Horseradish peroxidase conjugated protein a g

Manufactured by Thermo Fisher Scientific

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Horseradish peroxidase-conjugated Protein A/G is a lab equipment product. It is a conjugate of Protein A/G and horseradish peroxidase enzyme.

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Lab products found in correlation

Hrp conjugated mouse anti his mab, by Merck Group (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Power blotter xl, by Thermo Fisher Scientific (1 mentions) Precision plus protein kaleidoscope standard, by Bio-Rad (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Chemidoc mp imaging system, by Bio-Rad (1 mentions)

Spelling variants of this product

Horseradish peroxidase (215 citations) Protein A/G (47 citations) Horseradish peroxidase-conjugated protein A (6 citations) Peroxidase conjugated protein A/G (2 citations) Protein A–horseradish peroxidase (2 citations)

4 protocols using horseradish peroxidase conjugated protein a g

Brucella Antibody ELISA Protocol

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Anti-Brucella serum antibody was detected in the enzyme-linked immunosorbent assay (ELISA) according to the protocol described previously [1 (link)]. Briefly, commercially available inactivated B. abortus strain 125 (Kaketsuken Co., Kumamoto, Japan) and B. canis strain QE-13B (Kitasato
Institute Co., Tokyo, Japan) were solubilized and absorbed to the inner surface of each well (50 µg/50 µl/well) of a 96-well microtiter plate. The sera
diluted at 1:100 were used as the primary antibody, and horseradish peroxidase-conjugated Protein A/G (Thermo Fisher Scientific Inc., Waltham, MA, U.S.A.) diluted at 1:5,000 was used for
detection. The absorbance at 405 nm was measured and the arithmetic mean of triplicate absorbance data points with the standard deviation (SD) was calculated. Serum samples showing the
absorbance value higher than 0.2 against B. abortus, were regarded as positive, based on the values of serum samples from captive animals [1 (link)].

OHISHI K., ABE E., AMANO M., MIYAZAKI N., BOLTUNOV A., KATSUMATA E, & MARUYAMA T. (2018). Detection of serum antibodies to Brucella in Russian aquatic mammals. The Journal of Veterinary Medical Science, 80(11), 1696-1701.

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Recombinant Cap Protein Expression

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The MiCV HEB15 strain in this study was obtained previously by our team (GenBank accession No. KX268345) and used as the template in our current study. The gene encoding the Cap protein was amplified from the total viral DNA through PCR with the forward primer 5'-CGGGATCCGGCGGTTACAGATGGCG-3' and the reverse primer 5'-ACCTCGAGAGTTTGCTTTGGGA-3'. The amplified cap gene was subcloned into the BamHI and XhoI sites of the prokaryotic expression vector pET-32a in a frame with an amino terminal six-histidine tag. Recombinant plasmids designated as pET32a–cap were transformed into E. coli Rossetta cells to express His-tagged rCap. pET32a–cap was sequenced with commercial primers (T7 and S tag) by Comate Biotechnology Company (Changchun, China). rCap was purified using a Ni-Agarose 6× His-tagged protein purification kit (Qiagen, German) according to the manufacturer’s instructions. rCap was identified through Western blot by utilizing convalescent sera from minks infected with MiCV or healthy mink sera as primary antibodies. Horseradish peroxidase-conjugated protein A/G (Thermo Scientific) was set as a detection reagent. Similarly, rCap was also identified through Western blot analysis by applying HRP-conjugated mouse anti-His MAb (Sigma, USA) as antibodies.

Ge J., Cui X., Shi Y., Zhao L., Wei C., Wen S., Xia S, & Chen H. (2018). Development and application of an indirect enzyme-linked immunosorbent assay based on recombinant capsid protein for the detection of mink circovirus infection. BMC Veterinary Research, 14, 29.

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Western Blot Analysis of Brucella Strains

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Western blot analysis was performed according to the method described previously [36 (link)]. Proteins of the solubilized B. abortus strain
125 and B. canis strain QE-13B were respectively separated on a 10% polyacrylamide gel by SDS polyacrylamide gel electrophoresis (20 µg/lane) and blotted
onto a polyvinylidene difluoride membrane (Millipore Co., Billerica, MA, U.S.A.). Serum samples diluted to 1:100 were used as the first antibodies, and then horseradish peroxidase-conjugated
Protein-A/G (Thermo Fisher Scientific Inc.) diluted to 1:5,000 was used for detection.

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Western Blot Analysis of Protein Samples

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The PiCFA, BrCFA, and the synthesized I06 protein were separated by SDS-PAGE and transferred onto a nitrocellulose membrane (0.45 µm pore size; Bio-Rad, Hercules, CA, USA) using a Power Blotter XL semi-dry transferring machine (Invitrogen, Carlsbad, MA, USA) (setting: 1 Amp for 1 h). Molecular weight markers were run in parallel (Precision Plus Protein Kaleidoscope Standards, Bio-Rad, Hercules, CA, USA). The blotted membrane was incubated with gentle shaking in blocking buffer (5% skim milk in TBS-T buffer (20 mM Tris, 150 mM NaCl, 0.1% Tween 20; pH 7.4)) at 4 °C for overnight. The blotted membrane was incubated with each serum sample (prediluted at 1:1000 in the blocking buffer) (Table 2) at room temperature for 3 h. The membrane was washed with TBS-T 3 times (5 min each), incubated with the horseradish peroxidase-conjugated protein A/G (Thermo Scientific, Waltham, MA, USA) (1:50,000 dilution in blocking buffer) at room temperature for 2 h, and washed again with TBS-T 3 times and PBS 2 times. Finally, the probed membrane was incubated with colorimetric substrate solution (0.03% DAB, 0.05% CoCl₂, and 0.03% H₂O₂ in PBS) to generate WB signals. The processed membrane was photocopied using the ChemiDoc MP Imaging System (Bio-Rad, Hercules, CA, USA).

Rotchanapreeda T., Sae-Chew P., Lohnoo T., Yingyong W., Rujirawat T., Kumsang Y., Payattikul P., Jaturapaktrarak C., Intaramat A., Pathomsakulwong W., Yurayart C, & Krajaejun T. (2021). Immunological Cross-Reactivity of Proteins Extracted from the Oomycete Pythium insidiosum and the Fungus Basidiobolus ranarum Compromises the Detection Specificity of Immunodiagnostic Assays for Pythiosis. Journal of Fungi, 7(6), 474.

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