Horseradish peroxidase hrp conjugated goat anti mouse igg antibody

Manufactured by Merck Group

Sourced in United States

Horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody is a laboratory reagent used in various immunoassay techniques. It consists of a goat-derived antibody that specifically binds to mouse immunoglobulin G (IgG) molecules, conjugated to the enzyme horseradish peroxidase. The enzyme can catalyze a colorimetric or chemiluminescent reaction, allowing for the detection and quantification of target analytes in a sample.

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Lab products found in correlation

Complete freund adjuvant (cfa), by Merck Group (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Immuno plate, by Thermo Fisher Scientific (1 mentions) Ova solution, by Merck Group (1 mentions) Escherichia coli bl21 de3, by Tiangen Biotech (1 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by Biosharp (1 mentions) Mouse anti flag antibody, by Merck Group (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Mini beadbeater, by Biospec (1 mentions) Multispecies id screen toxoplasmosis indirect kit, by IDvet (1 mentions) 8 well chamber slide, by BD (1 mentions) Mouse monoclonal anti ha antibody, by Merck Group (1 mentions) Anti β actin antibody, by Merck Group (1 mentions) Lipofectamine ltx plus reagent, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG secondary antibody Horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG Horseradish peroxidase (HRP)-conjugated goat anti-mouse antibody Horseradish peroxidase (HRP)-conjugated anti-mouse IgG antibody Horseradish peroxidase-conjugated goat anti-mouse IgG antibody Goat-anti-mouse horseradish-peroxidase (HRP) antibody Anti-mouse horseradish peroxidase (HRP)-conjugated antibody Horseradish peroxidase-conjugated goat anti-mouse antibody Horseradish-peroxidase-conjugated anti-mouse IgG antibody Peroxidase-conjugated goat anti-mouse IgG antibody

8 protocols using horseradish peroxidase hrp conjugated goat anti mouse igg antibody

IgG Production Induction in Mice

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We induced mice in each group to produce IgG; production was initiated by the secondary immunization of a certain antigen. To achieve antigen-specific immunization, the mice were administered subcutaneously with ovalbumin (OVA) peptide dissolved in complete Freud’s adjuvant (CFA, Sigma-Aldrich Corp., St. Louis, MO, USA) after seven days of MAP treatment. A secondary injection of OVA peptide in incomplete Freud’s adjuvant (IFA, Sigma-Aldrich Corp., St. Louis, MO, USA) was performed eight days after the primary injection.
Following each immunization, peripheral blood samples were collected by retro-orbital bleeding of the live mice. Serum from the collected blood samples was used to monitor the IgG levels using an enzyme-linked immunosorbent assay (ELISA) analysis. An Immuno-plate (NUNC, Roskilde, Denmark) was coated overnight with OVA solution (in PBS, Sigma-Aldrich Corp.), followed by blocking with 10% fetal bovine saline (FBS) in PBS. The serum samples and standard were placed onto the plate, incubated, and then horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibodies (Sigma-Aldrich, Corp.) were added for specific binding, followed by 3,3′,5,5′-tetramethybenzidine (TMB) substrate solution and stop solution to detect the lgG concentration.

Lee Y., Im S.A., Kim J., Lee S., Kwon J., Lee H., Kong H., Song Y., Shin E., Do S.G., Lee C.K, & Kim K. (2016). Modified Aloe Polysaccharide Restores Chronic Stress-Induced Immunosuppression in Mice. International Journal of Molecular Sciences, 17(10), 1660.

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Quantifying Antibody Response to Ovalbumin Immunization

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The mice in each group were injected subcutaneously with ovalbumin (OVA) peptide suspended in complete Freud’s adjuvant (CFA, Sigma-Aldrich Corp., St. Louis MO, USA), followed by a secondary injection of OVA peptide in incomplete Freud’s adjuvant (IFA, Sigma-Aldrich Corp.). After the secondary immunization, the mice were euthanized, whole blood samples were collected, the serum was separated, and then immunoglobulin G (IgG) levels were measured by using an ELISA. In brief, an immunoplate (NUNC, Roskilde, Denmark) was coated overnight with 300 mg/mL of OVA solution (Sigma-Aldrich Corp.) followed by blocking with 10% fetal bovine serum (FBS) in PBS. The serum samples and standard were dropped onto the plate and incubated, followed by the addition of the horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibodies (Sigma-Aldrich, Corp.) for specific binding, and then incubation with 3,3′,5,5′-tetramethylbenzidine (TMB) substrate solution to determine the IgG concentration.

Lee Y., Kim J., An J., Lee S., Lee H., Kong H., Song Y., Choi H.R., Kwon J.W., Shin D., Lee C.K, & Kim K. (2016). Restoration of Declined Immune Responses and Hyperlipidemia by Rubus occidenalis in Diet-Induced Obese Mice. Biomolecules & Therapeutics, 25(2), 140-148.

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Recombinant Protein Expression and Purification

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The recombinant plasmids, pET‐28a (+)‐att, pET‐28a (+)‐trap, and pET‐28a (+)‐eAls, were transformed into in Escherichia coli BL21 (DE3) (Tiangen) and were expressed the ATT, TRAP, and eAls proteins with 0.1 mM isopropyl‐β‐D‐1‐thiogalactopyranoside (IPTG, Biosharp) induction at 37°C for 4 h, respectively. Then, the bacterial cells were obtained by centrifugation and were ultrasonicated, and the suspension was acquired. The His‐tagged ATT, TRAP, and eAls proteins were purified by using His‐binding‐resin (Novagen) according to the manufacturer's instructions. These proteins were confirmed with sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS‐PAGE) and Western blot. For Western blot, anti‐His tag monoclonal antibodies (mAbs) (Sigma) and horseradish peroxidase (HRP)‐conjugated goat antimouse IgG antibodies (Sigma) were used as the primary antibodies, the secondary antibodies, respectively.

Ma J., Liu W., Wang B., Yu S., Yu L., Song B., Yu Y., Zhu Z, & Cui Y. (2021). Als3‐Th‐cell‐epitopes plus the novel combined adjuvants of CpG, MDP, and FIA synergistically enhanced the immune response of recombinant TRAP derived from Staphylococcus aureus in mice. Immunity, Inflammation and Disease, 9(3), 971-983.

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Western Blot Analysis of Recombinant Protein

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To evaluate the expression of the protein of interest by the recombinant strains, pPG-COE/ΔAlr W56, pPG-Alr-COE/ΔAlr W56, pPG-T7g10-PPT/ΔAlr W56, and ΔAlr W56 were grown overnight in MRS broth with or without D-alanine, harvested by centrifugation at 10,000× g for 2 min and washed twice with sterile phosphate-buffered saline (PBS). The supernatants were lysed and centrifuged using a Mini-Beadbeater (BioSpec, Bartlesville, OK, USA) and separated in a 12% gel by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for the western blot assay. The proteins were then transferred to a polyvinylidene difluoride membrane (Millipore, Milford, MA, USA). Immunoblotting was performed using a mouse anti-Flag antibody (1:1000) as the primary antibody and horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody (1:5000) as the secondary antibody (Sigma-Aldrich, St. Louis, MO, USA). The results were visualized using a chemiluminescent substrate reagent (Thermo Fisher Scientific, Durham, NC, USA) according to the manufacturer’s instructions.

Li F., Wang X., Fan X., Sui L., Zhang H., Li Y., Zhou H., Wang L., Qiao X., Tang L, & Li Y. (2021). Immunogenicity of Recombinant-Deficient Lactobacillus casei with Complementary Plasmid Expressing Alanine Racemase Gene and Core Neutralizing Epitope Antigen against Porcine Epidemic Diarrhea Virus. Vaccines, 9(10), 1084.

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ELISA-based Toxoplasmosis Serology

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Serum obtained from C57BL/6 mice infected with T. gondii tachyzoites was assayed by enzyme-linked immunosorbent assay (ELISA) using antibodies against the T. gondii P30 protein with a Multispecies ID Screen® Toxoplasmosis Indirect kit (IDVET, Montpellier, France) following the manufacturer’s instructions. The serum was diluted 1:9 with dilution buffer and incubated for 1 h at room temperature. The plates were rinsed three times with washing buffer, after which horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody (Sigma, St. Louis, MO, USA) was added, and then, the plates were incubated for 1 h at room temperature. After the final washing, substrate solution was added to each well and incubated for 15 min at room temperature in the dark. The reaction was stopped using 0.5 M H₂SO₄ solution, and the absorbance was read at 450 nm using an ELISA reader. Mean OD values > 0.5 were defined as positive [28 (link)].

Seo H.H., Han H.W., Lee S.E., Hong S.H., Cho S.H., Kim S.C., Koo S.K, & Kim J.H. (2020). Modelling Toxoplasma gondii infection in human cerebral organoids. Emerging Microbes & Infections, 9(1), 1943-1954.

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Immunostaining of CD73 and STRO-1 in Cells

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The cells were cultured in an 8-well chamber slide (BD Falcon, Hamburg, Germany) and fixed with 4% paraformaldehyde for 30 min at 4°C. Then, the cells were washed with PBS, blocked, and permeabilized using 1% bovine serum albumin (BSA), 0.1% Triton X-100, 10% goat serum, and PBS for 30 min. Cells were then incubated in 1% BSA-PBS overnight at 4°C with the primary antibody [mouse anti-CD73 monoclonal antibody, unconjugated (Invitrogen, Carlsbad, CA, USA 1:100) and unconjugated mouse anti-STRO-1 monoclonal antibody (Invitrogen, Carlsbad, CA, USA 1:50)]. Subsequently, cells were incubated for 1.5 h with horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody (Sigma, 1:500). After 1 h of incubation with diaminobenzidine in darkness, images of the cells were produced using inverted microscope.

Kadivar M., Alijani N., Farahmandfar M., Rahmati S., Ghahhari N.M, & Mahdian R. (2014). Effect of acute hypoxia on CXCR4 gene expression in C57BL/6 mouse bone marrow-derived mesenchymal stem cells. Advanced Biomedical Research, 3, 222.

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Stability Analysis of S1 Protein in Mutant Strain

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The mutant strain S1/ΔAlr HLJ-27 was cultured overnight in MRS medium supplemented with 200 μg/mL d-alanine, and the bacterial precipitate was collected by centrifugation at 10,000 g for 2 min. The precipitate was incubated with 1% lysozyme and sonicated for 12% sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) detection and western blotting. SDS-PAGE was used to separate the proteins in the mixture, which were then transferred onto PVDF membranes (Millipore, Milford, MA, USA) using a mouse anti-S1 monoclonal antibody (mAb cell supernatant) prepared in our laboratory as the primary antibody (Xiao et al. 2022 (link)). Horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody (Sigma, Ronkonkoma, NY, USA) was used as the secondary antibody at a dilution of 1:5000. The results were evaluated using a chemiluminescent substrate reagent (Thermo Scientific, Durham, NC, USA) according to the manufacturer’s instructions. To determine the stability of S1 gene expression in the mutant strain S1/ΔAlr HLJ-27, protein samples for the western blot assay were obtained with every five generations of the strain within 20 generations. The strain ΔAlr HLJ-27 was used as a negative control.

Li F., Zhao H., Sui L., Yin F., Liu X., Guo G., Li J., Jiang Y., Cui W., Shan Z., Zhou H., Wang L., Qiao X., Tang L., Wang X, & Li Y. (2024). Assessing immunogenicity of CRISPR-NCas9 engineered strain against porcine epidemic diarrhea virus. Applied Microbiology and Biotechnology, 108(1), 248.

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PEDV Spike Protein Cleavage Confirmation

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In order to confirm the cleavability of PEDV S protein in Vero cells (with or without 18 µg/mL trypsin), Vero/TMPRSS2 (without trypsin) and Vero/MSPL (without trypsin) cells, cells were seeded into six-well plates and transfected with 2 µg/well of PEDV-S plasmids (pCMV-HA-S encoding PEDV LJB/03 S protein with an N-terminal HA tag, kept in our laboratory) using the Lipofectamine LTX & Plus Reagent (Invitrogen, Life Technologies, Carlsbad, CA, USA), empty pCMV-HA plasmid as a negative control. The cells were collected, separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and subsequently blotted onto PVDF membranes (Millipore, Milford, MA, USA). The PEDV S protein with an N-terminal HA-tag was analyzed using a mouse anti-HA monoclonal antibody (Sigma, USA) as the primary antibody and horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG antibody (Sigma, USA) as the secondary antibody, and proteins were visualized using a chemiluminescent substrate reagent (Thermo Scientific, Durham, NC). The expression ofβ-Actin was detected with an anti-β-actin antibody (Sigma, USA) as a loading control.

Wang X., Qiao X., Sui L., Zhao H., Li F., Tang Y.D., Shi W., Guo Y., Jiang Y., Wang L., Zhou H., Tang L., Xu Y, & Li Y. (2020). Establishment of stable Vero cell lines expressing TMPRSS2 and MSPL: A useful tool for propagating porcine epidemic diarrhea virus in the absence of exogenous trypsin. Virulence, 11(1), 669-685.

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