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his tag antibody (hrp), mouse mab  (Sino Biological)


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    Structured Review

    Sino Biological his tag antibody (hrp), mouse mab
    His Tag Antibody (Hrp), Mouse Mab, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+antibody+hrp/His+Tag+Antibody+(HRP)%2C+Mouse+MAb/custom%40105327-mm02t-h%4041839884
    Average 94 stars, based on 24 article reviews
    his tag antibody (hrp), mouse mab - by Bioz Stars, 2026-09
    94/100 stars

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    Incubation:

    Article Title: D3AI-Spike: A deep learning platform for predicting binding affinity between SARS-CoV-2 spike Receptor Binding Domain with multiple amino acid mutations and human angiotensin-converting enzyme 2
    Article Snippet: Then the plates were blocked for 1 h at 37 °C using 3% BAS in phosphate-buffered saline (PBS) (Thermo Fisher Scientific, Waltham, MA, USA), and finally incubated with 4- fold serial dilutions of RBDs at 37 °C for 1 h. The tested concentrations were between 10 μg/mL and 9.54 pg/mL. .. His tag antibody (HRP) (Sino Biological) diluted 1/10,000 was applied, and the plate was incubated at 37 °C for 1 h. After washing the plate thrice with 0.1% PBST, TMB substrate (SeraCare, Milford, MA, USA) was added and the reaction was terminated with 2 M H 2 SO 4 , and the absorbance was read at 450 nm with an Infinite F50 microplate reader (Tecan Trading AG, Zürich, Switzerland). ..

    Article Title: D3AI-Spike: A deep learning platform for predicting binding affinity between SARS-CoV-2 spike receptor binding domain with multiple amino acid mutations and human angiotensin-converting enzyme 2.
    Article Snippet: Then the plates were blocked for 1 h at 37 ◦C using 3% BAS in phosphate-buffered saline (PBS) (Thermo Fisher Scientific, Waltham, MA, USA), and finally incubated with 4- fold serial dilutions of RBDs at 37 ◦C for 1 h. The tested concentrations were between 10 μg/mL and 9.54 pg/mL. .. His tag antibody (HRP) (Sino Biological) diluted 1/10,000 was applied, and the plate was incubated at 37 ◦C for 1 h. After washing the plate thrice with 0.1% PBST, TMB substrate (SeraCare, Milford, MA, USA) was added and the reaction was terminated with 2 M H2SO4, and the absorbance was read at 450 nm with an Infinite F50 microplate reader (Tecan Trading AG, Zürich, Switzerland). ..

    Article Title: SARS-CoV-2 Omicron RBD shows weaker binding affinity than the currently dominant Delta variant to human ACE2
    Article Snippet: To measure the affinity constant of SARS-CoV-2 Spike protein RBDWT (His Tag) 80 (GenScript), SARS-CoV-2 Spike RBDDelta (K417N, L452R, T478K) protein (His Tag) 81 (Sino Biological), and SARS-CoV-2 B.1.1.529 (Omicron) Spike RBD protein (His Tag) 82 (Sino Biological) against the ACE2-Fc protein (GenScript), a non-competitive ELISA 83 was performed.18 After being coated with 1, 2, and 4 μg/mL ACE2-Fc Tag protein 84 overnight at 4°C, the 96-well plates were washed with 0.1% PBST, blocked with 3% 85 BSA in PBS (Thermo Fisher Scientific, Waltham, MA, USA), and then incubated with 86 4- fold serial dilutions of RBDs at 37 °C for 1 h. The tested concentrations were between 87 S4 10 μg/mL and 38 pg/mL. .. Thereafter, His tag antibody (HRP) (Sino Biological) was 88 added at 1:10000 dilution, and the plate was incubated at 37 °C for 1 h. After washing 89 the plate thrice with 0.1% PBST, TMB substrate (SeraCare, Milford, MA, USA) was 90 added and the reaction was stopped with 2 M H2SO4, and the absorbance was read at 91 450 nm with Infinite F50 microplate reader (Tecan Trading AG, Zürich, Switzerland). ..

    Article Title: TREM2 Recognition of Candidalysin Orchestrates Mucosal Immunity in Oropharyngeal Candidiasis
    Article Snippet: .. His tag antibody (HRP) (Sino Biological) was added and incubated for an additional hour at 37°C. .. Following additional washing, the binding of His-TREM2 was quanti ed using an ELISA kit as recommended by the manufacture (Multi sciences).

    Article Title: TREM2 Recognition of Candidalysin Orchestrates Mucosal Immunity in Oropharyngeal Candidiasis
    Article Snippet: .. His tag antibody (HRP) (Sino Biological) was added and incubated for an additional hour at 37°C. .. Following additional washing, the binding of His-TREM2 was quanti ed using an ELISA kit as recommended by the manufacture (Multi sciences).

    Article Title: Exploring the Binding Affinity and Mechanism between ACE2 and the Trimers of Delta and Omicron Spike Proteins by Molecular Dynamics Simulation and Bioassay.
    Article Snippet: Five major variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have emerged and posed challenges in controlling the pandemic.. Among them, the current dominant variant, viz., Omicron, has raised serious concerns about its infectiousness and antibody neutralization.. However, few studies pay attention to the effect of the mutations on the dynamic interaction network of Omicron S protein trimers binding to the host angiotensin-converting enzyme 2 (ACE2).



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    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Proteintech hrp conjugated polymer secondary antibody
    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Proteintech hrp his
    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse <t>monoclonal</t> antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.
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    Proteintech anti his hrp conjugated ab
    Solid-phase binding assays validate interactions between recombinant FHR proteins and selected serum ligands. When testing C4 and CTSG binding, C4 and CTSG were immobilized on microtiter plates and incubated with the FHR proteins. Whereas testing MBL2, and PPBP binding with FHR proteins, recombinant FHR proteins, FHL-1, and FH were immobilized on microtiter plates and incubated with the indicated candidate ligands: ( a ) Complement C4 (C4), ( b ) cathepsin G (CTSG), ( c ) mannose-binding lectin 2 (MBL2), and ( d ) platelet basic protein (PPBP). Bound ligands were detected using ligand-specific antibodies followed by <t>HRP-conjugated</t> secondary antibodies and colorimetric detection at 450 nm. Bar graphs represent mean ± SEM from three independent experiments, each with four technical replicates ( n = 3).
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    BPS Bioscience anti his hrp
    Solid-phase binding assays validate interactions between recombinant FHR proteins and selected serum ligands. When testing C4 and CTSG binding, C4 and CTSG were immobilized on microtiter plates and incubated with the FHR proteins. Whereas testing MBL2, and PPBP binding with FHR proteins, recombinant FHR proteins, FHL-1, and FH were immobilized on microtiter plates and incubated with the indicated candidate ligands: ( a ) Complement C4 (C4), ( b ) cathepsin G (CTSG), ( c ) mannose-binding lectin 2 (MBL2), and ( d ) platelet basic protein (PPBP). Bound ligands were detected using ligand-specific antibodies followed by <t>HRP-conjugated</t> secondary antibodies and colorimetric detection at 450 nm. Bar graphs represent mean ± SEM from three independent experiments, each with four technical replicates ( n = 3).
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    Image Search Results


    Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse monoclonal antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.

    Journal: Biotechnology Reports

    Article Title: Comparative analysis of anti-MICA scFv affinities: Insights from three label-free biophysical methods and biological validation

    doi: 10.1016/j.btre.2026.e00955

    Figure Lengend Snippet: Characterization of Recombinant Proteins: MICA and anti-MICA scFvs. (A) Molecular model, shown as a ribbon representation, of the variable fragment of the anti-MICA scFvs. The framework is displayed in white, the light chain CDRs are shown in cyan, and the heavy chain CDRs are shown in yellow. The residues with mutations are shown as magenta spheres [residues 32 (CDR L1), 164 (CDR H1), and 188/190 (CDR H2)]. (B) Schematic diagram of the scFv gene. The modified pET-15b vector was used for the expression of the WT and Beta mutant scFvs, each carrying four mutations: I32Y in CDR1 of the VL, and S164F, P188W, and G190W in CDR1, CDR2, and CDR2 of the VH, respectively. Recombinant proteins were expressed in E. coli BL21(DE3). (C) SDS-PAGE analysis showing the purity of recombinant proteins: WT scFv, Beta mutant scFv, and MICA. Proteins were resolved on a 12% acrylamide gel under reducing conditions. SDS-PAGE results show the soluble fraction (SF), unbound protein (UBP), elution of purified scFv (E), renatured proteins (R) and inclusion bodies (IB). MW, molecular weight. (D-E) Western blot analysis confirming the identity of scFvs and MICA using an anti-HisTag antibody. For the identification of the WT and Beta mutant scFvs, Anti-6xHis Epitope Tag mouse monoclonal antibody conjugated with peroxidase (200-303-382) was used at a dilution of 1:1000. For the identification of MICA, a biotinylated Anti-MICA antibody (BAMO3 (BAFI300, BamOmaB)) and Streptavidin were used at a dilution of 1:2000. A total of 2 μg of purified protein was loaded. The negative control (Ctrl -) for MICA detection was WT scFv and MICA protein was used for scFv detection. Original gel is presented in Fig. S1, Supplementary information.

    Article Snippet: The identity of MICA and scFvs proteins was confirmed by western blot using a HRP-conjugated anti-His tag monoclonal antibody (200-303-382, Rockland, USA).

    Techniques: Recombinant, Modification, Plasmid Preparation, Expressing, Mutagenesis, SDS Page, Acrylamide Gel Assay, Purification, Molecular Weight, Western Blot, Negative Control

    Solid-phase binding assays validate interactions between recombinant FHR proteins and selected serum ligands. When testing C4 and CTSG binding, C4 and CTSG were immobilized on microtiter plates and incubated with the FHR proteins. Whereas testing MBL2, and PPBP binding with FHR proteins, recombinant FHR proteins, FHL-1, and FH were immobilized on microtiter plates and incubated with the indicated candidate ligands: ( a ) Complement C4 (C4), ( b ) cathepsin G (CTSG), ( c ) mannose-binding lectin 2 (MBL2), and ( d ) platelet basic protein (PPBP). Bound ligands were detected using ligand-specific antibodies followed by HRP-conjugated secondary antibodies and colorimetric detection at 450 nm. Bar graphs represent mean ± SEM from three independent experiments, each with four technical replicates ( n = 3).

    Journal: Scientific Reports

    Article Title: Identification of novel blood-borne soluble binding partners of factor H-related proteins

    doi: 10.1038/s41598-026-44779-9

    Figure Lengend Snippet: Solid-phase binding assays validate interactions between recombinant FHR proteins and selected serum ligands. When testing C4 and CTSG binding, C4 and CTSG were immobilized on microtiter plates and incubated with the FHR proteins. Whereas testing MBL2, and PPBP binding with FHR proteins, recombinant FHR proteins, FHL-1, and FH were immobilized on microtiter plates and incubated with the indicated candidate ligands: ( a ) Complement C4 (C4), ( b ) cathepsin G (CTSG), ( c ) mannose-binding lectin 2 (MBL2), and ( d ) platelet basic protein (PPBP). Bound ligands were detected using ligand-specific antibodies followed by HRP-conjugated secondary antibodies and colorimetric detection at 450 nm. Bar graphs represent mean ± SEM from three independent experiments, each with four technical replicates ( n = 3).

    Article Snippet: Bound FHR proteins were detected through their His 6 tag using an anti-His HRP-conjugated Ab (Proteintech., HRP-66005).

    Techniques: Binding Assay, Recombinant, Incubation