Goat anti rabbit igg hrp

Manufactured by Santa Cruz Biotechnology

Sourced in United States, Germany, United Kingdom, Canada

Goat anti-rabbit IgG-HRP is a secondary antibody conjugated with horseradish peroxidase (HRP). It is designed to detect and bind to rabbit immunoglobulin G (IgG) in various immunoassay techniques.

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423 protocols using goat anti rabbit igg hrp

Molecular Signaling Pathway Analysis

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Anti-MMP-9 polyclonal goat antibody, anti-β-actin monoclonal mouse antibody, goat anti-rabbit IgG/HRP, goat anti-mouse IgG/HRP, rabbit anti-goat IgG/HRP were purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Anti-Phospho-EGFR rabbit mAb, anti-EGFR rabbit mAb, anti-p44/42 MAP Kinase monoclonal rabbit antibody, anti-Phospho-p44/42 MAP Kinase monoclonal rabbit antibody, anti-AKT monoclonal rabbit antibody, anti-Phospho-AKT monoclonal mouse antibody, anti-Phospho-SAPK/JNK (Thr183/Tyr185) (81E11) Rabbit mAb, anti-SAPK/JNK rabbit mAb, anti-Phospho-p38 MAPK (Thr180/Tyr182) (12F8) Rabbit mAb and anti-p38 MAPK rabbit antibody were purchased from Cell Signaling Laboratories (Beverly, MA). PMA (Phorbol-12-myristate-13-acetate), specific inhibitors of PI3K [LY294002 (LY)], MAPK family [PD98059 (PD), mitogen-activated protein kinase kinase (MEK) inhibitor; SP600125 (SP), c-jun N-terminal kinase (JNK) inhibitor and SB203580 (SB), P38 MAPK inhibitor], gelatin and FITC-phalloidin were purchased from Sigma Chemical Co, (St.Louis, MO). PC, cholesterol and PEG4000 were purchased from Sigma Chemical Co, (St.Louis, MO); Honokiol was separated and purified by our laboratory and its purity and structure were analyzed and identified by high performance liquid chromatography and nuclear magnetic resonance [16 ].

Yang J., Pei H., Luo H., Fu A., Yang H., Hu J., Zhao C., Chai L., Chen X., Shao X., Wang C., Wu W., Wan L., Ye H., Qiu Q., Peng A., Wei Y., Yang L, & Chen L. (2016). Non-toxic dose of liposomal honokiol suppresses metastasis of hepatocellular carcinoma through destabilizing EGFR and inhibiting the downstream pathways. Oncotarget, 8(1), 915-932.

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Protein Expression Profiling via Immunoblotting

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To evaluate the expression of proteins we used the following antibodies: mouse monoclonal anti-STAT3 (1:500) (BD Transduction Laboratories, 610,189), rabbit polyclonal anti-phospho-STAT3 (1:500) (p-Tyr705, clone D3A7, Cell Signaling Technology, 9145), mouse monoclonal anti-p53 (1:100) (clone DO-1, Santa Cruz Biotechnology Inc., sc-126), mouse monoclonal anti-HSP90 (1:100) (Santa Cruz Biotechnology Inc., sc-69703), mouse monoclonal anti-p21 (1:100) (clone F-8, Santa Cruz Biotechnology Inc., sc-271610), mouse monoclonal anti-SREBP1 (1:100) (clone A-4, Santa Cruz Biotechnology Inc., sc-365513), mouse monoclonal anti-MVK (1:100) (clone D-3, Santa Cruz Biotechnology Inc., sc-390669). Mouse monoclonal anti-β-actin (1:10,000) (Novus Biological, NB600-501) and goat polyclonal anti-lamin B (1:100) (Santa Cruz Biotechnology Inc, sc-374015) were used as loading control. The goat anti-mouse IgG-Horseradish Peroxidase (Santa Cruz Biotechnology Inc., sc- 2005), goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology Inc., sc-2004) and rabbit anti-goat IgG-HRP (Santa Cruz Biotechnology Inc., sc-2768) were used as secondary antibodies. All the primary and secondary antibodies were diluted in PBS-0.1% Tween20 solution containing 3% of BSA (SERVA).

Romeo M.A., Gilardini Montani M.S., Benedetti R., Santarelli R., D'Orazi G, & Cirone M. (2020). STAT3 and mutp53 Engage a Positive Feedback Loop Involving HSP90 and the Mevalonate Pathway. Frontiers in Oncology, 10, 1102.

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Immunoprecipitation and Immunoblotting Assay

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Cell lysates were prepared in modified RIPA buffer and incubated overnight at 4°C, with specific antibodies. The immunocomplexes were isolated using protein-A Sepharose (Incospharm), resolved by SDS-PAGE, and transferred to nitrocellulose membrane. Immunoblotting was performed with various antibodies. Anti-ICP27, anti-Bax, anti-14-3-3θ, anti-cytochrome c, anti-COX IV, anti-α-tubulin, anti-β-actin, anti-acetylated lysine, anti-SIRT2, goat anti-rabbit IgG-HRP, rabbit anti-goat IgG-HRP, and goat anti-mouse IgG-HRP antibodies were purchased from Santa Cruz. Anti-Flag and anti-GST antibodies were purchased from Sigma-Aldrich.

Kim J.A., Kim J.C., Min J.S., Kang I., Oh J, & Ahn J.K. (2017). HSV-1 ICP27 induces apoptosis by promoting Bax translocation to mitochondria through interacting with 14-3-3θ. BMB Reports, 50(5), 257-262.

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Intestinal Tight Junction Protein Analysis

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Following the instructions provided with the total protein extraction kit (KGP200, Keygen Biotech, Nanjing, Jiangsu, China), the total protein was isolated. Equal quantities of intestinal mucosa proteins were isolated using a polyacrylamide gel before being moved onto a polyvinylidene difluoride (PVDF) membrane (Millipore, Bedford, MA, USA). These were then incubated with primary antibodies (goat polyclonal claudin-1 antibody, rabbit polyclonal ZO-1 antibody, and β-actin rabbit antibody) (Santa Cruz Biotechnology, CA, USA) for 12 h at 4°C. PVDF membranes were subsequently incubated with the secondary antibodies (goat anti-rabbit IgG-HRP and rabbit anti-goat IgG-HRP) (Santa Cruz Biotechnology, CA, USA) for 120 min at 25°C. Western blots were visualised using an enhanced chemiluminescence detection kit (Amersham, Arlington Heights, IL, USA) and photographed with Alpha Imager 2200 software (Alpha Innotech Corporation, CA, USA). β-actin reference proteins were equally distributed between the groups. The value of protein expression was determined as the densitometry ratio of tight junction proteins and β-actin.

Guan G., Wang H., Peng H, & Li G. (2016). Low Dosage of Chitosan Supplementation Improves Intestinal Permeability and Impairs Barrier Function in Mice. BioMed Research International, 2016, 4847296.

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Quantifying Cardiac Troponin I Phosphorylation

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The cTnI phosphorylation profile was quantified using Western blot by calculating the amount of phosphorylated cTnI relative to the total amount of cTnI.^{10 (link),34 (link)} The phosphorylated cTnI was detected using a rabbit polyclonal to cTnI (phospho S22 + S23, from abcam, cat. no.: ab58545) as primary antibody (1:1000) and goat antirabbit IgG-HRP (Santa Cruz Biotechnology, sc-2004) as secondary antibody (1:5000). The total cTnI was quantified using antibodies rabbit polyclonal lgG to troponin I (H170, from Santa Cruz Biotechnology, sc-15368) (1:1000) and goat antirabbit IgG-HRP (1:5000).

Cheng Y., Lindert S., Oxenford L., Tu A.Y., McCulloch A.D, & Regnier M. (2016). Effects of Cardiac Troponin I Mutation P83S on Contractile Properties and the Modulation by PKA-Mediated Phosphorylation. The journal of physical chemistry. B, 120(33), 8238-8253.

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Western Blot Analysis of Recombinant Proteins

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Whole‐cell lysates were prepared by boiling bacteria for 10 min in SDS–PAGE sample buffer (50 mM Tris, 0.75% (w/v) SDS, 10% (v/v) glycerol, 25 mM EDTA, 1% (v/v) β‐mercaptoethanol, 0.11 mM bromophenol blue) at a dilution of an OD₆₀₀ unit per 333 μl. A 20 μl aliquot of lysate was separated by electrophoresis (SDS–PAGE) on 12% polyacrylamide gels at 150 V for 75 min in SDS–PAGE buffer (25 mM Tris, 192 mM glycine, 0.1% (w/v) SDS, pH 8.5). Proteins were transferred to nitrocellulose membranes using the Trans‐Blot Turbo System (Bio‐Rad). Tagged proteins were detected using anti‐FLAG M2 antibody (Sigma, F3165, 1:1,000) and goat anti‐mouse IgG‐HRP (Bio‐Rad, 172‐1011, 1:5,000), or an anti‐V5 (D3H8Q) antibody (Cell Signaling Technology, #13202, 1:1,000) and goat anti‐rabbit IgG‐HRP (Santa Cruz Biotechnology, sc‐2004, 1:5,000). RecA was detected using anti‐RecA antibody (Abcam, ab63797, 1:5,000) and goat anti‐rabbit IgG‐HRP (Santa Cruz Biotechnology, sc‐2004, 1:5,000). Bands were detected by chemiluminescence (ECL, GE Healthcare), and band intensity was quantified using Photoshop CC (Lynda.com) as follows: a section of the blots including the relevant protein bands was generated and the total number of pixels within each box was measured, which correlates with the amount of protein.

Liu G., Beaton S.E., Grieve A.G., Evans R., Rogers M., Strisovsky K., Armstrong F.A., Freeman M., Exley R.M, & Tang C.M. (2020). Bacterial rhomboid proteases mediate quality control of orphan membrane proteins. The EMBO Journal, 39(10), e102922.

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Western Blot Antibody Protocol

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Anti NGLY1 antibody (Rabbit anti Human), Sigma-Aldrich, HPA036825 (Sigma-Aldrich, St Louis, MO, United States). Secondary antibody IgG-HRP Goat anti-Rabbit, Santa Cruz Biotechnology (Dallas, Texas United States; Cat. No. SC 2004), Anti β-Actin antibody, anti-Mouse monoclonal, cell-signaling technology (Danvers, MA, United States) Cat. No. 8H10D10, Secondary antibody, IgG-HRP Goat anti-Mouse, Invitrogen (Paisley, United Kingdom; Cat. No. A16072).

Mesika A., Nadav G., Shochat C., Kalfon L., Jackson K., Khalaileh A., Karasik D, & Falik-Zaccai T.C. (2022). NGLY1 Deficiency Zebrafish Model Manifests Abnormalities of the Nervous and Musculoskeletal Systems. Frontiers in Cell and Developmental Biology, 10, 902969.

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Testicular Protein Expression Analysis

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Protein extraction was performed on frozen testicular tissue by the Trizol precipitation method. Protein concentrations were evaluated using the Bradford’s test (Bio-Rad; USA). Equal amounts of each protein (30 μg) were loaded onto 12% SDS polyacrylamide gels (PAGE) which were then transferred to PVDF membrane (Bio-Rad; USA). Blocking solutions were prepared separately for each antibody. Nrf2 (1/500, Anti-rabbit, Abcam, USA), Slc7a11 (1/500, Anti-rabbit, Abcam, USA), Gpx-4(1/1000, Anti-rabbit, Abcam, USA), p-Jnk (1/1000, Anti-mouse, Abcam, USA) and β-Actin (1/500, Anti-rabbit, Santacruz, USA) were used as primary antibodies. Polyclonal IgG-HRP goat Anti-mouse (1/5000, Dako, Denmark) and IgG-HRP goat Anti-rabbit (1/16000, Santacruz, USA) were then used as secondary antibodies. Detection was performed using the GE Amersham ECL and Western Blotting kits (Amersham; GE Health care) and autoradiography [19 (link)]. Signal quantification was performed using Image J software.

Shaygannia E., Nasr-Esfahani M.H., Sotoodehnejadnematalahi F, & Parivar K. (2021). Is ferroptosis involved in ROS-induced testicular lesions in a varicocele rat model?. Basic and Clinical Andrology, 31, 10.

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Immunodetection with Goat Anti-IgG HRP

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HRP goat anti-mouse IgG (RRID: AB_631736; 1:8000; sc-2055; Santa Cruz, Heidelberg, Germany).
HRP goat anti-rabbit IgG (RRID: AB_631748; 1:8000; sc-2054; Santa Cruz, Heidelberg, Germany).

Arnold S., Kortland J., Maltseva D.V., Nersisyan S.A., Samatov T.R., Lezius S., Tonevitsky A.G., Milde-Langosch K., Wicklein D., Schumacher U, & Stürken C. (2021). Fra-2 overexpression upregulates pro-metastatic cell-adhesion molecules, promotes pulmonary metastasis, and reduces survival in a spontaneous xenograft model of human breast cancer. Journal of Cancer Research and Clinical Oncology, 148(6), 1525-1542.

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Protein Expression Profiling by Western Blot

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Equal amounts of total protein were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis on a 10% gel and transferred to a polyvinylidene fluoride membrane (Roche). The membranes were blocked with 5% milk/Tris-buffered saline plus Tween 20 (TBST) and incubated with primary antibodies against PARP-1 (sc-8007), NEK2 (sc-55601), β-actin (sc-47778) (all from Santa Cruz Biotechnology, Santa Cruz, CA, USA), pro-caspase-3 (#9662), β-catenin (#9562), phospho-ERK (#9101), ERK (#9102) (all from Cell Signaling, Danvers, MA, USA), and RPL17 (ab155781, Abcam, Cambridge, UK). HRP goat anti-mouse IgG, HRP goat anti-rabbit IgG, and HRP rabbit anti-goat IgG (Santa Cruz) were used as secondary antibodies. Immunoreactive bands were visualized using the LAS-3000 Imager (Fujifilm Corporation, Tokyo, Japan).

Ko M.J., Seo Y.R., Seo D., Park S.Y., Seo J.H., Jeon E.H., Kim S.W., Park K.U., Koo D.B., Kim S., Bae J.H., Song D.K., Cho C.H., Kim K.S, & Lee Y.H. (2022). RPL17 Promotes Colorectal Cancer Proliferation and Stemness through ERK and NEK2/β-catenin Signaling Pathways. Journal of Cancer, 13(8), 2570-2583.

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