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Horseradish peroxidase conjugated sheep anti mouse antibody

Manufactured by GE Healthcare
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Sourced in Italy, United States

Horseradish peroxidase-conjugated sheep anti-mouse antibody is a laboratory reagent used as a detection tool. It consists of a sheep-derived antibody that specifically binds to mouse antibodies, conjugated with the enzyme horseradish peroxidase. This product is designed for use in various immunoassay techniques.

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Lab products found in correlation

Amersham enhanced chemiluminescence substrate, by GE Healthcare (2 mentions) Enhanced chemiluminescence detection kit, by GE Healthcare (1 mentions) Horseradish peroxidase conjugated sheep anti rabbit antibody, by GE Healthcare (1 mentions) Immobilon p membrane, by Merck Group (1 mentions) Western lightning chemiluminescence reagent plus, by PerkinElmer (1 mentions) Fluorchem sp imaging system, by Bio-Techne (1 mentions) Geneticin g418, by Thermo Fisher Scientific (1 mentions) Ha 11 monoclonal affinity matrix, by Fortrea (1 mentions) Ecl detection kit, by Thermo Fisher Scientific (1 mentions) Flag tag (flag), by Merck Group (1 mentions) Gapdh, by Merck Group (1 mentions) Bmal1, by Santa Cruz Biotechnology (1 mentions) Histone 2b, by Abcam (1 mentions)

Close spelling variants of this product

Horseradish peroxidase (113 citations) Horseradish peroxidase-conjugated anti-mouse antibody (5 citations) Sheep anti-mouse antibody conjugated to horseradish peroxidase (HRP) (4 citations) Horseradish peroxidase-conjugated sheep anti-mouse or donkey anti-rabbit IgG antibody (2 citations) Horseradish peroxidase-conjugated sheep anti-mouse IgG antibody (2 citations)

6 protocols using horseradish peroxidase conjugated sheep anti mouse antibody

1

Western Blot Analysis of C/EBPβ Isoforms

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Cells were resuspended in lysis buffer (50 mM Tris pH 8.0, 150 mM NaCl, 1% Triton X-100 with protease inhibitors [2 ug/ml Leupeptin, 1 ug/ml Apoprotinin, 1 ug/ml Petpstatin a, 0.1 mM PMSF]) and 20 μg of whole cell extract subjected to SDS-PAGE. C/EBPβ LAP and LIP isoforms were detected using a rabbit polyclonal antibody (Santa Cruz Biotechnology, cat: sc-150) and a horseradish peroxidase-conjugated sheep anti-rabbit antibody (GE healthcare, cat: NA934). Β-tubulin was detected using a mouse monoclonal antibody (Sigma-Aldrich, cat: T4026) and a horseradish peroxidase-conjugated sheep anti-mouse antibody (GE healthcare, cat: NA931). All proteins were detected using an enhanced chemiluminescence detection kit (GE Healthcare).
Alvarez J., Gagnon D., Coutlée F, & Archambault J. (2019). Characterization of an HPV33 natural variant with enhanced transcriptional activity suggests a role for C/EBPβ in the regulation of the viral early promoter. Scientific Reports, 9, 5113.
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2

Immunoblotting of Bacterial RecA Protein

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Cells from 1 ml culture were pelleted, resuspended in 100 μl SDS lysis buffer (50 mM Tris–HCl pH 6.8, 2% SDS, 10% glycerol, 0.1% bromophenol blue, 5% 2-mercaptoethanol, 50 mM dithiothreitol), and boiled for 5 min. After boiling, suspension was pelleted and 15 μl of supernatant was run on a 10% acrylamide (37.5:1 acrylamide:bis) SDS-PAGE gel by standard methods. Protein was transferred to Immobilon-P membrane (Millipore) using a BioRad Mini-PROTEAN 3 Trans-Blot electrophoretic transfer cell. Blots were incubated at 4°C for 12–14 h with monoclonal mouse anti-RecA antibody diluted to 0.11 ng/ml in blocking buffer. Secondary labeling was done using horseradish peroxidase conjugated sheep anti-mouse antibody (GE Healthcare) diluted 1:1000 in blocking buffer. Blots were treated with Western Lightning Plus chemiluminescence reagent (Perkin Elmer) and imaged using the Alpha Innotech FluorChem SP imaging system.
Gataulin D.V., Carey J.N., Li J., Shah P., Grubb J.T, & Bishop D.K. (2018). The ATPase activity of E. coli RecA prevents accumulation of toxic complexes formed by erroneous binding to undamaged double stranded DNA. Nucleic Acids Research, 46(18), 9510-9523.
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3

Signaling Pathway Characterization with Synthetic PTH

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Human Nle8.18,Tyr34-PTH(1-34) was purchased from Bachem (Torrance, CA). Anti-p44/p42 MAP kinase (ERK1/2) and phospho-p44/42 MAP kinase (pERK1/2) (Thr202/Tyr204) polyclonal antibodies were purchased from Cell Signaling Technology (Beverly, MA). HA.11 ascites monoclonal antibody (mAb) and HA.11 monoclonal affinity matrix were obtained from Covance (Berkeley, CA). β-catenin polyclonal antibody was from Millipore (Billerica, MA). Horseradish peroxidase-conjugated goat anti-rabbit antibody was from Pierce Chemical (Rockford, IL). Horseradish peroxidase-conjugated sheep anti-mouse antibody was from GE Healthcare (Little Chalfont, Buckinghamshire, United Kingdom). Bisindolylmaleimide I (Bis I), H89 and PD98059 were from Calbiochem (San Diego, CA). Geneticin (G418) was obtained from Invitrogen (Carlsbad, CA). FuGENE6 was purchased from Roche Applied Science (Indianapolis, IN). All other reagents were from Sigma-Aldrich (St.Louis, MO).
Yang Y, & Wang B. (2015). Disruption of β-catenin binding to parathyroid hormone (PTH) receptor inhibits PTH-stimulated ERK1/2 activation. Biochemical and biophysical research communications, 464(1), 27-32.
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4

Immunoblotting Assay for Protein Detection

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The following primary antibodies were used: Mouse monoclonal antibodies against FLAG (Sigma-Aldrich; Merck KGaA; cat. no. F9291; 1:1,000), GAPDH (Chemicon; Merck KGaA; cat. no. SAB2108668; 1:5,000), GFP (Santa Cruz Biotechnology, Inc.; cat. no. (B-2):SC-9996; 1:1,000), HA (Santa Cruz Biotechnology, Inc.; cat. no. sc-7392; 1:500), BMAL1 (Santa Cruz Biotechnology, Inc.; cat. no. SC-365645; 1:500), Ub (Santa Cruz Biotechnology, Inc.; cat. no. sc-8017; 1:500); rabbit polyclonal antibodies against HRD1 (Abgent; cat. no. ap2184a; 1:500) and Histone 2B (Abcam; cat. no. ab52599; 1:500).
The following secondary antibodies were used: Horseradish peroxidase-conjugated sheep anti-mouse antibody (GE Healthcare; cat. no. NA931; 1:5,000) and anti-rabbit antibody (GE Healthcare; cat. no. NA934; 1:5,000) for 2 h at room temperature. The proteins were visualized with an ECL detection kit (Thermo Fisher Scientific, Inc.).
Guo D., Zhu Y., Wang H., Wang G., Wang C, & Ren H. (2020). E3 ubiquitin ligase HRD1 modulates the circadian clock through regulation of BMAL1 stability. Experimental and Therapeutic Medicine, 20(3), 2639-2648.
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5

Western Blot Analysis Protocol

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WB was performed as described [7 (link)], using equal amounts of protein (50 µg) for each sample and horseradish peroxidase-conjugated sheep anti-mouse antibody (GE Healthcare Life Science, Milan, Italy). WB were detected using the Amersham enhanced chemiluminescence substrate (GE Healthcare Life Science) following the manufacturer’s instructions. Densitometric analyses of WB were performed using the National Institutes of Health Image J analysis program (version 1.40. National Institutes of Health, Bethesda, MD).
Caruso Bavisotto C., Cipolla C., Graceffa G., Barone R., Bucchieri F., Bulone D., Cabibi D., Campanella C., Marino Gammazza A., Pitruzzella A., Porcasi R., San Biagio P.L., Tomasello G., Conway de Macario E., Macario A.J., Cappello F, & Rappa F. (2019). Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating Exosomes: Potential Use in Clinics. International Journal of Molecular Sciences, 20(18), 4496.
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6

Western Blot Analysis of EVs Hsp60

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The EVs Hsp60 was assessed by WB, using equal amounts of protein (50 µg) for each sample, anti-Hsp60 monoclonal antibody (mouse anti-Hsp60, LK1 clone, Sigma, St. Louis, MO, USA), and horseradish peroxidase-conjugated sheep anti-mouse antibody (GE Healthcare Life Science, Milan, Italy). WBs were detected using the Amersham enhanced chemiluminescence substrate (GE Healthcare Life Science, Marlborough, MA, USA), following the manufacturer's instructions. Densitometric analyses of WB were performed using the National Institutes of Health Image J analysis program (version 1.40. National Institutes of Health, Bethesda, MD, USA).
Graziano F., Iacopino D.G., Cammarata G., Scalia G., Campanella C., Giannone A.G., Porcasi R., Florena A.M., Macario E.C.d., Macario A.J.L., Nicoletti G.F., & Bavisotto C.C. (2021). The Triad Hsp60-miRNAs-Extracellular Vesicles in Brain Tumors: Assessing Its Components for Understanding Tumorigenesis and Monitoring Patients. Applied Sciences, 11(6), 2867-2867.
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