Hrp conjugated goat anti rabbit antibody

Manufactured by Thermo Fisher Scientific

Sourced in United States

The HRP-conjugated goat anti-rabbit antibody is a secondary antibody that binds to rabbit primary antibodies. It is conjugated with horseradish peroxidase (HRP), which can be used for various detection and quantification applications in research and diagnostic settings.

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Close spelling variants of this product

Goat anti-rabbit HRP (85 citations) HRP-conjugated goat anti-rabbit secondary antibody (39 citations) HRP-conjugated anti-rabbit antibody (31 citations) HRP-conjugated goat anti-rabbit IgG antibody (28 citations) HRP-conjugated goat anti-rabbit (21 citations) HRP-conjugated goat anti-rabbit IgG secondary antibody (18 citations) HRP-conjugated goat anti-rabbit IgG (H + L) secondary antibody (11 citations) Horseradish peroxidase (HRP)-conjugated goat anti-rabbit secondary antibody (9 citations) Horseradish peroxidase (HRP)-conjugated goat anti-rabbit antibody (8 citations) Goat anti-rabbit IgG (H+L) HRP-conjugated antibody (7 citations)

16 protocols using hrp conjugated goat anti rabbit antibody

Western Blot Analysis of Transcription Factors

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PC3 cells were harvested and nuclear extracts were separated by SDS-PAGE and transferred to a polyvinylidene difluoride membranes (Life Technologies). After incubation with 5% nonfat milk in TBST (10 mM Tris, pH 8.0, 150 mM NaCl, 0.5% Tween 20) for 1 hour, the membrane was washed once with TBST and incubated with antibodies against CREB (Millipore) (1:10000), HIF-1α (BD Biosciences) (1:500), or HIF-1β/ARNT (Cell Signaling) (1:1000) at room temperature for 1 h, or p300 (Santa Cruz) (1:200) at 4°C overnight. Membranes were washed and incubated with a 1:10000 dilution of HRP-conjugated goat anti-rabbit antibody (Life Technologies) for 1 hour. Blots were washed with TBST and developed with an ECL detection system (Thermo Scientific).

Tong Q., Weaver M.R., Kosmacek E.A., O’Connor B., Harmacek L., Venkataraman S, & Oberley-Deegan R.E. (2016). MnTE-2-PyP reduces prostate cancer growth and metastasis by suppressing p300 activity and p300/HIF-1/CREB binding to the promoter region of the PAI-1 gene. Free radical biology & medicine, 94, 185-194.

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Hepatic PAH Protein Quantification

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Western blotting was performed using an SDS-PAGE electrophoresis system. Homogenized liver samples were quantitated via Bradford assay, and 30-ug aliquots were resuspended in a reducing sample buffer, boiled and run on an 8% acrylamide reducing gel. Gels were blotted to PVDF membrane, and probed with PAH R400 polyclonal antibody (Bioworld Technology, #BS3704) at a dilution of 1:500. GAPDH (ThermoFisher #MA5-15738) was used as a loading control at a dilution of 1:50,000. Two secondary antibodies were used: an HRP-conjugated goat anti-rabbit antibody (Life Technologies #G21234) to bind to the PAH primary, and a goat anti-mouse antibody (Santa Cruz #sc-2055) for the GAPDH. Results were visualized on autoradiograph film using enhanced chemiluminenscence (SuperSignal West Pico Chemiluminescent).

Kaiser R.A., Carlson D.F., Allen K.L., Webster D.A., VanLith C.J., Nicolas C.T., Hillin L.G., Yu Y., Kaiser C.W., Wahoff W.R., Hickey R.D., Watson A.L., Winn S.R., Thöny B., Kern D.R., Harding C.O, & Lillegard J.B. (2021). Development of a porcine model of phenylketonuria with a humanized R408W mutation for gene editing. PLoS ONE, 16(1), e0245831.

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Western Blot Detection of Bacterial Proteins

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To detect LesA, anti-LesA antibody was diluted in PBS-M 1% (PBS plus 1% non-fat dried milk; 1:1000), followed by detection using HRP-conjugated goat anti-rabbit antibody (1:2000 for grapevines and 1:4000 for Xff samples) (Life Technologies, USA). Blocking and washing steps were performed with PBS-M 5% (PBS plus 5% non-fat dried milk) and PBS-T 0.1% (PBS plus 0.1% Tween 20), respectively. Developments were carried out using ECL Plus western blotting detection reagents (GE Life Sciences, USA). To detect MopB and EF-Tu in Xff samples, polyclonal antibodies (dilutions of 1:20,000 for MopB and 1:10,000 for EF-Tu) were used, followed by detection using HRP-conjugated goat anti-rabbit antibody (1:20,000). Blocking and washing steps were carried out as described for LesA. Blots were developed using SuperSignal West Dura Chemiluminescent Substrate (Thermo Scientific, USA). The anti-LesA polyclonal antibody was generated by immunizing rabbits with LesA immunogenic synthetic peptides (GeneScript, USA). The anti-MopB27 (link) and anti-EF-Tu polyclonal antibodies were kindly provided by George Bruening (Plant Pathology, UC Davis).

Nascimento R., Gouran H., Chakraborty S., Gillespie H.W., Almeida-Souza H.O., Tu A., Rao B.J., Feldstein P.A., Bruening G., Goulart L.R, & Dandekar A.M. (2016). The Type II Secreted Lipase/Esterase LesA is a Key Virulence Factor Required for Xylella fastidiosa Pathogenesis in Grapevines. Scientific Reports, 6, 18598.

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Granzyme B Expression in Immunotherapy

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All specimens were acquired from patients following informed consent and according to a Massachusetts General Hospital institutional review board-approved clinical protocol. Immunohistochemistry was performed on formalin-fixed paraffin embedded sections following standard antigen retrieval in citrate buffer. Granzyme B expression was detected with either an anti-Granzyme B antibody (ab5049, Abcam) or a biotinylated and humanized version of GZP (Biotin-βAla-GGG-IEPD-CHO) (hGZP). Bound antibody was detected with either HRP-conjugated goat anti-rabbit antibody and reacted with DAB substrate for IHC staining or AlexaFluor 488 goat anti-rabbit or AlexaFluor 594 goat anti-rabbit antibodies (Life Technologies) for immunofluorescent visualization. Bound peptide was detected with either HRP-conjugated streptavidin (Abcam) followed by reaction with DAB substrate or Oregon green conjugated-neutravidin (Life Technologies). Patient samples were grouped as either immunotherapy treated or non-treated, and treated specimens were further distinguished as responders or non-responders using modified RECIST criteria. Fluorescence quantification was performed using imageJ software (National Institutes of Health, Bethesda, MD).

Larimer B.M., Wehrenberg-Klee E., Dubois F., Mehta A., Kalomeris T., Flaherty K., Boland G, & Mahmood U. (2017). Granzyme B PET Imaging as a Predictive Biomarker of Immunotherapy Response. Cancer research, 77(9), 2318-2327.

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Antibody Characterization for HIV-1 p24 Detection

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Antibodies were obtained from the following sources: Mouse anti-p24 monoclonal antibody and rabbit anti-p24 polyclonal antibody from Abcam, Cambridge, United Kingdom (Cat numbers: ab9071 and ab63913, respectively); HRP-conjugated goat antirabbit antibody from Life Technologies, Carlsbad, CA (Cat numbers: 31460). Antibodies were used at a concentration of 0.5 μg/ml unless otherwise indicated. N-terminal biotinylated CPSF6(308–327) peptide (DRPPPPVLFPGQPFGQPPLG) and non-biotinylated CPSF6(313327) peptide (PVLFPGQPFGQPPLG) were synthesized by GenScript Corp. (Piscataway, NJ).

Xu J.P., Francis A.C., Meuser M.E., Mankowski M., Ptak R.G., Rashad A.A., Melikyan G.B, & Cocklin S. (2018). Exploring Modifications of an HIV-1 Capsid Inhibitor: Design, Synthesis, and Mechanism of Action. Journal of drug design and research, 5(2), 1070.

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Surface DAT Biotinylation and Quantification

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Surface DAT was assessed with sulfo-NHS-SS-biotin as described by us previously (Ng et al. 2014 (link)). Total lysates and biotinylated proteins were resolved on 8% Tris-Glycine mini gels and probed with polyclonal anti-DAT antibody against the N-terminal of DAT (Millipore, Billerica, MA, USA), followed by HRP-conjugated goat anti-rabbit antibody (Thermo scientific, Waltham, MA, USA). Polyclonal anti–β-actin antibody (Sigma-Aldrich, St. Louis, MO, USA) was used as an internal control for loading. The transporter signal was visualized using Thermo Scientific SuperSignal West Pico Chemiluminescent Substrate solution (Thermo Scientific, Waltham, MA, USA) and quantified using Image-J (from website of National Institute of Heath).

Zhen J, & Reith M.E. (2016). Impact of disruption of secondary binding site S2 on dopamine transporter function. Journal of neurochemistry, 138(5), 694-699.

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Temporal Protein Extraction and Quantification

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Total protein was extracted from seedlings grown under LD and harvested at 4h intervals from ZT0 to ZT20 on day 10. Whole protein extract was extracted using a buffer containing 50 mM Na-phosphate pH 7.4, 100 mM NaCl, 10% (v/v) glycerol, 5 mM EDTA, 1 mM DTT, 0.1% Triton X-100, 50 μM MG-132, 2mM Na₃VO₄, 2 mM NaF, and Pierce Protease Inhibitor Tablets, EDTA-free. Approximately 30 μg protein in each sample was run in 12% SDS-PAGE gels, and transferred to Nitrocellulose membranes (Bio-Rad). TCP4-3F6H proteins were detected by using a HRP-conjugated anti-FLAG antibody (A8592, Sigma), whereas histone H3 protein was detected by anti-histone H3 antibody (ab1791, Abcam), followed by a HRP-conjugated goat anti-rabbit antibody (Thermo Fisher Scientific). Immunoreactive proteins were visualized with SuperSignal West Pico Chesmiluminescent Substrate (Thermo Fisher Scientific) and Amersham ECL Select Western Blotting Detection Reagent (GE healthcare). For protein quantification, signals from immunoblottted membranes incubated in chemiluminescent detection reagents were imaged and quantified by a high sensitivity cooled CCD camera system (NightOWL, Berthold) and the IndiGo program (Berthold). Histone H3 was used for normalization of a protein in whole extract.

Kubota A., Ito S., Shim J.S., Johnson R.S., Song Y.H., Breton G., Goralogia G.S., Kwon M.S., Laboy Cintrón D., Koyama T., Ohme-Takagi M., Pruneda-Paz J.L., Kay S.A., MacCoss M.J, & Imaizumi T. (2017). TCP4-dependent induction of CONSTANS transcription requires GIGANTEA in photoperiodic flowering in Arabidopsis. PLoS Genetics, 13(6), e1006856.

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Western Blot Analysis of mCherry Protein

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Tissues (stomach and intestine) were lysed and homogenized in T-PER™ Tissue Protein Extraction Reagent (ThermoFisher Scientific, #78510) plus Protease Inhibitor (Sigma, #P8340). Protein concentration was determined using Pierce™ Coomassie (Bradford) Protein Assay Kit (ThermoFisher #23200). 100μg of lysate per well of each sample was loaded on Bolt™ 4-12% Bis-Tris Plus Gel (ThermoFisher, #NW04120BOX), along with SeeBlue® Plus2 Pre-Stained Standard (ThermoFisher Scientific, LC5925) and 0.1 μg mCherry protein (VWR #10190-818) as a positive control. After electrophoresis at 200V for 35 minutes, the gel was blotted on 0.45 μm pore size PVDF membrane using XCell II™ Blot Module (ThermoFisher Scientific). The membrane was then blocked with 3% nonfat milk in TBS (Sigma, T8793). Primary antibody, mCherry Antibody (ThermoFisher Scientific, #PA5-34974), was added to the blot at 1:1000 dilution in 3% nonfat milk in TBS, and incubated overnight at 4 °C. Following several washes with TBST (Sigma, T9039-10PAK), HRP-conjugated goat anti-rabbit antibody (ThermoFisher #31460) was added at 1:3000 dilution in TBST and incubated at room temperature for 1 h. mCherry protein was detected with 1-Step Ultra TMB-Blotting Solution (ThermoFisher Scientific, #37574).

Oz-Levi D., Olender T., Bar-Joseph I., Zhu Y., Marek-Yagel D., Barozzi I., Osterwalder M., Alkelai A., Ruzzo E.K., Han Y., Vos E.S., Reznik-Wolf H., Hartman C., Shamir R., Weiss B., Shapiro R., Pode-Shakked B., Tatarskyy P., Milgrom R., Schvimer M., Barshack I., Imai D.M., Coleman-Derr D., Dickel D.E., Nord A.S., Afzal V., van Bueren K.L., Barnes R.M., Black B.L., Mayhew C.N., Kuhar M.F., Pitstick A., Tekman M., Stanescu H.C., Wells J.M., Kleta R., de Laat W., Goldstein D.B., Pras E., Visel A., Lancet D., Anikster Y, & Pennacchio L.A. (2019). Noncoding Deletions Expose a Novel Gene Critical for Intestinal Function. Nature, 571(7763), 107-111.

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Immunoblot Analysis of Neuronal Signaling Pathways

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Total protein extraction from cultured hippocampal neurons and immunoblot analysis were performed as previously described [35 (link)]. The following primary antibodies were used: rabbit anti-pSer9-GSK-3β, anti-GSK-3β, rabbit anti-pThr172-AMPK, mouse anti-AMPKα1 (1:1000), Cell Signaling (Danvers, Massachusetts, USA); mouse anti-AMPKα1/α2 (1:1000), Abcam (Cambridge, Cambridgeshire UK); rabbit anti-PP2Ac (1:1000), Cell Signaling (Danvers, Massachusetts, USA); rabbit anti-LC3B (1:1000), (Danvers, Massachusetts, USA); rabbit anti-β-catenin (1:500), Santa Cruz (Dallas, Texas, USA); and mouse anti-α-actin (1:15000), Sigma (Frankfurt, Darmstadt, Germany). Primary antibodies were recognized using either horseradish peroxidase (HRP)-conjugated goat anti-rabbit antibody (1:7000, Thermo Scientific, Waltham, Massachusetts, USA) or HRP-conjugated rabbit anti-mouse antibody (1:7000, Thermo Scientific, Waltham, Massachusetts, USA). Secondary antibodies were detected via enhanced chemiluminescence using an ECL Plus WB detection system (Little Chalfont, Buckinghamshire, UK). Densitometric analysis was performed using ImageJ software (NIH, USA), and quantification was performed by normalization strategies proposed in 2013 [36 (link)].

Ríos J.A., Godoy J.A, & Inestrosa N.C. (2018). Wnt3a ligand facilitates autophagy in hippocampal neurons by modulating a novel GSK-3β-AMPK axis. Cell Communication and Signaling : CCS, 16, 15.

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Cell Harvest and Immunoblot Analysis

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Cells were harvested from 2 mL of the synchronous culture at the indicated time points by centrifugation. Cells were then resuspended in the SDS-PAGE sample buffer (50 mM Tris, pH 6.8, 6% 2-mercaptoethanol, 2% sodium dodecyl sulfate, 10% glycerol). Protein content was quantified with XL-Bradford (APROSCIENCE), and equal amounts of the total protein were subjected to immunoblot analysis. Immunoblotting was performed as described in Miyagishima et al.^{34 (link)} using 12% SDS-polyacrylamide gels. The anti-FtsZ, anti-nucleomorph H2A or anti-H3S10Ph^{35 (link), 36 (link)} antibodies was diluted to 1:1000. The primary antibodies were detected by HRP-conjugated goat anti-rabbit antibody (Thermo Scientific) diluted to 1:20,000.

Onuma R., Mishra N, & Miyagishima S.Y. (2017). Regulation of chloroplast and nucleomorph replication by the cell cycle in the cryptophyte Guillardia theta. Scientific Reports, 7, 2345.

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