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Goat anti human igg conjugated with hrp horseradish peroxidase

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Goat anti-human IgG conjugated with HRP (horseradish peroxidase) is a secondary antibody reagent used in immunoassays and other immunochemical techniques. It is specific for human immunoglobulin G (IgG) and is labeled with the enzyme horseradish peroxidase, which can be detected through colorimetric or chemiluminescent methods.

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Lab products found in correlation

3 3 5 5 tetramethylbenzidine tmb substrate, by Thermo Fisher Scientific (5 mentions) 3 3 5 5 tetramethylbenzidine (tmb), by Thermo Fisher Scientific (4 mentions) Prism v8, by GraphPad (4 mentions) Recombinant zikv e protein, by Meridian Bioscience (2 mentions)

Spelling variants of this product

Goat anti-human IgG-HRP (33 citations) HRP-conjugated goat anti-human IgG (19 citations) HRP conjugated anti-human IgG (7 citations) Goat anti-human IgG conjugated with horseradish peroxidase (5 citations) Horseradish peroxidase–conjugated goat anti-human IgG (4 citations) Goat anti-human IgG conjugated with HRP (4 citations) Horseradish peroxidase (HRP)-conjugated goat anti-human IgG (3 citations) Horseradish peroxidase (HRP)-conjugated anti-human IgG (3 citations) Peroxidase-conjugated goat anti-human IgG (3 citations) Horseradish peroxidase (HRP)-conjugated anti-human (2 citations)

9 protocols using goat anti human igg conjugated with hrp horseradish peroxidase

1

SARS-CoV-2 Spike Protein Binding Assay

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Wells of 96-well microtiter plates were coated with purified recombinant SARS-CoV-2 S protein or SARS-CoV-2 SRBD protein at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech, Cat# 2040-05, Lot B3919-XD29, 1:5,000 dilution) and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (Thermo Fisher Scientific). Color development was monitored, 1 N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose-response assays, serial dilutions of purified mAbs were applied to the wells in triplicate, and mAb binding was detected as detailed above. Half-maximal effective concentration (EC50) values for binding were determined using Prism v8.0 software (GraphPad) after log transformation of mAb concentration using sigmoidal dose-response nonlinear regression analysis.
Zost S.J., Gilchuk P., Case J.B., Binshtein E., Chen R.E., Nkolola J.P., Schäfer A., Reidy J.X., Trivette A., Nargi R.S., Sutton R.E., Suryadevara N., Martinez D.R., Williamson L.E., Chen E.C., Jones T., Day S., Myers L., Hassan A.O., Kafai N.M., Winkler E.S., Fox J.M., Shrihari S., Mueller B.K., Meiler J., Chandrashekar A., Mercado N.B., Steinhardt J.J., Ren K., Loo Y.M., Kallewaard N.L., McCune B.T., Keeler S.P., Holtzman M.J., Barouch D.H., Gralinski L.E., Baric R.S., Thackray L.B., Diamond M.S., Carnahan R.H, & Crowe JE J.r. (2020). Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature, 584(7821), 443-449.
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2

SARS-CoV-2 Protein Binding Assay

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Wells of 96-well microtiter plates were coated with purified recombinant SARS-CoV-2 S protein, SARS-CoV-2 Srbd protein, SARS-CoV-2 SNTD (kindly provided by Patrick McTamney, Kuishu Ren, and Arnita Barnes, Astra Zeneca) or SARS-CoV S protein (kindly provided by Sandhya Bangaru and Andrew Ward, The Scripps Research Institute) at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. For mAb screening assays, CHO cell culture supernatants or purified mAbs were diluted 1:20 in blocking buffer, added to the wells, and incubated for 1 hr at ambient temperature. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech) and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (Thermo Fisher Scientific). Color development was monitored, 1N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose-response assays, serial dilutions of purified mAbs were applied to the wells in triplicate, and mAb binding was detected as detailed above. Half-maximal effective concentration (EC50) values for binding were determined using Prism v8.0 software (GraphPad) after log transformation of mAb concentration using sigmoidal dose-response nonlinear regression analysis.
Zost S.J., Gilchuk P., Chen R.E., Case J.B., Reidy J.X., Trivette A., Nargi R.S., Sutton R.E., Suryadevara N., Chen E.C., Binshtein E., Shrihari S., Ostrowski M., Chu H.Y., Didier J.E., MacRenaris K.W., Jones T., Day S., Myers L., Lee F.E., Nguyen D.C., Sanz I., Martinez D.R., Rothlauf P.W., Bloyet L.M., Whelan S.P., Baric R.S., Thackray L.B., Diamond M.S., Carnahan R.H, & Crowe JE J.r. (2020). Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein. Nature medicine, 26(9), 1422-1427.
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3

Antibody Binding Assay for Filovirus GPs

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Wells of microtiter plates were coated with purified, recombinant EBOV, BDBV, SUDV, or MARV GP ΔTM and incubated at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 h. For mAb screening assays, hybridoma culture supernatants were diluted in blocking buffer 1:5, added to the wells, and incubated for 1 h at ambient temperature. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech) and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (ThermoFisher Scientific). Color development was monitored, 1N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose-response and cross-reactivity assays, serial dilutions of purified mAbs were applied to the wells in triplicate or quadruplicate, and mAb binding was detected as detailed above.
Gilchuk P., Murin C.D., Milligan J.C., Cross R.W., Mire C.E., Ilinykh P.A., Huang K., Kuzmina N., Altman P.X., Hui S., Gunn B.M., Bryan A.L., Davidson E., Doranz B.J., Turner H.L., Alkutkar T., Flinko R., Orlandi C., Carnahan R., Nargi R., Bombardi R.G., Vodzak M.E., Li S., Okoli A., Ibeawuchi M., Ohiaeri B., Lewis G.K., Alter G., Bukreyev A., Saphire E.O., Geisbert T.W., Ward A.B, & Crowe JE J.r. (2020). Analysis of a Therapeutic Antibody Cocktail Reveals Determinants for Cooperative and Broad Ebolavirus Neutralization. Immunity, 52(2), 388-403.e12.
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4

Screening and Characterization of ZIKV E Antibodies

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Wells of 96-well microtiter plates were coated with purified recombinant ZIKV E protein (Meridian Bioscience) at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. For mAb screening assays, CHO cell culture supernatants or purified mAbs were diluted 1:20 in blocking buffer, added to the wells, and incubated for 1 hr at ambient temperature. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech) at 1:5,000 dilution and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (ThermoFisher Scientific). Color development was monitored, 1N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). O.D.450 nm of 0.3 was set as a threshold for mAb reactivity. This screening approach could underestimate the total number of target-specific mAbs in the panel but allowed elimination of poorly produced mAbs. For dose-response assays, serial dilutions of purified mAbs were applied to the wells in triplicate or quadruplicate, and mAb binding was detected as detailed above.
Gilchuk P., Bombardi R.G., Erasmus J.H., Tan Q., Nargi R., Soto C., Abbink P., Suscovich T.J., Durnell L.A., Khandhar A., Archer J., Liang J., Fouch M.E., Davidson E., Doranz B.J., Jones T., Larson E., Ertel S., Granger B., Fuerte-Stone J., Roy V., Broge T., Linnekin T.C., Linde C.H., Gorman M.J., Nkolola J., Alter G., Reed S.G., Barouch D.H., Diamond M.S., Crowe JE J.r., Van Hoeven N., Thackray L, & Carnahan R. (2020). Integrated pipeline for the accelerated discovery of antiviral antibody therapeutics. Nature biomedical engineering, 4(11), 1030-1043.
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5

Ebola Glycoprotein Antibody Screening

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Wells of microtiter plates were coated with purified, recombinant EBOV, BDBV, SUDV, or MARV GP ΔTM and incubated at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. For mAb screening assays, hybridoma culture supernatants were diluted in blocking buffer 1:5, added to the wells, and incubated for 1 hr at ambient temperature. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech) and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (ThermoFisher Scientific). Color development was monitored, 1N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose-response and cross-reactivity assays, serial dilutions of purified mAbs were applied to the wells in triplicate or quadruplicate, and mAb binding was detected as detailed above.
Gilchuk P., Murin C.D., Milligan J.C., Cross R.W., Mire C.E., Ilinykh P.A., Huang K., Kuzmina N., Altman P.X., Hui S., Gunn B.M., Bryan A.L., Davidson E., Doranz B.J., Turner H.L., Alkutkar T., Flinko R., Orlandi C., Carnahan R., Nargi R., Bombardi R.G., Vodzak M.E., Li S., Okoli A., Ibeawuchi M., Ohiaeri B., Lewis G.K., Alter G., Bukreyev A., Saphire E.O., Geisbert T.W., Ward A.B, & Crowe JE J.r. (2020). Analysis of a Therapeutic Antibody Cocktail Reveals Determinants for Cooperative and Broad Ebolavirus Neutralization. Immunity, 52(2), 388-403.e12.
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6

Screening and Characterization of ZIKV E Antibodies

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Wells of 96-well microtiter plates were coated with purified recombinant ZIKV E protein (Meridian Bioscience) at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. For mAb screening assays, CHO cell culture supernatants or purified mAbs were diluted 1:20 in blocking buffer, added to the wells, and incubated for 1 hr at ambient temperature. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech) at 1:5,000 dilution and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (ThermoFisher Scientific). Color development was monitored, 1N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). O.D.450 nm of 0.3 was set as a threshold for mAb reactivity. This screening approach could underestimate the total number of target-specific mAbs in the panel but allowed elimination of poorly produced mAbs. For dose-response assays, serial dilutions of purified mAbs were applied to the wells in triplicate or quadruplicate, and mAb binding was detected as detailed above.
Gilchuk P., Bombardi R.G., Erasmus J.H., Tan Q., Nargi R., Soto C., Abbink P., Suscovich T.J., Durnell L.A., Khandhar A., Archer J., Liang J., Fouch M.E., Davidson E., Doranz B.J., Jones T., Larson E., Ertel S., Granger B., Fuerte-Stone J., Roy V., Broge T., Linnekin T.C., Linde C.H., Gorman M.J., Nkolola J., Alter G., Reed S.G., Barouch D.H., Diamond M.S., Crowe JE J.r., Van Hoeven N., Thackray L, & Carnahan R. (2020). Integrated pipeline for the accelerated discovery of antiviral antibody therapeutics. Nature biomedical engineering, 4(11), 1030-1043.
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7

SARS-CoV-2 Spike Protein Binding Assay

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Wells of 96-well microtiter plates were coated with purified recombinant SARS-CoV-2 S protein or SARS-CoV-2 SRBD protein at 4°C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in DPBS containing 0.05% Tween-20 (DPBS-T) for 1 hr. The bound antibodies were detected using goat anti-human IgG conjugated with HRP (horseradish peroxidase) (Southern Biotech, Cat# 2040-05, Lot B3919-XD29, 1:5,000 dilution) and TMB (3,3′,5,5′-tetramethylbenzidine) substrate (Thermo Fisher Scientific). Color development was monitored, 1 N hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose-response assays, serial dilutions of purified mAbs were applied to the wells in triplicate, and mAb binding was detected as detailed above. Half-maximal effective concentration (EC50) values for binding were determined using Prism v8.0 software (GraphPad) after log transformation of mAb concentration using sigmoidal dose-response nonlinear regression analysis.
Zost S.J., Gilchuk P., Case J.B., Binshtein E., Chen R.E., Nkolola J.P., Schäfer A., Reidy J.X., Trivette A., Nargi R.S., Sutton R.E., Suryadevara N., Martinez D.R., Williamson L.E., Chen E.C., Jones T., Day S., Myers L., Hassan A.O., Kafai N.M., Winkler E.S., Fox J.M., Shrihari S., Mueller B.K., Meiler J., Chandrashekar A., Mercado N.B., Steinhardt J.J., Ren K., Loo Y.M., Kallewaard N.L., McCune B.T., Keeler S.P., Holtzman M.J., Barouch D.H., Gralinski L.E., Baric R.S., Thackray L.B., Diamond M.S., Carnahan R.H, & Crowe JE J.r. (2020). Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature, 584(7821), 443-449.
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8

SARS-CoV-2 Antigen Binding Assay

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Wells of 96-well microtiter plates were coated with purified recombinant SARS-CoV-2 S6Pecto, SARS-CoV-2 S NTD, or SARS-CoV-2 RBS protein at 4 °C overnight. Plates were blocked with 2% non-fat dry milk and 2% normal goat serum in Dulbecco’s phosphate-buffered saline (DPBS) containing 0.05% Tween-20 (DPBS-T) for 1 h. The bound antibodies were detected using goat anti-human IgG conjugated with horseradish peroxidase (HRP) (Southern Biotech, cat. 2040-05, lot B3919-XD29, 1:5,000 dilution) and a 3,3′,5,5′-tetramethylbenzidine (TMB) substrate (Thermo Fisher Scientific). Color development was monitored, 1M HCl was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). For dose–response assays, serial dilutions of purified mAbs were applied to the wells in triplicate, and antibody binding was detected as detailed above. EC50 values for binding were determined using Prism v.8.0 software (GraphPad) after log transformation of the mAb concentration using sigmoidal dose–response nonlinear regression analysis.
Suryadevara N., Shrihari S., Gilchuk P., VanBlargan L.A., Binshtein E., Zost S.J., Nargi R.S., Sutton R.E., Winkler E.S., Chen E.C., Fouch M.E., Davidson E., Doranz B.J., Chen R.E., Shi P.Y., Carnahan R.H., Thackray L.B., Diamond M.S, & Crowe JE J.r. (2021). Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. Cell, 184(9), 2316-2331.e15.
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9

SARS-CoV-2 RBD Protein Binding ELISA

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For screening and characterizing the second set of 204 designs (Fig. ED2), wells of 384-well microtiter plates were coated with purified recombinant SARS-CoV-2 RBD proteins at 4 °C overnight at an antigen concentration of 2 mg/mL. Plates were washed with Dulbecco’s phosphate-buffered saline (DPBS) containing 0.05% Tween-20 (DPBS-T) and blocked with 2% bovine serum albumin and 2% normal goat serum in DPBS-T (blocking buffer) for 1 h. mAbs were diluted in 12 three-fold serial dilutions in blocking buffer at a starting concentration of 10 μg/mL. Plates were then washed and mAb dilutions were added and incubated for 1 h. Plates were washed, a goat anti-human IgG conjugated with horseradish peroxidase (HRP) (Southern Biotech, cat. 2014-05, lot L2118-VG00B, 1:5,000 dilution in blocking buffer) was added, and the plates were incubated for 1 h. After plates were washed, signal was developed with a 3,3’,5,5’-tetramethylbenzidine (TMB) substrate (Thermo Fisher Scientific). Color development was monitored, 1M hydrochloric acid was added to stop the reaction, and the absorbance was measured at 450 nm using a spectrophotometer (Biotek). Dose-response ELISAs were performed in technical triplicate with at least two independent experimental replicates.
Desautels T.A., Arrildt K.T., Zemla A.T., Lau E.Y., Zhu F., Ricci D., Cronin S., Zost S.J., Binshtein E., Scheaffer S.M., Dadonaite B., Petersen B.K., Engdahl T.B., Chen E., Handal L.S., Hall L., Goforth J.W., Vashchenko D., Nguyen S., Weilhammer D.R., Lo J.K., Rubinfeld B., Saada E.A., Weisenberger T., Lee T.H., Whitener B., Case J.B., Ladd A., Silva M.S., Haluska R.M., Grzesiak E.A., Earnhart C.G., Hopkins S., Bates T.W., Thackray L.B., Segelke B.W., Lillo A.M., Sundaram S., Bloom J., Diamond M.S., Crowe JE J.r., Carnahan R.H, & Faissol D.M. (2023). Computationally restoring the potency of a clinical antibody against SARS-CoV-2 Omicron subvariants. bioRxiv.
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