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anti human igg fc gen ii hfcii probes  (Gator Bio Inc)


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    Structured Review

    Gator Bio Inc anti human igg fc gen ii hfcii probes
    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg <t>mouse</t> <t>anti-human</t> TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
    Anti Human Igg Fc Gen Ii Hfcii Probes, supplied by Gator Bio Inc, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses"

    Article Title: CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses

    Journal: bioRxiv

    doi: 10.64898/2026.04.21.719929

    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg mouse anti-human TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
    Figure Legend Snippet: (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg mouse anti-human TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).

    Techniques Used: Staining, SDS Page, Purification, Binding Assay, Fluorescence, Labeling

    (A) Reducing/denaturing or non-denaturing Coomassie of sCD164 mutant proteins . Asterisk (*) denotes denaturing. (B) Final binding response of 1 µg N6B6 anti-human CD164 antibody to 100nM immobilized sCD164 mutants. (C) Inhibition of chimeric VSV expressing indicated glycoproteins by anti-CD164 monoclonal antibody, N6B6. Cells were pretreated with N6B6 for 1 hour on ice, virus was then added at MOI=1. At 6 hours post-infection, cells were fixed and % GFP-positive cells was determined by flow cytometry. % GPF+ was normalized to HeLa cells infected with no inhibition (n=2). (D) Relative expression of CD164 in CD164 mutant addback cells. Top: area under the curve (CD164/actin) compared to WT; bottom: representative Western blot. (E) Representative histograms of total CD164 expression in CD164 mutant addback cells.
    Figure Legend Snippet: (A) Reducing/denaturing or non-denaturing Coomassie of sCD164 mutant proteins . Asterisk (*) denotes denaturing. (B) Final binding response of 1 µg N6B6 anti-human CD164 antibody to 100nM immobilized sCD164 mutants. (C) Inhibition of chimeric VSV expressing indicated glycoproteins by anti-CD164 monoclonal antibody, N6B6. Cells were pretreated with N6B6 for 1 hour on ice, virus was then added at MOI=1. At 6 hours post-infection, cells were fixed and % GFP-positive cells was determined by flow cytometry. % GPF+ was normalized to HeLa cells infected with no inhibition (n=2). (D) Relative expression of CD164 in CD164 mutant addback cells. Top: area under the curve (CD164/actin) compared to WT; bottom: representative Western blot. (E) Representative histograms of total CD164 expression in CD164 mutant addback cells.

    Techniques Used: Mutagenesis, Binding Assay, Inhibition, Expressing, Virus, Infection, Flow Cytometry, Western Blot

    Related Articles

    Purification:

    Article Title: Anti-GAL3 antibodies and uses thereof
    Article Snippet: .. Purified antibodies were loaded at 10 ug/mL onto anti-human Fc probes using a Gator (Probe Life, East Palo Alto, CA) for 180 seconds. ..

    Article Title: Anti-Gal3 antibodies and uses thereof
    Article Snippet: Thereafter, the plate was washed three times with 300 μl of PBST per well, and 100 ul of avidin-HRP (1:1000) (Jackson ImmunoResearch) was then added to each well. .. Purified antibodies were loaded at 10 ug/mL onto anti-human Fc probes using a Gator (Probe Life, East Palo Alto, Calif.) for 180 seconds. .. 100 ul of TMB substrate (Fisher Scientific, 34029) was then added to each well.



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    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg <t>mouse</t> <t>anti-human</t> TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
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    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg <t>mouse</t> <t>anti-human</t> TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
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    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg <t>mouse</t> <t>anti-human</t> TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
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    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg <t>mouse</t> <t>anti-human</t> TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).
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    Image Search Results


    (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg mouse anti-human TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).

    Journal: bioRxiv

    Article Title: CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses

    doi: 10.64898/2026.04.21.719929

    Figure Lengend Snippet: (A) Coomassie-stained SDS-PAGE of soluble proteins used in . 2.5 µg of PNGaseF treated, nondenatured, or denatured purified protein. (B) Nonlinear fit of binding curves at pH 5.0 (blue) and 7.4 (grey) for PICV sGP1, PARV sGP1, FLEXV sGP1, and MACV sGP1 to 100 nM of immobilized sCD164. Curves represent the averaged final response at the end of association (n=3, independent experiments in triplicate). (C) Binding of 5 µM MACV sGP1 (maroon triangle) or 1 µg mouse anti-human TfR1 (CD71) antibody (cyan diamond) to 100 nM of immobilized hTfR1-Fc as a function of pH. Normalized to max binding at pH 8.0 (n=2, independent experiments in duplicate). (D) pH 7.4 binding curve of MACV sGP1 to hTfR1 (100 nM). Left: 1:1 Langmuir fit; middle: nonlinear fit; right: Scatchard plot. Binding affinity (K D ) calculated from 1:1 Langmuir fit, K D = 2.52 µM ± 0.006 µM. (n=2, independent experiments in duplicate). (E) Representative histogram of mean fluorescence intensity (MFI) from . Cells bound with 2.5 µM AF647-labeled PICV sGP1 at pH=6.0 (orange: CD164 KO +WT-CD164 PM ; purple: CD164 KO ) or pH 7.4 (red: CD164 KO +CD164 PM ; blue: CD164 KO ) (n=3, independent experiments in triplicate) (F) MFI (/10,000) of CD164 KO +WT-CD164 PM or CD164 KO cells from and S4E, labeled with 5 µM AF647-PICV sGP1 at pH 6.0 and then washed at pH 7.4 (hashed) or 6.0 (solid). (n=3, independent experiments in triplicate).

    Article Snippet: For each binding assay, sCD164-Fc, hTfR1-Fc, sCRD-Fc, or mutant CD164, were first immobilized on GatorBio anti-human IgG Fc Gen II (HFCII) probes (GatorBio,160024) for 300 sec.

    Techniques: Staining, SDS Page, Purification, Binding Assay, Fluorescence, Labeling

    (A) Reducing/denaturing or non-denaturing Coomassie of sCD164 mutant proteins . Asterisk (*) denotes denaturing. (B) Final binding response of 1 µg N6B6 anti-human CD164 antibody to 100nM immobilized sCD164 mutants. (C) Inhibition of chimeric VSV expressing indicated glycoproteins by anti-CD164 monoclonal antibody, N6B6. Cells were pretreated with N6B6 for 1 hour on ice, virus was then added at MOI=1. At 6 hours post-infection, cells were fixed and % GFP-positive cells was determined by flow cytometry. % GPF+ was normalized to HeLa cells infected with no inhibition (n=2). (D) Relative expression of CD164 in CD164 mutant addback cells. Top: area under the curve (CD164/actin) compared to WT; bottom: representative Western blot. (E) Representative histograms of total CD164 expression in CD164 mutant addback cells.

    Journal: bioRxiv

    Article Title: CD164 is an endolysomal host factor for entry of Clade A New World Arenaviruses

    doi: 10.64898/2026.04.21.719929

    Figure Lengend Snippet: (A) Reducing/denaturing or non-denaturing Coomassie of sCD164 mutant proteins . Asterisk (*) denotes denaturing. (B) Final binding response of 1 µg N6B6 anti-human CD164 antibody to 100nM immobilized sCD164 mutants. (C) Inhibition of chimeric VSV expressing indicated glycoproteins by anti-CD164 monoclonal antibody, N6B6. Cells were pretreated with N6B6 for 1 hour on ice, virus was then added at MOI=1. At 6 hours post-infection, cells were fixed and % GFP-positive cells was determined by flow cytometry. % GPF+ was normalized to HeLa cells infected with no inhibition (n=2). (D) Relative expression of CD164 in CD164 mutant addback cells. Top: area under the curve (CD164/actin) compared to WT; bottom: representative Western blot. (E) Representative histograms of total CD164 expression in CD164 mutant addback cells.

    Article Snippet: For each binding assay, sCD164-Fc, hTfR1-Fc, sCRD-Fc, or mutant CD164, were first immobilized on GatorBio anti-human IgG Fc Gen II (HFCII) probes (GatorBio,160024) for 300 sec.

    Techniques: Mutagenesis, Binding Assay, Inhibition, Expressing, Virus, Infection, Flow Cytometry, Western Blot