Hrp conjugated anti mouse igg secondary antibody

Manufactured by GE Healthcare

Sourced in United States

The HRP-conjugated anti-mouse IgG secondary antibody is a laboratory reagent used to detect the presence of mouse immunoglobulin G (IgG) in various assays and experiments. The antibody is conjugated with horseradish peroxidase (HRP), which allows for colorimetric or chemiluminescent detection of the target mouse IgG.

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Lab products found in correlation

Ab113687, by Abcam (1 mentions) Anti pgk1, by Abcam (1 mentions) Pierce ecl chemiluminescence substrate, by Thermo Fisher Scientific (1 mentions) Image quant las 4000 station, by GE Healthcare (1 mentions) Nitrocellulose, by GE Healthcare (1 mentions) Hrp conjugated neutravidin, by Thermo Fisher Scientific (1 mentions) Bio dot apparatus assembly, by Bio-Rad (1 mentions) Anti 5mc antibody, by Diagenode (1 mentions) Wizard genomic dna purification kit, by Promega (1 mentions) Immobilon p pvdf membrane, by Merck Group (1 mentions) Anti rabbit igg antibody, by GE Healthcare (1 mentions) Pk mg proteins, by Fujifilm (1 mentions) Anti gapdh antibody, by Santa Cruz Biotechnology (1 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (1 mentions) Image gauge software, by Fujifilm (1 mentions) Las 4000 mini, by Fujifilm (1 mentions) Sigmafast o phenylenediamine tablets, by Merck Group (1 mentions) Mouse anti flag m2 primary antibody, by Merck Group (1 mentions)

Close spelling variants of this product

HRP-conjugated secondary antibodies (278 citations) HRP-conjugated anti-mouse secondary antibody (25 citations) HRP-conjugated anti-mouse antibody (8 citations) HRP anti-mouse (3 citations) Secondary anti‐mouse (2 citations)

5 protocols using hrp conjugated anti mouse igg secondary antibody

Quantitative BteA Protein Analysis

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Yeast cells harboring pYC2-CT derivatives encoding BteA-GFP fusion proteins were cultivated in SC-Ura-galactose media for 2, 5, and 20 h to induce the BteA expression. Equivalents of OD₆₀₀ = 1 of yeast cell cultures were collected and denatured yeast protein extracts were prepared by NaOH lysis/TCA precipitation method according to Volland et al. 1994 [41 (link)]. Equal amounts of protein extracts were separated by SDS-PAGE electrophoresis (10% gel) followed by the transfer onto a nitrocellulose membrane. Membranes were probed overnight with mouse polyclonal antibodies raised against BteA (dilution 1:10,000, kindly provided by Branislav Vecerek, Institute of Microbiology, Prague, Czech Republic) or mouse monoclonal antibody against yeast phosphoglycerate kinase PGK1 (anti-PGK1, dilution 1:5,000, Abcam, ab113687) as a loading control. The detected proteins were revealed with 1:3,000-diluted horseradish peroxidase (HRP)-conjugated anti-mouse IgG secondary antibody (GE Healthcare) using a Pierce ECL chemiluminescence substrate (Thermo Fisher Scientific, USA) and an Image Quant LAS 4000 station (GE Healthcare, USA).

Bayram J., Malcova I., Sinkovec L., Holubova J., Streparola G., Jurnecka D., Kucera J., Sedlacek R., Sebo P, & Kamanova J. (2020). Cytotoxicity of the effector protein BteA was attenuated in Bordetella pertussis by insertion of an alanine residue. PLoS Pathogens, 16(8), e1008512.

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Sindbis Viral Envelope Protein Analysis

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Viral vectors (0.3–0.5 μg protein) were separated on a 12% Bis-Tris NuPAGE gel (Life Technologies Corporation, Carlsbad, CA) under reducing conditions. Proteins were transferred to nitrocellulose (GE Healthcare Biosciences, Pittsburgh, PA). Immunoblot analysis of envelope proteins was performed with anti-Sindbis ascites fluid (ATCC, Manassas, VA) and HRP-conjugated anti-mouse IgG secondary antibody (GE Healthcare Biosciences). Biotinylation of envelope proteins was detected using HRP-conjugated NeutrAvidin^® (Thermo Fisher Scientific). Protein bands were visualized using Chemiglow and Alpha Innotech FluorChem Imaging System (ProteinSimple, Santa Clara, CA).

Leoh L.S., Morizono K., Kershaw K.M., Chen I.S., Penichet M.L, & Daniels-Wells T.R. (2014). Gene delivery in malignant B cells using the combination of lentiviruses conjugated to anti-transferrin receptor antibodies and an immunoglobulin promoter. The journal of gene medicine, 16(0), 11-27.

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Quantifying Genomic 5-Methylcytosine Levels

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5-mC dot blot assays were performed as previously described (Cai et al., 2017 (link)). Briefly, genomic DNA was extracted using the Wizard Genomic DNA Purification Kit (Promega) and diluted in TE buffer. The DNA samples were denatured in 0.4 M NaOH/10 mM EDTA at 95 °C for 10 min, and immediately neutralized with equal volume of ice-cold 2 M NH4OAc (pH 7.0). The samples were spotted on a pre-wetted nitrocellulose membrane in two-fold serial dilutions using a Bio-Dot Apparatus Assembly (Bio-Rad). The membrane was rinsed briefly in 2x SSC, baked at 80 °C for 2 hours, blocked in 5% non-fat milk for 1 hour at room temperature and incubated with anti-5-mC antibody (Diagenode, C15200081, 1:300) at 4 °C overnight. The membrane was washed in TBST (5 × 5 min), incubated with HRP-conjugated anti-mouse IgG secondary antibody (GE, 1:5000) for 1 hour at room temp, incubated with ECL substrate (Pierce), and developed.

Kong X., Chen J., Xie W., Brown S.M., Cai Y., Wu K., Fan D., Nie Y., Yegnasubramanian S., Tiedemann R.L., Tao Y., Yen R.W., Topper M.J., Zahnow C.A., Easwaran H., Rothbart S.B., Xia L, & Baylin S.B. (2019). Defining UHRF1 Domains That Support Maintenance of Human Colon Cancer DNA Methylation and Oncogenic Properties. Cancer cell, 35(4), 633-648.e7.

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Western Blot Detection of PrP^Sc

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For detection of PrP^Sc, brain homogenates and cell lysates treated with PK (20 μg PK/mg proteins; Wako Pure Chemical Industries) at 37 °C for 30 min. Total proteins were separated by 15% SDS-polyacrylamide gels and then electrically transferred onto an Immobilon-P PVDF membrane (Millipore Corp). The membrane was blocked with 5% nonfat dry milk in TBST (0.5% Tween-20, 150 mM NaCl, 10 mM Tris-HCl, pH7.4) for 1 h at room temperature and then incubated with SAF61 mouse monoclonal antibody (Bertin Pharma), 3F4 mouse monoclonal anti-PrP antibody (BioLegend), IBL-N rabbit polyclonal anti-PrP antibodies (Immuno-Biological Laboratories), and anti-GAPDH antibody (Santa Cruz Biotechnology) overnight at 4 °C. After washed three times in TBST, the membrane was then incubated with HRP-conjugated anti-mouse IgG secondary antibody (GE Healthcare), anti-rabbit IgG antibody (GE Healthcare) in 1% nonfat dry milk-containing TBST for 1 h at room temperature. The immunoreactive signals were detected using Immobilon Western Chemiluminescent HRP substrate (Millipore) and a chemiluminescence image analyzer (LAS-4000 mini; Fujifilm Co). Densitometric analysis was performed using Image Gauge software (Fuji Film).

Pasiana A.D., Miyata H., Chida J., Hara H., Imamura M., Atarashi R, & Sakaguchi S. (2022). Central residues in prion protein PrPC are crucial for its conversion into the pathogenic isoform. The Journal of Biological Chemistry, 298(9), 102381.

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Quantifying RAMP Cell Surface Expression

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HEK-293S cells were transfected with GPCR and FLAG-RAMP/pcDNA3.1 at a 1:1 ratio. Cell surface expression of FLAG-RAMPs was determined as previously described 22 . Briefly, 48 hours posttransfection, cells were fixed with 3.7% paraformaldehyde and washed 3 times with PBS before and after incubation with mouse anti-FLAG M2 primary antibody (Sigma, diluted 1:2000 in PBS with 1% BSA) or HRP-conjugated anti-mouse IgG secondary antibody (GE Healthcare, diluted 1:4000 in PBS with 1% BSA). Cells were then incubated in o-phenylenediamine (OPD) solution (SigmaFast ophenylenediamine tablets, Sigma, dissolved in 20 ml distilled water) for 3-5 min, before termination of the reaction by addition to 100 μL 1 M sulphuric acid. Plates were read using a Mithras LB 940 multimode microplate reader at 492 nm. Data were normalised to cell surface expression for cells co-transfected with CLR and RAMP2 as 100% and cells transfected with pcDNA3.1 as 0%.

Harris M., Mackie D.I., Pawlak J., Carvalho S.d.E.S., Truong T.T., Safitri D., Yeung H.Y., Routledge S.J., Harper M.T., Al‐Zaid B., Soave M., Al‐Sabah S., Inoue A., Poyner D.R., Hill S.J., Briddon S.J., Sexton P.M., Wootten D., Zhao P., Caron K.M., & Ladds G. (2021). RAMPs regulate signalling bias and internalisation of the GIPR.

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