Horseradish peroxidase conjugated goat anti human igg f ab 2

Manufactured by Jackson ImmunoResearch

Horseradish peroxidase conjugated goat-anti human IgG F(ab′)2 is a laboratory reagent used in immunoassay applications. It consists of goat-derived antibody fragments specific for the F(ab′)2 region of human immunoglobulin G (IgG), conjugated to the enzyme horseradish peroxidase.

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Lab products found in correlation

3 3 5 5 tetramethylbenzidine substrate, by Thermo Fisher Scientific (2 mentions) Maxisorp elisa plate, by Thermo Fisher Scientific (2 mentions) Tristar microplate reader, by Berthold Technologies (2 mentions)

Close spelling variants of this product

Horseradish peroxidase (189 citations) Peroxidase-conjugated anti-human IgG (10 citations) Horseradish peroxidase-conjugated goat anti-human IgG (8 citations) Horseradish peroxidase-conjugated anti-human IgG (8 citations) Peroxidase-conjugated goat anti-human IgG (7 citations)

2 protocols using horseradish peroxidase conjugated goat anti human igg f ab 2

Fc Receptor Binding Assay with Recombinant Proteins

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Recombinant murine FcγRI, FcγRIIb, and FcγRIV protein (R&D Systems) was immobilized on Maxisorp ELISA plates (Thermo Fisher) overnight in sodium bicarbonate buffer, pH 9.3. Plates were rinsed with PBS and 0.05% Tween-20 and blocked with 4% BSA for 1 h at 25°C. Intact or LALA-PG mAbs were diluted in 2% BSA and added to plates for 1 h at 25°C. After rinsing, primary mAbs were detected with horseradish peroxidase conjugated goat-anti human IgG F(ab′)2 (1:5,000 dilution, Jackson ImmunoResearch) for 1 h at 25°C. Plates were washed and developed with 3,3′-5,5′ tetramethylbenzidine substrate (Thermo Fisher), stopped with 2N H₂SO₄, and read at 450 nM using a TriStar Microplate Reader (Berthold).

Winkler E.S., Gilchuk P., Yu J., Bailey A.L., Chen R.E., Chong Z., Zost S.J., Jang H., Huang Y., Allen J.D., Case J.B., Sutton R.E., Carnahan R.H., Darling T.L., Boon A.C., Mack M., Head R.D., Ross T.M., Crowe JE J.r, & Diamond M.S. (2021). Human neutralizing antibodies against SARS-CoV-2 require intact Fc effector functions for optimal therapeutic protection. Cell, 184(7), 1804-1820.e16.

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Quantification of mAb Binding to Fc Receptors

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Recombinant FcγRI or FcγRIV protein (R&D Systems) was immobilized on Maxisorp ELISA plates (Thermo Fisher) overnight in sodium bicarbonate buffer, pH 9.3. Plates were rinsed with PBS and 0.05% Tween-20 and blocked with 4% BSA for 1 h at 25°C. Intact and N297Q mAbs were diluted in 2% BSA and added to plates for 1 h at 25°C. After subsequent rinses, primary mAbs were detected with horseradish peroxidase conjugated goat-anti human IgG F(ab’)₂ (1:5,000 dilution, Jackson ImmunoResearch) for 1 h at 25°C. Plates were washed and developed with 3,3′-5,5′ tetramethylbenzidine substrate (Thermo Fisher), stopped with 2 N H₂SO₄, and read at 450 nM using a TriStar Microplate Reader (Berthold).

Kim A.S., Kafai N.M., Winkler E.S., Gilliland TC J.r., Cottle E.L., Earnest J.T., Jethva P.N., Kaplonek P., Shah A.P., Fong R.H., Davidson E., Malonis R.J., Quiroz J.A., Williamson L.E., Vang L., Mack M., Crowe JE J.r., Doranz B.J., Lai J.R., Alter G., Gross M.L., Klimstra W.B., Fremont D.H, & Diamond M.S. (2021). Pan-protective anti-alphavirus human antibodies target a conserved E1 protein epitope. Cell, 184(17), 4414-4429.e19.

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