Polyclonal human igg

Manufactured by Thermo Fisher Scientific

Sourced in United States

Polyclonal human IgG is a laboratory reagent produced from pooled human serum. It contains a mixture of immunoglobulin G (IgG) antibodies that recognize a variety of epitopes. This product is commonly used as a reference standard or control in immunoassays and other immunological applications.

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Lab products found in correlation

Rituximab, by Genentech (1 mentions) Streptavidin sepharose, by GE Healthcare (1 mentions) Streptavidin coated magnetic beads, by New England Biolabs (1 mentions) Polystyrene beads, by Polysciences (1 mentions) Bevacizumab, by Genentech (1 mentions) Prism v8, by GraphPad (1 mentions) Prism 8, by GraphPad (1 mentions)

3 protocols using polyclonal human igg

Antibody-coated Bead Preparation for Protein Selections

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Streptavidin-coated magnetic beads (NEB) were used for selections/staining for streptavidin-specific DeNAno with no modifications. For rituximab and bevacizumab selections/staining, coated beads were made as follows: 6 μm polystyrene beads (Polysciences, Warrington, PA, USA) were washed with 20 mM sodium phosphate buffer pH 7.5 (Boston BioProducts, Ashland, MA, USA), then coated with 100 μg/ml rituximab (Genentech, South San Francisco, CA, USA), bevacizumab (Genentech), or polyclonal human IgG (Thermo Fisher Scientific, Waltham, MA, USA) diluted in 20 mM sodium phosphate pH 7.5. Beads and antibody were incubated for 2 h at room temperature (RT) or overnight at 4°C. Non-adsorbed antibody was removed with 3 × 1 ml washes with 20 mM sodium phosphate pH 7.5. Finally, beads were resuspended in phosphate bufferedsaline (PBS) (without calcium and magnesium, Mediatech, Manassas, VA, USA) supplemented with 0.02% NaN₃ (Ricca Chemical Company, Arlington, TX, USA).
In one control experiment, streptavidin polymethyl methacrylate (PMMA) (Sapidyne Instruments, Boise, ID, USA) and streptavidin sepharose (GE Healthcare Life Sciences, Piscataway, NJ, USA) were used in place of streptavidin magnetic beads.

Ruff L.E., Sapre A.A., Plaut J.S., De Maere E., Mortier C., Nguyen V., Separa K., Vandenbogaerde S., Vandewalle L., Esener S.C, & Messmer B.T. (2016). Selection of DNA nanoparticles with preferential binding to aggregated protein target. Nucleic Acids Research, 44(10), e96.

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HCVpp Neutralization Assay Protocol

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Neutralization assays were performed as described previously^{45 (link)}. MAbs were serially five-fold diluted, starting at a concentration of 100 μg/mL (leaving the last well as PBS only), and incubated with HCVpp for one hour at 37°C before addition to Huh7 target cells in duplicate. HCVpp entry was measured as above. The percentage of neutralization was calculated as [1 – (RLU_mAb / RLU_PBS)] × 100 with the PBS RLU values averaged across three plates. R04 and polyclonal human IgG (Thermo Fisher) were used as negative controls. Log₁₀ fifty percent inhibitory concentrations (log₁₀IC₅₀) were calculated from neutralization curves fit by nonlinear regression [log(inhibitor) vs. normalized response, variable slope] in Prism v8 (GraphPad Software). Mab-HCVpp tests that did not reach 50% inhibition were assigned an IC₅₀ of 100 μg/mL. IC₅₀ values for 7 mAbs generated with the final panel of 15 HCVpp are shown in Supplemental Table 2. Plasma samples were tested at a 1:20 dilution. Pooled plasma from 10 HCV-negative donors also at 1:20 dilution was used as a negative control. Percentage neutralization of each HCVpp was calculated as [1 – (RLU_{immune plasma} / RLU_{control plasma})] × 100.

Salas J.H., Urbanowicz R.A., Guest J.D., Frumento N., Figueroa A., Clark K.E., Keck Z., Cowton V.M., Cole S.J., Patel A.H., Fuerst T.R., Drummer H.E., Major M., Tarr A.W., Ball J.K., Law M., Pierce B.G., Foung S.K, & Bailey J.R. (2022). An Antigenically Diverse, Representative Panel of Envelope Glycoproteins for Hepatitis C Virus Vaccine Development. Gastroenterology, 162(2), 562-574.

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Neutralization Assay for HCV Pseudoparticles

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Neutralization assays were performed as described previously.⁴⁵ (link) mAbs were serially 5-fold diluted, starting at a concentration of 100 μg/mL (leaving the last well as phosphate-buffered saline [PBS] only), and incubated with HCVpps for 1 hour at 37°C before addition to Huh7 target cells in duplicate. HCVpps entry was measured as above. The percentage of neutralization was calculated as [1 − (RLU_mAb/RLU_PBS)] × 100, with the PBS RLU values averaged across 3 plates. R04 and polyclonal human IgG (Thermo Fisher, Waltham, MA) were used as negative controls. Log₁₀ 50% inhibitory concentrations (log₁₀IC₅₀) were calculated from neutralization curves fit by nonlinear regression (log[inhibitor] vs normalized response, variable slope) in Prism 8 software (GraphPad Software, San Diego, CA). mAb-HCVpp tests that did not reach 50% inhibition were assigned an IC₅₀ of 100 μg/mL. IC₅₀ values for 7 mAbs generated with the final panel of 15 HCVpps are listed in Supplementary Table 2. Plasma samples were tested at a 1:20 dilution. Pooled plasma from 10 HCV-negative donors also at 1:20 dilution was used as a negative control. The percentage neutralization of each HCVpp was calculated as [1 − (RLU_{immune plasma}/RLU_{control plasma})] × 100.

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