Hrp conjugated anti mouse igg

Manufactured by Bio-Rad

Sourced in United States

HRP-conjugated anti-mouse IgG is a secondary antibody conjugated with the enzyme Horseradish Peroxidase (HRP). This product is designed for use in immunodetection techniques that require a labeled secondary antibody, such as Western blotting, ELISA, and immunohistochemistry.

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Lab products found in correlation

Hrp conjugated anti rabbit igg, by Bio-Rad (3 mentions) Chemidoc xrs system, by Bio-Rad (3 mentions) Pvdf membrane, by Merck Group (2 mentions) Alexa fluor 488 conjugated goat anti rabbit igg, by Thermo Fisher Scientific (2 mentions) Alexa fluor 594 conjugated goat anti mouse igg, by Thermo Fisher Scientific (2 mentions) Gapdh, by Proteintech (2 mentions) Hrp conjugated protein g, by Bio-Rad (2 mentions) Mouse anti β actin, by Santa Cruz Biotechnology (2 mentions) Sds page, by Bio-Rad (1 mentions) Pvdf blotting membrane, by GE Healthcare (1 mentions) Reactive oxygen species assay kit, by Nanjing Jiancheng (1 mentions) Cox 4, by Abcam (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by neoFroxx (1 mentions) Bcl 2, by Cell Signaling Technology (1 mentions) Complex 1 enzyme activity microplate assay kit, by Abcam (1 mentions) Ubiquitin, by Santa Cruz Biotechnology (1 mentions) Bcl2 associated x (bax), by Proteintech (1 mentions) Beclin 1, by Proteintech (1 mentions) 0.45 μm membrane, by Merck Group (1 mentions) Clarity western ecl substrate, by Bio-Rad (1 mentions)

14 protocols using hrp conjugated anti mouse igg

Cell Lysis and Western Blotting

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Cell lysates were prepared with lysis buffer containing 2 mM N-ethylmaleimide (NEM) [10 (link)]. The cell lysates were mixed with 2x sample buffer with or without 10 % 2-mercaptoethanol (2-ME) (Wako), and were subjected to SDS-PAGE (BioRad) with or without 2-ME. The fractionated proteins were transferred onto a PVDF membrane (Millipore). The membrane was treated with an appropriate primary antibody, and then with HRP-conjugated anti-mouse IgG, anti-goat IgG, or protein G (BioRad).

Kubo Y., Izumida M., Yashima Y., Yoshii-Kamiyama H., Tanaka Y., Yasui K., Hayashi H, & Matsuyama T. (2016). Gamma-interferon-inducible, lysosome/endosome-localized thiolreductase, GILT, has anti-retroviral activity and its expression is counteracted by HIV-1. Oncotarget, 7(44), 71255-71273.

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Western Blot Analysis of gp39 Protein

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The protein samples were fractionated by SDS-PAGE using 14 % polyacrylamide gels. Then the gels were transferred onto polyvinylidene difluoride (PVDF) blotting membranes (GE Healthcare Life Science, Freiburg, Germany) under semi-dry conditions. The blocking step was carried out in 1 × Roti-Block solution (Carl Roth GmbH and Co, Karlsruhe, Germany) for 1 h at room temperature with shaking. After several washes with Tris-buffered saline (TBS) containing 0.1 % Tween 20 (TBS-T), membranes were incubated per night with gp39 protein-specific polyclonal antibody (2 μg/ml in TBS-T, an in-house produced murine antibody from the Institute of Biotechnology, Vilnius University). After washing with TBS-T, the membranes were incubated for 2 h with HRP-conjugated anti-mouse IgG (1:3000 in TBS-T, BioRad). After several washes with TBS-T and the final wash with TBS, the detection based on the HRP reaction was carried out by adding 4-chloro-1-naphthol and H₂O₂ (Fluka, Buchs, Switzerland).

Avižinienė A., Dalgėdienė I., Armalytė J, & Petraitytė-Burneikienė R. (2024). Immunogenicity of novel vB_EcoS_NBD2 bacteriophage-originated nanotubes as a carrier for peptide-based vaccines. Virus Research, 345, 199370.

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Comprehensive Neurodegenerative Protein Analysis

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The following antibodies and reagents were used: pα-Syn (Ser129, Biolegend, 825701), pα-Syn (Ser129, Cell Signaling Technology, 23706s), MAP2 (Thermo Fisher Scientific, SF254293), COX IV (Abcam, ab16056), ATG5 (Proteintech, 10181-2-AP), Beclin1 (Proteintech, 11306-1-AP), LC3 (Cell Signaling Technology, 12741), Bcl2 (Cell Signaling Technology, 3498S), Bax (Proteintech, 50599-2-Ig), GAPDH (Proteintech, 60004-1-Ig), TH (Sigma-Aldrich, AB152), Ubiquitin (Santa Cruz Biotechnology, sc-8017), Iba-1 (Wako, 019-19741), Alexa Fluor 594-conjugated goat anti-mouse IgG (Invitrogen, A-11005), Alexa Fluor 488-conjugated goat anti-rabbit IgG (Invitrogen, A-11012), DAPI (Biofroxx, EZ3412B205), HRP-conjugated anti-mouse IgG (BIO-RAD, 170-6516), HRP-conjugated anti-rabbit IgG (BIO-RAD, 170-6515), Complex I Enzyme Activity Microplate Assay Kit (Abcam, ab109721), and Reactive Oxygen Species Assay Kit (Nanjing Jiancheng Bioengineering Institute, E004-1-1).

Yuan X., Yang Y., Xia D., Meng L., He M., Liu C, & Zhang Z. (2022). Silica Nanoparticles Promote α-Synuclein Aggregation and Parkinson’s Disease Pathology. Frontiers in Neuroscience, 15, 807988.

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Viral Protein Detection in Cell Cultures

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Culture supernatants of the vector-producing cells were filtered through a 0.45-μm membrane (Millipore), and centrifuged at 16,114 × g through 20% sucrose for 5 h to collect virion pellets. Cell lysates and virion pellets were subjected to SDS polyacrylamide gel electrophoresis with or without Phos-tag reagent (Kinoshita et al., 2006 (link)), and proteins were transferred onto a PVDF membrane. Membranes treated with rabbit anti-HIV-1 p24 (BioAcademia or ZeptoMetrix), sheep anti-HIV-1 gp120 (provided by Dr. T. Murakami), or rabbit anti-ezrin antibody (Santa Cruz Biotechnology) then were treated with HRP-conjugated protein G (BioRad) to detect the proteins. Membranes treated with mouse anti-VSV-G epitope (Sigma-Aldrich) and mouse anti-actin antibodies (Santa Cruz Biotechnology) were treated with HRP-conjugated anti-mouse IgG (BioRad) as the secondary antibody. Antigen proteins were visualized using the Clarity Western ECL substrate (BioRad).

Kamiyama H., Izumida M., Umemura Y., Hayashi H., Matsuyama T, & Kubo Y. (2018). Role of Ezrin Phosphorylation in HIV-1 Replication. Frontiers in Microbiology, 9, 1912.

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Antibody Panel for Immunophenotyping

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We used rabbit anti-ESAT-6 antibody (Abcam, Cambridge, MA), mouse anti-His_6X antibody (Sigma-Aldrich, St. Louis MA), anti-FLAG antibody (Sigma-Aldrich, St. Louis MA), HRP conjugated anti-mouse IgG (Bio-rad, Hercules, CA), anti-rabbit FITC conjugated secondary antibody (Jackson-ImmunoResearch, West Grove, PA) and anti-mouse Texas Red secondary antibody (Jackson-ImmunoResearch, West Grove, PA) for in vitro studies. For in vivo studies, anti-CD4 (clone: GK1.5)-FITC, -PerCP-Cy5 or -APC, anti-CD8 (clone: 53–6.7)-FITC, -PerCP-Cy5 or -APC, anti-CD44 (clone: IM7)-APC, anti-Brdu (clone: Bu20a)-PE, anti-CD11b (clone: M1/70)-APC, anti-CD11c (clone: N418)-APC, 7AAD, anti-IFN-γ (clone: XMG1.2)-APC, anti-IL-17 (clone: TC11-18H10.1)-PE, anti-IL-4 (clone: 11B11)-PE, anti-IL-6 (clone: MPS-20 F3)-PE, anti-IL-12 (clone: C15.6)-PE, anti-IL-22 (clone: Poly5164)-PE, anti-IL-10 (clone: JES5-16E3)-PE, anti-IL-9 (clone: MH9A4)-PE, anti-TNF-α (clone: MP6-XT22)-PE, (all from Biolegend, USA) and anti-CD69 (clone: H1.2 F3)-PE (from eBiosciences, USA) were used.

Samuchiwal S.K., Tousif S., Singh D.K., Kumar A., Ghosh A., Bhalla K., Prakash P., Kumar S., Bhattacharyya M., Moodley P., Das G, & Ranganathan A. (2014). A peptide fragment from the human COX3 protein disrupts association of Mycobacterium tuberculosis virulence proteins ESAT-6 and CFP10, inhibits mycobacterial growth and mounts protective immune response. BMC Infectious Diseases, 14, 355.

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Splenic NK Cell Subset Isolation and Analysis

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Splenic NK cells were purified from Bach2^Flag animals by total NK cell enrichment followed by FACS, as described above. CD49b⁺ NK cells were sorted into three subset populations according to expression of the following surface markers: iNK (CD27⁺ CD11b⁻), mNK1 (CD27⁺ CD11b⁺), or mNK2 (CD27⁻ CD11b⁺). Samples were lysed in Pierce RIPA Buffer containing cOmplete Mini protease inhibitor cocktail (Roche) and PhosSTOP phosphatase inhibitor cocktail (Roche). The blots were probed with the primary antibodies anti-Flag M2 (Sigma-Aldrich) and an anti–β-actin control (Sigma-Aldrich). The secondary antibody was HRP-conjugated anti-mouse IgG (Bio-Rad). Blots were imaged and resultant bands quantified using ImageJ.

Imianowski C.J., Whiteside S.K., Lozano T., Evans A.C., Benson J.D., Courreges C.J., Sadiyah F., Lau C.M., Zandhuis N.D., Grant F.M., Schuijs M.J., Vardaka P., Kuo P., Soilleux E.J., Yang J., Sun J.C., Kurosaki T., Okkenhaug K., Halim T.Y, & Roychoudhuri R. (2022). BACH2 restricts NK cell maturation and function, limiting immunity to cancer metastasis. The Journal of Experimental Medicine, 219(12), e20211476.

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Western Blot Analysis of DLK, JUN, and pJUN

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Experiments were performed as previously described (Fernandes et al., 2012 (link)). Approximately 30μg of protein was loaded in each lane (Nanodrop was used to quantify protein concentrations from retinal protein lysates). Proteins of interest were detected with the following primary antibodies: rabbit anti-DLK (1:300, (Hirai et al., 2002 (link))), rabbit anti-JUN (Cell Signaling, 9165S; 1:500), rabbit anti-pJUN (Cell Signaling, 9261S, 1:500), mouse anti-GAPDH, Calbiochem CB1001, 1:3000), and mouse anti-α-tubulin (Sigma, T5168, 1:1000). After overnight incubation with primary antibody at 4C, membranes were washed and then incubated with secondary antibodies: HRP-conjugated anti-rabbit IgG (Biorad Laboratories, 170-6515, 1:10,000) HRP-conjugated anti-mouse IgG (Biorad Laboratories, 170-6516, 1:10,000) for 1 hour at room temperature. Immunoreactive bands were detected using an enhanced chemiluminescence reagent kit (Supersignal West Dura Extended Substrate, Pierce, 34075 or Immun-star, BioRad 170-5070). Densitometric analysis was used to determine the relative abundance of proteins using Quantity One software (BioRad). Amounts of protein were normalized to the loading control and then expressed relative to appropriate control group for the experiment.

Fernandes K.A., Harder J.M., John S.W., Shrager P, & Libby R.T. (2014). DLK-dependent signaling is important for somal but not axonal degeneration of retinal ganglion cells following axonal injury. Neurobiology of disease, 69, 108-116.

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Protein Expression Analysis in Chicken Tissues

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Total proteins from feather pulp and homogenized muscle (pectoralis major) from wild-type and hCST3 transgenic chickens were extracted with 1× radioimmunoprecipitation (RIPA) lysis buffer (Rockland, Limerick, PA, USA). These samples separated on a 15% polyacrylamide gel followed by transfer to a nitrocellulose membrane. Additionally, we analysed hCST3 proteins after purification from muscle and egg white. The primary antibodies used were mouse anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) or anti-human cystatin C (Abcam, Cambridge, UK). HRP-conjugated anti-mouse IgG or anti-rabbit IgG (Bio-Rad, Hercules, CA, USA) were used as secondary antibodies. The blots were treated with ECL substrate solutions and exposed in a ChemiDoc XRS System (Bio-Rad, Hercules, CA, USA) to detect chemiluminescence.

Kim S.W., Lee J.H., Han J.S., Shin S.P, & Park T.S. (2021). piggyBac Transposition and the Expression of Human Cystatin C in Transgenic Chickens. Animals : an Open Access Journal from MDPI, 11(6), 1554.

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Protein Expression Analysis Protocol

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Total protein was extracted with 1× radioimmunoprecipitation lysis buffer and separated on a 10% polyacrylamide gel followed by transfer to a nitrocellulose membrane (Bio-Rad, USA). The primary antibodies used were mouse anti-β-actin (Santa Cruz Biotechnology, Dallas, TX, USA), anti-MyoD (Santa Cruz Biotechnology, USA), anti-desmin (Novus Biologicals, Littleton, CO, USA), and anti-MF20 (Developmental Studies Hybridoma Bank, Iowa City, IA, USA). HRP-conjugated anti-mouse IgG or anti-rabbit IgG (Bio-Rad, USA) were used as secondary antibodies. The blots were treated with enhanced chemiluminescence substrate solutions and exposed in a ChemiDoc XRS System (Bio-Rad, USA) to detect chemiluminescence.

Kim S.W., Lee J.H., Park B.C, & Park T.S. (2016). Myotube differentiation in clustered regularly interspaced short palindromic repeat/Cas9-mediated MyoD knockout quail myoblast cells. Asian-Australasian Journal of Animal Sciences, 30(7), 1029-1036.

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Lentivirus production and analysis

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COS7, Vero, or 293T cells were transfected as indicated or treated with concanamycin A (CMA) or MG-132 (Sigma-Aldrich). Cells were transfected with the HIV-1 vector construction plasmids. The transfected cells were cultured for 24 h, and washed with medium to remove the transfection reagent and plasmids. The cells were additionally cultured for 24 h, and cell lysates and culture supernatants were prepared from the cells. Cell lysates were subjected to SDS polyacrylamide gel electrophoresis (BioRad). Proteins were transferred to a PVDF membrane (Millipore). The membrane was treated with indicated first antibodies. As the first antibodies, rabbit anti-HIV-1 p24 (BioAcademia), goat anti-HIV-1 gp120 (Fitzgerald), goat anti-MLV p30 (ViroMed Biosafety Laboratories), mouse anti-actin (Santa Cruz), mouse anti-VSV-G (Sigma-Aldrich), and goat anti-ezrin (Santa Cruz) antibodies were used. When mouse antibodies were used as the first antibody, HRP-conjugated anti-mouse IgG (BioRad) was used. When the membrane was treated with a rabbit or goat antibody, HRP-conjugated protein G (BioRad) was used. Intensities of protein bands were measured by the ImageJ software.

Izumida M., Togawa K., Hayashi H., Matsuyama T, & Kubo Y. (2020). Production of Vesicular Stomatitis Virus Glycoprotein-Pseudotyped Lentiviral Vector Is Enhanced by Ezrin Silencing. Frontiers in Bioengineering and Biotechnology, 8, 368.

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