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Goat anti rabbit igg whole molecule peroxidase antibody

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Goat anti-rabbit IgG (whole molecule)-peroxidase antibody is a laboratory reagent used in various immunoassay techniques. It is an antibody produced in goats that specifically recognizes and binds to rabbit immunoglobulin G (IgG) molecules. The antibody is conjugated with the enzyme peroxidase, which can be utilized for signal detection and amplification in immunoassays.

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Lab products found in correlation

M iggκ bp hrp, by Santa Cruz Biotechnology (3 mentions) Cellytic m cell lysis reagent, by Merck Group (3 mentions) Rabbit anti actin antibody, by Merck Group (2 mentions) Mab810, by Merck Group (2 mentions) Ibright fl1500 imaging system, by Thermo Fisher Scientific (2 mentions) Amersham protran 0.45 μm nitrocellulose membrane, by GE Healthcare (2 mentions) Affinipure f ab 2 fragment goat anti mouse igg, by Jackson ImmunoResearch (2 mentions) Streptavidin, by Thermo Fisher Scientific (2 mentions) Anti gapdh, by Santa Cruz Biotechnology (2 mentions) Diaminobenzidine tetrahydrochloride, by Merck Group (1 mentions) Mini problott membranes, by Thermo Fisher Scientific (1 mentions) Rabbit anti mouse igg whole molecule peroxidase antibody, by Merck Group (1 mentions) Trans blot, by Bio-Rad (1 mentions) X ray film, by GE Healthcare (1 mentions) Immobilon p, by Merck Group (1 mentions) Anti gst, by Cell Signaling Technology (1 mentions) Anti his, by Merck Group (1 mentions) Anti gfp, by Abmart (1 mentions) Anti ub, by Cell Signaling Technology (1 mentions) Anti myc, by Merck Group (1 mentions)

8 protocols using goat anti rabbit igg whole molecule peroxidase antibody

1

Western Blot Analysis of HCMV Proteins

Cited 1 time
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Western blot was performed on triplicate infections carried out in confluent HFF in 6-well plates at the indicated MOI and treatment conditions. Sonicated whole-cell extracts in lysis buffer containing phosphatase and protease inhibitors were prepared as previously described (44 (link)). The gel-loading buffer contained 2% SDS and 100 mM beta-mercaptoethanol. The proteins were fractionated on freshly made 8% SDS-PAGE Tris-glycine gels prior to transfer to Amersham Protran 0.45-μm nitrocellulose membranes (GE Healthcare Life Sciences 10600002). HCMV IE1-72 and IE2-86 were detected by murine monoclonal antibody MAB810 (EMD Millipore, 1:1,000 dilution). Host actin was detected with polyclonal rabbit anti-actin antibody (Sigma-Aldrich, A2066, 1:4,000 dilution). Primary antibodies were detected with peroxidase AffiniPure F(ab’)2 fragment goat anti mouse IgG (Jackson ImmunoResearch, 115-036-006) at 1:40,000 dilution and goat anti-rabbit IgG (whole molecule)–peroxidase antibody (Sigma-Aldrich, A0545) at 1:40,000 dilution. Blots were imaged and analyzed using the iBright FL1500 Imaging System (Invitrogen).
Forte E., Li M., Ayaloglu Butun F., Hu Q., Borst E.M., Schipma M.J., Piunti A., Shilatifard A., Terhune S.S., Abecassis M., Meier J.L, & Hummel M. (2023). Critical Role for the Human Cytomegalovirus Major Immediate Early Proteins in Recruitment of RNA Polymerase II and H3K27Ac To an Enhancer-Like Element in OriLyt. Microbiology Spectrum, 11(1), e03144-22.
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2

Evaluating Anti-PHB Recombinant Protein Sera

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To test the quality and specificity of the sera produced against the PHB recombinant proteins, we loaded 20 μg of protein from different purification samples and mixed with 2× Laemmli sample buffer [15 ]. Samples were loaded on 12.5% PGE-SDS gels and afterwards the electrophoresis gels were stained with Coomassie blue or silver nitrate [16 (link)]. Protein bands were transferred onto a PVDF membrane (Mini ProBlott Membranes, Applied Biosystems, Foster City, CA, USA) using a Bio-Rad transblot. Membrane strips were then incubated for 2 h at 37 °C with diluted 1:50 sera and, after several washes with PBST (PBS + Tween20), they were incubated for 2 h at RT with rabbit anti-mouse IgG (whole molecule)-peroxidase antibody (Sigma Aldrich, St. Louis, Missouri, USA) for Leish r PHB1 or with goat anti-rabbit IgG (whole molecule)-peroxidase antibody (Sigma Aldrich) at 1:1,000 for Leish r PHB2. Samples were developed using diaminobenzidine tetrahydrochloride (Sigma Aldrich) as a substrate (0.05% w/v) and H2O2 (dilution 1/5000).
Cruz-Bustos T., Ibarrola-Vannucci A.K., Díaz-Lozano I., Ramírez J.L, & Osuna A. (2018). Characterization and functionality of two members of the SPFH protein superfamily, prohibitin 1 and 2 in Leishmania major. Parasites & Vectors, 11, 622.
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3

Western Blot Analysis of Protein Samples

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Protein samples were separated on home-made polyacrylamide gels and transferred to a PVDF film (Immobilon-P; Millipore) using a semi-dry method. After being blocked for 1 h at room temperature with blocking solution containing 5% milk in PBST (2.56 g/L Na2HPO4·7H2O, 8 g/L NaCl, 0.2 g/L KCl, 0.2 g/L KH2PO4, 0.1% Tween-20, pH 7.4), the film was incubated with primary antibody in PBST containing 3% bovine serum albumin (BSA; Sigma) overnight at 4 °C and then washed 3 times with PBST followed by incubation with 1:10000 dilution of Goat Anti-Mouse IgG (whole molecule)-Peroxidase antibody (Sigma) or Goat Anti-Rabbit IgG (whole molecule)-Peroxidase antibody (Sigma) in blocking solution for 1h at room temperature. After being washed 3 times with PBST, the PVDF film was developed with ECL prime (GE Healthcare) and visualized on X-ray film (GE Healthcare). The primary antibodies were anti-GFP (1:1000; Abmart), anti-Myc (1:1000; Sigma), anti-flag (1:2500; Sigma), anti-His (1:500; Sigma), anti-GST (1:1000; Cell Signaling Technology), anti-Ub (1:1000; Cell Signaling Technology) anti-CUL1 (1:1000) [42 (link)], anti-PIF3 (1:500) [10 (link)], anti-RPN6 (1:1000) [43 (link)] and anti-RPT5 (1:1000) [43 (link)].
Dong J., Ni W., Yu R., Deng X.W., Chen H, & Wei N. (2017). Light Dependent Degradation of PIF3 by SCFEBF1/2 Promotes the Photomorphogenic Response in Arabidopsis. Current biology : CB, 27(16), 2420-2430.e6.
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4

Western Blot Analysis of HCMV Proteins

Cited 1 time
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Western blot was performed on triplicate infections carried out in confluent HFF in 6-well plates at the indicated MOI and treatment conditions. Sonicated whole-cell extracts in lysis buffer containing phosphatase and protease inhibitors were prepared as previously described (44 (link)). The gel-loading buffer contained 2% SDS and 100 mM beta-mercaptoethanol. The proteins were fractionated on freshly made 8% SDS-PAGE Tris-glycine gels prior to transfer to Amersham Protran 0.45-μm nitrocellulose membranes (GE Healthcare Life Sciences 10600002). HCMV IE1-72 and IE2-86 were detected by murine monoclonal antibody MAB810 (EMD Millipore, 1:1,000 dilution). Host actin was detected with polyclonal rabbit anti-actin antibody (Sigma-Aldrich, A2066, 1:4,000 dilution). Primary antibodies were detected with peroxidase AffiniPure F(ab’)2 fragment goat anti mouse IgG (Jackson ImmunoResearch, 115-036-006) at 1:40,000 dilution and goat anti-rabbit IgG (whole molecule)–peroxidase antibody (Sigma-Aldrich, A0545) at 1:40,000 dilution. Blots were imaged and analyzed using the iBright FL1500 Imaging System (Invitrogen).
Forte E., Li M., Ayaloglu Butun F., Hu Q., Borst E.M., Schipma M.J., Piunti A., Shilatifard A., Terhune S.S., Abecassis M., Meier J.L, & Hummel M. (2023). Critical Role for the Human Cytomegalovirus Major Immediate Early Proteins in Recruitment of RNA Polymerase II and H3K27Ac To an Enhancer-Like Element in OriLyt. Microbiology Spectrum, 11(1), e03144-22.
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5

Protein Expression Profiling of MCF-7 and TamR Cells

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MCF-7 and TamR MCF-7 cells, which were cultured in a 6-well plate until their confluency levels reached 40–50%, were treated for 24 h with 4-OHT at the indicated concentrations. The cells were lysed with CelLytic M cell lysis reagent (Sigma-Aldrich), and the supernatant was collected for Western blot analysis. Primary antibodies employed for Western blot analysis included those recognizing human ATF3 (Santa Cruz Biotechnology, sc-81189), YTHDF2 (EMD Millipore, Q2490423), ABCB1 (ABclonal, A11747), and AK4 (Santa Cruz Biotechnology, sc-271161). Goat anti-rabbit IgG (whole molecule)-peroxidase antibody (Sigma-Aldrich, A0545) and m-IgGκ BP-HRP (Santa Cruz Biotechnology, sc-516102) were used as secondary antibodies. Membranes were also probed with anti-GAPDH antibody (Santa Cruz Biotechnology, sc-32233) to confirm equal protein loading.
Liu X., Yuan J., Zhang X., Li L., Dai X., Chen Q, & Wang Y. (2021). ATF3 Modulates the Resistance of Breast Cancer Cells to Tamoxifen through an N6‑Methyladenosine-Based Epitranscriptomic Mechanism. Chemical research in toxicology, 34(7), 1814-1821.
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6

Quantitative Protein Purification and Analysis

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Approximately 2 × 107 cells were harvested and lysed in CelLytic M Cell Lysis reagent supplemented with a complete protease inhibitor cocktail (Sigma-Aldrich). The lysates were subjected to rotation at 4 °C for 15 min, followed by sonication using a Qsonica sonicator q125 (1/8 probe) for 15 s three times (42% amplitude, 15 s on/15 s off). After sonication, the cell lysates were rotated for another 15 min and then centrifuged at 13,000 rpm for 10 min at 4 °C. The supernatant was incubated with prewashed anti-Flag M2 beads at 4 °C for 2 h. The beads were washed three times with PBS-T (PBS buffer containing 0.05% Tween 20), and subsequently boiled in 2× SDS–PAGE loading buffer to elute the captured proteins for western blot analysis.
Antibodies recognizing human XPO5 (Proteintech, #28628–1-AP; 1:2000), SOD1 (Proteintech, #10269–1-AP; 1:4000), V5 (Proteintech, #14440–1-AP; 1:2000), streptavidin (Thermo Scientific, #S911), and lamin B1 (Proteintech, #12987–1-AP; 1:10000) were used as primary antibodies for western blot analysis. Goat antirabbit IgG (whole molecule)-peroxidase antibody (Sigma, #A0545; 1:4000) and m-IgGκ BP-HRP (Santa Cruz Biotechnology, #sc-516102; 1:4000) were employed as secondary antibodies. Anti-GAPDH (Santa Cruz Biotechnology, #sc-32233; 1:10000) was used for internal control (GAPDH) to confirm an equal amount of protein loading.
Chen X., He X., Yang Y.Y, & Wang Y. (2022). Amyotrophic Lateral Sclerosis-Associated Mutants of SOD1 Modulate miRNA Biogenesis through Aberrant Interactions with Exportin 5. ACS chemical biology, 17(12), 3450-3457.
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7

Protein Characterization via Immunoblotting

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Protein samples were combined with Laemmli sample buffer and then loaded on 10% Criterion™ Tris–HCl Precast Gels (from Bio-Rad) and run at a constant voltage. Coomassie staining was achieved using GelCode® Blue Stain Reagent (from Thermo Scientific). For immunoblot, proteins were transferred to nitrocellulose membrane using a Trans-Blot® SD Semi-Dry Transfer Cell system (from Bio-Rad). Specific proteins were detected using peptide antibodies generated by Thermo Scientific’s Pierce Custom Antibody Services: CDH-1 (NCU00206), GH5-1 (NCU00762), GH10-1 (NCU05924), GH61-5 (NCU08760), GH51-1 (NCU02343) and GH10-2 (NCU08189). In addition, an antibody directed against GLA-1 (NCU01517) was kindly provided by Stephen Free. These primary antibodies were detected using a goat anti-rabbit IgG (whole molecule)-peroxidase antibody (from Sigma) secondary antibody. The specific protein bands were visualized using the LumiSensor™ Chemiluminescent HRP Substrate Kit (from GenScript) and ChemiDoc™ XRS+ molecular imager with Image Lab™ software (from Bio-Rad).
Reilly M.C., Qin L., Craig J.P., Starr T.L, & Glass N.L. (2015). Deletion of homologs of the SREPB pathway results in hyper-production of cellulases in Neurospora crassa and Trichoderma reesei. Biotechnology for Biofuels, 8, 121.
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8

Western Blot Analysis of Cell Lysates

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Cell lysis was conducted by using a CelLytic M cell lysis reagent (Sigma-Aldrich), and the supernatant was collected for Western blot experiments. The following primary antibodies were used: human Aha1 (Santa Cruz Biotechnology, sc-166610), HSP90 (Santa Cruz Biotechnology, sc-13119), SULT1A1 (Abclonal, A1599), V5 (Proteintech, no. 14440-1-AP), Flag (Cell Signaling Technology, no. 14973S), and streptavidin (Thermo Scientific, no. S911). The secondary antibodies were the goat anti-rabbit IgG (whole molecule)-peroxidase antibody (Sigma, no. A0545) and m-IgGκ BP-HRP (Santa Cruz Biotechnology, sc-516102). Membranes were also probed with anti-tubulin (Santa Cruz Biotechnology, sc-166729) or anti-GAPDH (Santa Cruz Biotechnology, sc-32233) to verify equal protein loading.
Liu X, & Wang Y. (2022). Aha1 Is an Autonomous Chaperone for SULT1A1. Chemical research in toxicology, 35(8), 1418-1424.
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