 1 h. Unbound virus particles were washed away and serial dilutions of the bispecific VHHs or monoclonal antibodies were added and incubated for 30 min, followed by the addition of the FcγRIV-ζ BW5147 reporter cells (C) or human FcγRIIIa-ζ BW5147 reporter cells (D) . After overnight incubation supernatants were analyzed by an anti mIL-2 sandwich ELISA. Data points represent averages of triplicates and error bars represent standard deviations. The graphs are a representative of one out of three repeat experiments.
    Figure Legend Snippet: Bispecific fusion construct of anti-mouse FcγRIV VHH with M2e-VHH-23m selectively activates FcγRIV in vitro . (A) Schematic representation of the bispecific VHHs and ELISA on human H3N2 M2e peptide and recombinant FcγRIV protein is shown on the right. Wells of microtiter plates were coated with 100 ng peptide or protein. Dilution series of the bispecific VHH fusion constructs were added to the coated plates. Binding was detected with a mouse anti-His tag MAb, followed by a secondary sheep anti-mouse IgG Ab conjugated to HRP for the peptide ELISA. In the ELISA with coated recombinant FcγRIV protein, binding was detected with a HRP-conjugated rabbit anti-camelid VHH antibody. (B) Serial dilutions of the bispecific VHH fusion construct or monoclonal antibodies were added to HEK293T cells stably transfected with an influenza M2 expression plasmid. Thirty minutes later, FcγR-ζ BW5147 reporter cells were added to the HEK293T cells. After overnight incubation produced mIL-2 was measured in a sandwich-ELISA, which served as an indicator for the magnitude of FcγR activation. (C) MDCK cells were infected with A/Puerto Rico/8/1934 (H1N1) virus for 1 h. Unbound virus particles were washed away and serial dilutions of the bispecific VHHs or monoclonal antibodies were added and incubated for 30 min, followed by the addition of the FcγRIV-ζ BW5147 reporter cells (C) or human FcγRIIIa-ζ BW5147 reporter cells (D) . After overnight incubation supernatants were analyzed by an anti mIL-2 sandwich ELISA. Data points represent averages of triplicates and error bars represent standard deviations. The graphs are a representative of one out of three repeat experiments.

    Techniques Used: Construct, In Vitro, Enzyme-linked Immunosorbent Assay, Recombinant, Binding Assay, Peptide ELISA, Protein Binding, Stable Transfection, Transfection, Expressing, Plasmid Preparation, Incubation, Produced, Sandwich ELISA, Activation Assay, Infection

    Related Articles

    Transfection:

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection
    Article Snippet: .. VHH Binding to FcγRs Expressing CellsHuman Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection. .. A GFP-reporter plasmid was co-transfected.

    Binding Assay:

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection
    Article Snippet: .. VHH Binding to FcγRs Expressing CellsHuman Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection. .. A GFP-reporter plasmid was co-transfected.

    Expressing:

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection
    Article Snippet: .. VHH Binding to FcγRs Expressing CellsHuman Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection. .. A GFP-reporter plasmid was co-transfected.

    Construct:

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection
    Article Snippet: .. VHH Binding to FcγRs Expressing CellsHuman Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection. .. A GFP-reporter plasmid was co-transfected.

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  • 92
    Sino Biological fcγriv
    Characterization of the isolated <t>FcγRIV-specific</t> VHH. (A) The predicted amino acid residue sequence of FcγRIV-VHH-7m, isolated after panning on recombinant mouse FcγRIV protein of a VHH library derived from a llama immunized with immature mouse dendritic cells. Above the sequences the Kabat numbering is indicated. CDR1, −2, and −3 are boxed. (B) Flow cytometric analysis showing binding of FcgRIV-VHH-7m and M2e-VHH-23m to HEK 293T cells transiently transfected with expression vectors coding for mouse FcγRI, FγRIIb, FcγRIII, and FcγRIV along with the common γ-chain for the activating FcγRs and a GFP expression plasmid. The lower graph depicts binding to Mf4/4 cells. The cells were incubated with fourfold serial dilution of Alexa Fluor™ 647 labeled FcγRIV-VHH-7m or M2e-VHH-23m, starting at a concentration of 0.2 μM, binding of the VHHs to the GFP positive cells was analyzed. Data points represent averages of triplicates and error bars standard deviations.
    Fcγriv, 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/fcγriv/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fcγriv - by Bioz Stars, 2021-02
    92/100 stars
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    Full length Clone DNA of Mouse syntaphilin with N terminal His tag
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    Full length Clone DNA of Mouse interleukin 6 with N terminal His tag
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    Characterization of the isolated FcγRIV-specific VHH. (A) The predicted amino acid residue sequence of FcγRIV-VHH-7m, isolated after panning on recombinant mouse FcγRIV protein of a VHH library derived from a llama immunized with immature mouse dendritic cells. Above the sequences the Kabat numbering is indicated. CDR1, −2, and −3 are boxed. (B) Flow cytometric analysis showing binding of FcgRIV-VHH-7m and M2e-VHH-23m to HEK 293T cells transiently transfected with expression vectors coding for mouse FcγRI, FγRIIb, FcγRIII, and FcγRIV along with the common γ-chain for the activating FcγRs and a GFP expression plasmid. The lower graph depicts binding to Mf4/4 cells. The cells were incubated with fourfold serial dilution of Alexa Fluor™ 647 labeled FcγRIV-VHH-7m or M2e-VHH-23m, starting at a concentration of 0.2 μM, binding of the VHHs to the GFP positive cells was analyzed. Data points represent averages of triplicates and error bars standard deviations.

    Journal: Frontiers in Immunology

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection

    doi: 10.3389/fimmu.2019.02920

    Figure Lengend Snippet: Characterization of the isolated FcγRIV-specific VHH. (A) The predicted amino acid residue sequence of FcγRIV-VHH-7m, isolated after panning on recombinant mouse FcγRIV protein of a VHH library derived from a llama immunized with immature mouse dendritic cells. Above the sequences the Kabat numbering is indicated. CDR1, −2, and −3 are boxed. (B) Flow cytometric analysis showing binding of FcgRIV-VHH-7m and M2e-VHH-23m to HEK 293T cells transiently transfected with expression vectors coding for mouse FcγRI, FγRIIb, FcγRIII, and FcγRIV along with the common γ-chain for the activating FcγRs and a GFP expression plasmid. The lower graph depicts binding to Mf4/4 cells. The cells were incubated with fourfold serial dilution of Alexa Fluor™ 647 labeled FcγRIV-VHH-7m or M2e-VHH-23m, starting at a concentration of 0.2 μM, binding of the VHHs to the GFP positive cells was analyzed. Data points represent averages of triplicates and error bars standard deviations.

    Article Snippet: VHH Binding to FcγRs Expressing Cells Human Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection.

    Techniques: Isolation, Sequencing, Recombinant, Derivative Assay, Flow Cytometry, Binding Assay, Transfection, Expressing, Plasmid Preparation, Incubation, Serial Dilution, Labeling, Concentration Assay

    Bispecific fusion construct of a FcγRIV- and M2e-specific VHH protects mice against a potentially lethal influenza A virus infection. (A) Groups of 16 (bispecific VHHs) or 14 (PBS) BALB/c mice were intranasally treated with 50 μg of the bispecific VHHs or PBS 4 h before and 24 h after challenge with 2xLD 50 of A/X47 (H3N2) influenza virus. Body weight change (left) and survival (right) were monitored for 14 days. The mean relative changes in body weight together with their standard errors, are represented. The difference in body weight loss between FcγRIV VHH-M2e VHH and the negative-control groups was statistically significant (*** P

    Journal: Frontiers in Immunology

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection

    doi: 10.3389/fimmu.2019.02920

    Figure Lengend Snippet: Bispecific fusion construct of a FcγRIV- and M2e-specific VHH protects mice against a potentially lethal influenza A virus infection. (A) Groups of 16 (bispecific VHHs) or 14 (PBS) BALB/c mice were intranasally treated with 50 μg of the bispecific VHHs or PBS 4 h before and 24 h after challenge with 2xLD 50 of A/X47 (H3N2) influenza virus. Body weight change (left) and survival (right) were monitored for 14 days. The mean relative changes in body weight together with their standard errors, are represented. The difference in body weight loss between FcγRIV VHH-M2e VHH and the negative-control groups was statistically significant (*** P

    Article Snippet: VHH Binding to FcγRs Expressing Cells Human Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection.

    Techniques: Construct, Mouse Assay, Infection, Negative Control

    Bispecific fusion construct of anti-mouse FcγRIV VHH with M2e-VHH-23m selectively activates FcγRIV in vitro . (A) Schematic representation of the bispecific VHHs and ELISA on human H3N2 M2e peptide and recombinant FcγRIV protein is shown on the right. Wells of microtiter plates were coated with 100 ng peptide or protein. Dilution series of the bispecific VHH fusion constructs were added to the coated plates. Binding was detected with a mouse anti-His tag MAb, followed by a secondary sheep anti-mouse IgG Ab conjugated to HRP for the peptide ELISA. In the ELISA with coated recombinant FcγRIV protein, binding was detected with a HRP-conjugated rabbit anti-camelid VHH antibody. (B) Serial dilutions of the bispecific VHH fusion construct or monoclonal antibodies were added to HEK293T cells stably transfected with an influenza M2 expression plasmid. Thirty minutes later, FcγR-ζ BW5147 reporter cells were added to the HEK293T cells. After overnight incubation produced mIL-2 was measured in a sandwich-ELISA, which served as an indicator for the magnitude of FcγR activation. (C) MDCK cells were infected with A/Puerto Rico/8/1934 (H1N1) virus for 1 h. Unbound virus particles were washed away and serial dilutions of the bispecific VHHs or monoclonal antibodies were added and incubated for 30 min, followed by the addition of the FcγRIV-ζ BW5147 reporter cells (C) or human FcγRIIIa-ζ BW5147 reporter cells (D) . After overnight incubation supernatants were analyzed by an anti mIL-2 sandwich ELISA. Data points represent averages of triplicates and error bars represent standard deviations. The graphs are a representative of one out of three repeat experiments.

    Journal: Frontiers in Immunology

    Article Title: Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection

    doi: 10.3389/fimmu.2019.02920

    Figure Lengend Snippet: Bispecific fusion construct of anti-mouse FcγRIV VHH with M2e-VHH-23m selectively activates FcγRIV in vitro . (A) Schematic representation of the bispecific VHHs and ELISA on human H3N2 M2e peptide and recombinant FcγRIV protein is shown on the right. Wells of microtiter plates were coated with 100 ng peptide or protein. Dilution series of the bispecific VHH fusion constructs were added to the coated plates. Binding was detected with a mouse anti-His tag MAb, followed by a secondary sheep anti-mouse IgG Ab conjugated to HRP for the peptide ELISA. In the ELISA with coated recombinant FcγRIV protein, binding was detected with a HRP-conjugated rabbit anti-camelid VHH antibody. (B) Serial dilutions of the bispecific VHH fusion construct or monoclonal antibodies were added to HEK293T cells stably transfected with an influenza M2 expression plasmid. Thirty minutes later, FcγR-ζ BW5147 reporter cells were added to the HEK293T cells. After overnight incubation produced mIL-2 was measured in a sandwich-ELISA, which served as an indicator for the magnitude of FcγR activation. (C) MDCK cells were infected with A/Puerto Rico/8/1934 (H1N1) virus for 1 h. Unbound virus particles were washed away and serial dilutions of the bispecific VHHs or monoclonal antibodies were added and incubated for 30 min, followed by the addition of the FcγRIV-ζ BW5147 reporter cells (C) or human FcγRIIIa-ζ BW5147 reporter cells (D) . After overnight incubation supernatants were analyzed by an anti mIL-2 sandwich ELISA. Data points represent averages of triplicates and error bars represent standard deviations. The graphs are a representative of one out of three repeat experiments.

    Article Snippet: VHH Binding to FcγRs Expressing Cells Human Embryonic Kidney (HEK) 293T cells were transiently transfected with full length mouse FcγRI (MG50086-CF), FcγRIIb (MG50030-CY, SinoBiological Inc.), FcγRIII (MG50326, SinoBiological Inc.) or FcγRIV (MG50036-CF, SinoBiological Inc.) expression constructs along with the common γ-chain for the activating FcγRs (MG50935-CF) by polyethylenimine (PEI)-based transfection.

    Techniques: Construct, In Vitro, Enzyme-linked Immunosorbent Assay, Recombinant, Binding Assay, Peptide ELISA, Protein Binding, Stable Transfection, Transfection, Expressing, Plasmid Preparation, Incubation, Produced, Sandwich ELISA, Activation Assay, Infection