Anti-EphA4, anti-EphA7, and anti-TNFR1 antibodies were purchased from Santa Cruz Biotechnology (USA). Anti-caspase-8 and anti-cleaved caspase-3 antibodies were purchased from Cell Signaling Technology. FITC-conjugated goat anti-human IgG, rhodamine-conjugated anti-rabbit IgG, and FITC-conjugated anti-rabbit IgG antibodies were purchased from Invitrogen (USA). Horseradish peroxidase-conjugated anti-rat IgG and anti-rabbit IgG antibodies were acquired from Zymed (USA).
Horseradish peroxidase conjugated anti rat igg
Manufactured by Zymo Research
Sourced in United States
Horseradish peroxidase-conjugated anti-rat IgG is a laboratory reagent used in various immunoassay techniques. It is composed of anti-rat immunoglobulin G (IgG) antibodies that are conjugated to the enzyme horseradish peroxidase. This reagent can be used to detect and measure the presence of rat IgG in samples.
Automatically generated - may contain errors
Lab products found in correlation
Enhanced chemiluminescence system, by Roche (3 mentions)
Polyvinylidene difluoride membrane, by Cytiva (2 mentions)
Uvp biospectrum imaging system, by Analytik Jena (2 mentions)
Fitc conjugated anti rabbit igg, by Thermo Fisher Scientific (1 mentions)
Anti tnfr1, by Santa Cruz Biotechnology (1 mentions)
Anti cleaved caspase 3, by Cell Signaling Technology (1 mentions)
Anti epha4, by Santa Cruz Biotechnology (1 mentions)
Fitc conjugated goat anti human igg, by Thermo Fisher Scientific (1 mentions)
Anti caspase 8, by Cell Signaling Technology (1 mentions)
Anti rabbit igg, by Zymo Research (1 mentions)
4 protocols using horseradish peroxidase conjugated anti rat igg
1
Antibody Validation for Cell Signaling
2
Western Blotting of Thyroid Proteins
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For Western blotting, total cellular proteins were prepared from the thyroid tissues by the method described previously [27 (link)]. Fifty micrograms of sample protein was separated with 12% SDS/PAGE, and transferred to polyvinylidene difluoride membrane (Amersham, Buckinghamshire, UK). The membrane was blocked with 5% skimmed milk in NaCl/Tris-T (10 mM Tris-Cl, pH 8.0, 150 mM NaCl, and 0.5% Tween-20) at 4 °C overnight. It was rinsed three times (10 min each) with NaCl/Tris-T, and this was followed by 3 h of incubation with the same first antibodies that were used in immunohistochemical staining in the appropriate concentrations (IL-6, 1:500; COX-2, 1:500; NF-κB/p65, 1:500; β-actin, 1:3000, and IkBα, 1:1000) and 1 h of incubation with horseradish peroxidase-conjugated anti-rat IgG (Zymed Laboratories, San Francisco, CA, USA). Immunolabeling was detected with an enhanced chemiluminescence system (Roche, Mannheim, Germany), and visualized with the UVP Bio-spectrum Imaging System (UVP, Upland, CA, USA). β-actin was used as the internal quantitative control in densitometry analyses.
3
Western Blot Protein Analysis Protocol
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Total cellular proteins were prepared from the cells by the method described previously 17 (link). 30 μg sample proteins were separated with 12% SDS/PAGE, and transferred to a polyvinylidene difluoride membrance (Amersham, Buckinghamshire, UK). The membrance was blocked with 5% skimmed milk in NaCl/Tris-T (10 mM Tris/HCl, pH 8.0, 150 mM NaCl, and 0.5% Tween-20) at 4 °C overnight, incubated for 2 hours with the primary antibody and then with horseradish peroxidase-conjugated anti-rat IgG (Zymed Laboratories, San Francisco, CA, USA) for one hour. Immunolabeling was detected with an enhanced chemiluminescence system (Roche Inc., Mannheim, Germany), and visualized with the UVP Bio-spectrum Imaging System (UVP, Upland, CA, USA). β-actin was used as the internal quantitative control in densitometry analyses.
4
Quantitative Western Blot Analysis
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For Western blotting, total cellular proteins were prepared from the cells by the method described previously [23 (link)]. Fifty micrograms of sample protein was separated with 12% SDS/PAGE and transferred to a polyvinylidene difluoride membrane (Amersham, Buckinghamshire, UK). The membrane was blocked with 5% skimmed milk in NaCl/Tris-T (10 mM Tris/HCl, pH 8.0, 150 mM NaCl, and 0.5% Tween-20) at 4°C overnight. It was rinsed three times (10 min each) with NaCl/Tris-T, and this was followed by 2 h of incubation with the first antibodies in the appropriate concentrations (β-actin, 1 : 3000; SOD2, 1 : 4000; Cat, 1 : 3000; pro-caspase-9, 1 : 300; pro-caspase-3, 1 : 500; active-caspase-9, 1 : 300; active-caspase-3, 1 : 500; SULT1A1, 1: 1000; and SULT1C2, 1: 600) and 1 h of incubation with horseradish peroxidase-conjugated anti-rat IgG (Zymed Laboratories, San Francisco, CA, USA). Immunolabeling was detected with an enhanced chemiluminescence system (Roche, Mannheim, Germany) and visualized with the UVP BioSpectrum Imaging System (UVP, Upland, CA, USA). ImageJ was used to measure the density of bands (National Institutes of Health, Bethesda, MD). β-Actin was used as the internal quantitative control in densitometry analyses.
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