Goat anti rabbit

Manufactured by Bio-Rad

Sourced in United States

Goat anti-rabbit is a secondary antibody produced in goats and designed to recognize and bind to rabbit primary antibodies. It can be used in various immunoassay techniques to detect and quantify target proteins or antigens in biological samples.

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Lab products found in correlation

Goat anti mouse, by Bio-Rad (25 mentions) Ripa buffer, by Thermo Fisher Scientific (4 mentions) Pvdf membrane, by Bio-Rad (4 mentions) Dc protein assay, by Bio-Rad (4 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Clarity western ecl substrate, by Bio-Rad (3 mentions) C600 imager, by Azure Biosystems (3 mentions) β actin, by Merck Group (3 mentions) Ab19487, by Abcam (3 mentions) Sc 32233, by Santa Cruz Biotechnology (3 mentions) Horseradish peroxidase conjugated secondary antibody, by Bio-Rad (2 mentions) Ab6160, by Abcam (2 mentions) Ab19247, by Abcam (2 mentions) Ab6877, by Abcam (2 mentions) Ab13970, by Abcam (2 mentions) Ab62478, by Abcam (2 mentions) Ta 09, by Zhongshan Golden Bridge Biotechnology (2 mentions) Sc 2048, by Santa Cruz Biotechnology (2 mentions) Sc 23950, by Santa Cruz Biotechnology (2 mentions) β actin, by Zhongshan Golden Bridge Biotechnology (2 mentions)

58 protocols using goat anti rabbit

Antibody Detection in Yeast Protein Study

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Antibodies used in this study are described herein. To detect ubiquitin, we used the polyclonal rabbit anti-Ubiquitin antibody (ab19247; Abcam, UK). The goat anti-Rsp5 (sc-26193; Santa Cruz Biotechnology, TX, USA) polyclonal antibody was used to detect presence of Rsp5. Yca1-GFP presence was detected using the chicken polyclonal to GFP antibody (ab13970; Abcam, UK). mCherry fused proteins were detected using mouse monoclonal anti-RFP antibody (MBL International, MA, USA). This antibody does not react with GFP. Tubulin levels were detected using monoclonal rat anti-tubulin antibody (ab6160; Abcam, USA). IgG levels were detected using the goat anti-rat IgG HRP conjugate antibody (STAR113P; Bio-Rad, CA, USA). Secondary HRP conjugated antibodies used to detect the primary antibodies in this study are as follows: goat anti-mouse (170–6516), goat anti-rabbit (170–6515), rabbit anti-goat (172–1034; Bio-Rad, CA, USA), and goat anti-chicken (ab6877; Abcam, UK).

Shrestha A., Brunette S., Stanford W.L, & Megeney L.A. (2019). The metacaspase Yca1 maintains proteostasis through multiple interactions with the ubiquitin system. Cell Discovery, 5, 6.

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Western Blot Analysis of Protein Targets

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All rats were deeply anesthetized with 10% chloral hydrate (0.3 g/kg, i.p.). The nitrocellulose membranes were incubated overnight at 4 °C with the primary antibody. The following commercially available antibodies were used as primary antibodies: ace-α-tubulin (1:10,000, sc23950, Santa Cruz Biotechnology, Dallas, Texas, USA), pCRMP2 T514 polyclonal antibody (1:1000, ab62478; Abcam, Waltham, MA, USA) guinea pig anti-TRPV-1 polyclonal antibody (1:1000, AB5566; MilliporeSigma, Burlington, MA, USA), GADPH (1:2000, TA-08, Zhongshan Golden Bridge Biotechnology, Guangdong, China), and β-actin (1:2000, TA-09, Zhongshan Golden Bridge Biotechnology, Guangdong, China). The blots were washed 3 times in Tris-buffered saline-Tween. The membranes were incubated with horseradish–conjugated secondary antibody (1:2000, goat anti-rabbit, rabbit anti-goat, rabbit anti-guinea pig, or goat anti-mouse; Bio-Rad, Hercules, CA, USA) for 1 h at room temperature, and developed with a chemiluminescence kit (sc-2048, Santa Cruz Biotechnology).

Chen L., Hu Q., Liu H., Zhao Y., Chan S.O, & Wang J. (2021). Nogo-A Induced Polymerization of Microtubule Is Involved in the Inflammatory Heat Hyperalgesia in Rat Dorsal Root Ganglion Neurons. International Journal of Molecular Sciences, 22(19), 10360.

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Western Blot Analysis of Cellular Proteins

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Cell lysates were collected in 2x-sample buffer containing 2-mercaptoethanol. Media was concentrated using 30k centrifugal devices (MCP030C41, Microsep^® Advance Centrifugal Devices Pall Corporation, Port Washington, NY) (UFC803024, Amicon^® Ultra-4 Centrifugal Filter Unit, Millipore Sigma) and mixed with NuPAGE^™ LDS 4x-Sample Buffer containing 2-mercaptoethanol. Tissue samples were lysed in RIPA buffer (#89900, Thermo-Fisher-Scientific, Waltham, MA) supplemented with 1×Halt^™ protease and phosphatase-inhibitor cocktail (78430, Thermo-Fisher-Scientific) and mixed with 2x-sample buffer. Samples were boiled for 5-minutes, loaded onto 4%-15% gradient polyacrylamide gels (4561084, Bio-Rad, Hercules, CA), and then transferred to PVDF membranes (#1620177, Bio-Rad). Blots were blocked using 5% milk in TBST. Primary antibodies were: 1:500 GPNMB (AF2550-SP R&D Biosystems, Minneapolis, MN), 1:4000 GAPDH (14C10, Cell Signaling), 1:1000 pS6 (S235/236, Cell Signaling), 1:1000 tS6 (5G10, Cell Signaling, Danvers, MA). Secondary antibodies were: 1:2000 Rabbit anti-goat (#1721034, Biorad) and 1:4000 Goat anti-rabbit (#1706515, Biorad). ECL Prime Western Blotting Detection Reagent (RPN2236, Cytiva, Marlborough, MA) or Clarity Western ECL Substrate (1705062, Bio-Rad) were used, and intensities determined using ImageJ.

Gibbons E., Taya M., Wu H., Lopa S.H., Moss J., Henske E.P., McCormack F.X, & Hammes S.R. (2024). GPNMB Promotes Tumor Growth and is a Biomarker for Lymphangioleiomyomatosis. Endocrine-related cancer, 31(6), e230312.

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Western Blot Analyses Across Multiple Pathways

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Western blots were performed as previously described [22 (link)]. All antibodies were from Cell Signaling except for ATF4 (Santa Cruz Biotechnology) and iNOS (BD Biosciences), and were used at a dilution of 1/1000 to 1/2000. The primary antibodies used were: 4E-BP1 (20 kD), phospho-4E-BP1 (20 kD), 5-LOX (78 kD), ACC1 (265 kD), phospho-ACC1 (265 kD), AKT (60 kD), phospho-AKT (60 kD), AMPK (62 kD), phospho-AMPK (62 kD), ATF4 (38 kD), cleaved caspase 1 (22 kD), COX2 (74 kD), eIF2α (38 kD), phospho-eIF2α (38 kD), ERK1/2 (44/42 kD), phospho-ERK1/2 (44/42 kD), HSP27 (27 kD), HSP40 (40 kD), HSP60 (60 kD), HSP70 (70 kD), HSP90 (90 kD), iNOS (130 kD), JNK1/2 (46/54 kD), phospho-JNK1/2 (46/54 kD), P38 (40 kD), phospho-P38 (40 kD), P62 (62 kD), NF-κB P65 (65 kD), RIG-1 (102 kD), S6 (32 kD), phospho-S6 (32 kD), S6 kinase (70 kD), phospho-S6 kinase (70 kD), and TNFα (17 kD). Horseradish peroxidase-conjugated secondary antibodies (goat anti-rabbit, goat anti-mouse, or rabbit anti-goat) (BioRad) diluted 1/5000) were used.

Kepchia D., Currais A., Dargusch R., Finley K., Schubert D, & Maher P. (2021). Geroprotective effects of Alzheimer’s disease drug candidates. Aging (Albany NY), 13(3), 3269-3289.

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Western Blot Analysis of aPKCζ in Parotid Glands

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Parotid glands from wild type and Prkcz^−/− mice were lysed in RIPA buffer with 5 mM sodium orthovanadate (Fisher Scientific, Waltham, MA), protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO) and 100 mM PMSF (Pierce/Thermo Scientific, Rockford, IL); then, samples were sonicated for 2 minutes and boiled for 10 min until homogeneous. 100 ug of protein from supernatant were loaded in 12% polyacrylamide gels. Transference was performed for 1 hour at 100 V using 0.45 μm Immobilon-P membranes (Millipore, Billerica, MA). After blocking in TBST buffer containing 2% BSA, membranes were incubated at 4 °C overnight in primary antibody at 1:1000 dilution. For detection, HRP conjugated secondary antibodies were applied to the membranes for 1 hour at room temperature and ECL substrate (Pierce/Thermo Scientific) was used following instructions by the manufacturer. The following antibodies were used: anti-total aPKCζ (Cell signaling, #9368), anti-PKCζ (phospho T560) antibody [EP2037AY] (Abcam, ab62372), Anti-Beta-tubulin (Thermo Scientific, #rb-9249-p), anti-Yap (D8H1X) XP Rabbit mAb (Cell Signaling, # 14074), anti-Rabbit-HRP (1:2000, Cell signaling, #7074 S), and Goat-anti-rabbit (1:10000, BioRad, #972-4446).

Chibly A.M., Wong W.Y., Pier M., Cheng H., Mu Y., Chen J., Ghosh S, & Limesand K.H. (2018). aPKCζ-dependent Repression of Yap is Necessary for Functional Restoration of Irradiated Salivary Glands with IGF-1. Scientific Reports, 8, 6347.

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Western Blot Analysis of Phosphorylated AKT

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Frozen tissues were homogenized for Western Blot analysis. Protein concentration was equalized and proteins were separated with SDS-PAGE and transferred to polyvinylidene difluoride membranes (GE Healthcare Life Sciences, Diegem, Belgium). Membranes were incubated overnight at 4°C with an antibody against pAKT (Ser473, Cell Signaling Technology, Leiden, Netherlands) or AKT (Cell Signaling Technology) in 5% bovine serum albumin. The following day, membranes were incubated with a secondary antibody containing horse-radish peroxidase (Goat-anti-rabbit: Bio-Rad, Veenendaal, Netherlands). To visualize the immune complex, membranes were treated with enhanced chemiluminescence reaction reagent and a picture was taken using Gel Doc XR+ Imaging system (Bio-Rad). Protein bands were analyzed using Image Lab 3.0.1 (Bio-Rad).

Gruben N., Funke A., Kloosterhuis N.J., Schreurs M., Sheedfar F., Havinga R., Houten S.M., Shiri-Sverdlov R., van de Sluis B., Kuivenhoven J.A., Koonen D.P, & Hofker M.H. (2015). Cholesterol-Induced Hepatic Inflammation Does Not Underlie the Predisposition to Insulin Resistance in Dyslipidemic Female LDL Receptor Knockout Mice. Journal of Diabetes Research, 2015, 956854.

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Immunoprecipitation and Western Blot Analysis

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Embryonic day E11.5 embryos were placed in lysis buffer (50 mM Tris-HCl at pH7.4, 150 mM NaCl, 1 mM EDTA, 1% Triton X-100, including 1 tablet protease inhibitor (Roche Complete) per 10 mls lysate) and incubated on ice for 10 min. Tissue debris was pelleted at 12,500 rpm for 10 min at 4°C, and the supernatant was incubated with primary antibodies overnight at 4°C. The lysates were incubated with Protein A or G Sepharose beads for 2 h, followed by washing of the immunoprecipitates three times with lysis buffer and elution of bound proteins in SDS–PAGE sampling buffer for 10 min at 100°C. Western blots were performed as described previously (Chen et al., 2005 (link)) using primary antibodies as listed. Secondary antibodies used were goat anti-rabbit (172–1019, Bio-Rad), and goat anti-mouse (172- 1011, Bio-Rad).

Harmacek L., Watkins-Chow D.E., Chen J., Jones K.L., Pavan W.J., Salbaum J.M, & Niswander L. (2014). A Unique Missense Allele of BAF155, a Core BAF Chromatin Remodeling Complex Protein, Causes Neural Tube Closure Defects in Mice. Developmental neurobiology, 74(5), 483-497.

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Detecting IGF System and Differentiation Markers

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In this study, the following antibodies were used to detect the IGF system: phospho-p44/42 MAPK (#4377), p44/42 MAPK (#9102), phospho-AKT (Ser473, #4051), and AKT (#9272) (Cell Signaling Technologies, Burlington, ON) and IGF-1Rα (N-20, sc-712) and IR-α (N-20, sc-710) (Santa Cruz Biotech., Santa Cruz, CA). For multipotency markers, we used OCT3/4 antibody (N-19, sc-8628) (Santa Cruz Biotech., Santa Cruz, CA) and SOX-2 (2683-1) (Epitomics, Burlington, ON). For the osteogenic differentiation markers, we used RUNX2 (#8486) (Cell Signaling Technologies, Burlington, ON), phospho-RUNX2 (PA5-12988) (Thermo Fisher Scientific, Burlington, ON), and OPN (K-20, sc-1059) (Santa Cruz Biotech., Santa Cruz, CA). For the loading control, we used pan-Actin Ab-5 (#MS-1295) (Thermo Fisher Scientific, Fremont, CA). The secondary antibodies used for immunoblotting were goat anti-rabbit (#170-6515), anti-mouse (#170-6516) HRP-conjugated antibodies (Bio-Rad Laboratories, Hercules, CA), or donkey anti-goat antibody (sc-2020) (Santa Cruz Biotech., Santa Cruz, CA).

Youssef A, & Han V.K. (2017). Regulation of Osteogenic Differentiation of Placental-Derived Mesenchymal Stem Cells by Insulin-Like Growth Factors and Low Oxygen Tension. Stem Cells International, 2017, 4576327.

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Western Blot Analysis of p63 Protein

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Cell and tissues extracts were resolved on SDS polyacrylamide gels and blotted onto Hybond P, PVDF membrane (GE Healtcare Chicago, IL, USA). Membranes were blocked with PBST 5% non-fat dry milk, incubated with primary antibodies for 2 h at room temperature, washed and hybridized with peroxidase conjugated secondary antibodies for 1 h at room temperature (goat anti-rabbit or goat anti-mouse, Biorad Hercules, CA, USA). Detection was performed with the ECL chemiluminescence kit (Perkin Elmer, Waltham, MA, USA) The antibodies used were: anti-p63α (D2K8X, Cell Signaling Technologies, Danvers, MA, USA; 1/500 dilution), anti-p63 (D9L7L, Cell Signaling Technologies, Danvers, MA, USA; 1/250), anti-GAPDH (clone 6C5, Merck Millipore, Darmstadt, Germany), anti-HA.11 (Biolegend, San Diego, CA, USA; 1/500), and anti-βactin (AC-15, Sigma, St. Louis, MO, USA; 1/5000).
Uncropped blots for westerns and other blots can be found in the Source data file.

Lena A.M., Rossi V., Osterburg S., Smirnov A., Osterburg C., Tuppi M., Cappello A., Amelio I., Dötsch V., De Felici M., Klinger F.G., Annicchiarico-Petruzzelli M., Valensise H., Melino G, & Candi E. (2021). The p63 C-terminus is essential for murine oocyte integrity. Nature Communications, 12, 383.

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Quantification of CB1 and SLP2 in Mouse Forebrain

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CD-1 mouse embryos at E13.5 (n=4), E16.5 (n=6) or new-born mice (n=6) were decapitated and forebrains were removed. Crudely purified mitochondrial fractions were prepared as described (Morozov et al., 2013 (link)). 20 μg protein samples were separated using electrophoresis at 210V in 4-12% NuPAGE Bis-Tris mini gels (Invitrogen, Carlsbad, CA, USA) and electrophoretically transferred to PVDF membranes (Bio-Rad Laboratories, Hercules, CA, USA). The membranes were subsequently immunoblotted with anti-CB₁-L31 (made-in-Guinea pig; Frontier Science Co. Ltd, Japan; 1:400) and anti-SLP2 (made-in-rabbit; 1:200; Santa Cruz Biotechnology Inc, Santa Cruz, CA, USA). The membranes were counterstained using corresponding donkey anti-Guinea pig (1:5000; Jackson Immunoresearch, West Grove, PA, USA) or goat anti-rabbit (1:3000; Bio-Rad Laboratories, Hercules, CA, USA) horse radish peroxidase conjugates, immersed in Clarity Western ECL Substrate (Bio-Rad Laboratories, Hercules, CA, USA) and exposed to X-ray films during recorded periods. Between the immunoblot procedures, membranes were rinsed and incubated in Restore Western Blot Stripping Buffer (Thermo Scientific; Rockford, IL, USA). Before repetitive immunoblots, the membranes were kept in Tris-saline buffer (pH 7.5) at +4°C for 4 days.

Morozov Y.M., Sun Y.Y., Kuan C.Y, & Rakic P. (2015). Alteration of SLP2-like Immunolabeling in Mitochondria Signifies Early Cellular Damage in Developing and Adult Mouse Brain. The European journal of neuroscience, 43(2), 245-257.

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