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Goat anti rabbit hrp

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Goat anti-rabbit HRP is a secondary antibody that is conjugated with the enzyme horseradish peroxidase (HRP). It is designed to detect and bind to rabbit primary antibodies in immunoassays and other applications.

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Lab products found in correlation

Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (2 mentions) Ripa buffer, by Thermo Fisher Scientific (2 mentions) G418 sulfate, by Corning (1 mentions) Mv1lu, by American Type Culture Collection (1 mentions) Ab34173, by Abcam (1 mentions) Ab190685, by Abcam (1 mentions) Ab137431, by Abcam (1 mentions) Ab124954, by Abcam (1 mentions) Sc 166570, by Santa Cruz Biotechnology (1 mentions) Beadblaster24r, by Benchmark Scientific (1 mentions) Image studio, by LI COR (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Rabbit anti vinculin, by Abcam (1 mentions) Polyjet, by SignaGen (1 mentions) Crl1729, by American Type Culture Collection (1 mentions) Phosphatase inhibitor cocktail 3, by Merck Group (1 mentions) Immobilon, by Merck Group (1 mentions) Alkaline phosphatase conjugated streptavidin, by Southern Biotech (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Pvdf membrane, by GE Healthcare (1 mentions)

Spelling variants of this product

HRP-labeled goat anti-rabbit IgG (5 citations) Horseradish peroxidase (HRP)-conjugated goat anti-mouse or goat anti-rabbit secondary antibodies (3 citations) HRP-conjugated goat anti-rabbit secondary antibody (3 citations) HRP-conjugated goat anti-mouse or goat anti-rabbit secondary antibodies (3 citations) Horseradish peroxidase (HRP)–conjugated goat anti-rabbit IgG (2 citations) Goat anti–rabbit IgG antibodies conjugated to HRP (2 citations) Rabbit anti-goat-HRP secondary antibody (2 citations) Goat anti-rabbit Ig-HRP (2 citations) Horseradish peroxidase (HRP)-conjugated goat anti-rabbit (2 citations) HRP)-conjugated goat anti-rabbit (2 citations)

11 protocols using goat anti rabbit hrp

1

Establishment and Characterization of Cell Lines

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293T, MDBK (B. taurus), OHH1.K (O. hemionus), OA3.Ts (O. aries), Ch1 Es (C. hircus), ST (S. scrofa), NZP-29 (O. dammah), MDCK (C. lupus familiaris), CRFK (F. catus), Mv1 Lu (N. vison), FoLu (U. cineroargenteus) and NZP-12 (C. obscurus) cells were obtained from ATCC (Manassas, VA). Ferret (M. putorius furo) MA139 cells were obtained from Dr. Janet Hartley (NIAID, Bethesda, MD). Each cell line was grown in DMEM (Thermo Fisher, Waltham, MA) supplemented with 1% penicillin and 100 μg/mL streptomycin and 10% fetal bovine serum.
The PCR 2.1 TOPO and pcDNA-V5-TOPO plasmids were purchased from Thermo Fisher. The pLNCX2 and pVSV-G plasmids were obtained from Clontech (Mountain View, CA). The pCMVgagpol plasmid which encodes the gagpol gene of the Moloney murine leukemia virus was obtained from Cell Biolabs (San Diego, CA). The pcDNA 3.1 plasmid with a C-terminal HA tag was a kind gift from Dr. Klaus Strebel (NIAID, Bethesda, MD).
Anti-HA and anti-V5 mouse monoclonal antibodies were obtained from Thermo Fisher. Anti-Beta-actin rabbit polyclonal antibody was obtained from Sigma-Aldrich (St. Louis, MO). Goat anti-rabbit-HRP and rabbit anti-mouse-HRP antibodies were purchased from Southern Biotech (Birmingham, AL). G418 sulfate was obtained from Corning (New York, NY).
Simpson J., Kozak C.A, & Boso G. (2022). Cross-species transmission of an ancient endogenous retrovirus and convergent co-option of its envelope gene in two mammalian orders. PLOS Genetics, 18(10), e1010458.
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2

Western Blot Analysis of Antioxidant Proteins

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Lung tissues were lysed in 1× RIPA buffer using a BeadBlaster24R (Benchmark Scientific, Sayreville, NJ, USA). Proteins were separated into 4–20% SDS-polyacrylamide gels and semi-dry-transferred to nitrocellulose membranes. Membranes were blocked for 1 h in 5% milk and probed overnight on a 4 °C rocker with the following primary antibodies: anti-Gclc (ab190685, Abcam, Cambridge, UK), anti-Gpx2 (ab137431, 1:2000, Abcam), anti-Gpx4 (sc-166570, 1:1000, Santa Cruz, Santa Cruz, CA, USA), NQO1 (ab34173, 1:2000, Abcam), Sepp1 (PA5-112707, 1:1000, Invitrogen, Waltham, MA, USA) or Txnrd11 (ab124954, 1:1000, Abcam). Membranes were then incubated at room temperature for 1 h in secondary antibody of goat anti-mouse HRP (horseradish peroxidase) (1031-05, 1:2000, Southern Biotech, Birmingham, AL, USA) or goat anti-rabbit HRP (4030-05, 1:2000, Southern Biotech). Membranes were developed using enhanced chemiluminescence (ECL) with ChemiDoc imaging and quantified by densitometry using Image Studio (Li-Cor, v 5.2.1, Lincoln, Nebraska). All quantifications for western blots were normalized to β-actin (8H10D10, 1:2000 Cell Signaling Technology, Danvers, MA, USA).
Bailey-Downs L.C., Sherlock L.G., Crossley M.N., Rivera Negron A., Pierce P.T., Wang S., Zhong H., Carter C., Burge K., Eckert J.V., Rogers L.K., Vitiello P.F, & Tipple T.E. (2024). Selenium Deficiency Exacerbates Hyperoxia-Induced Lung Injury in Newborn C3H/HeN Mice. Antioxidants, 13(4), 391.
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3

Protein Expression in HEK293T Cells

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HEK293T cells were plated and transfected after 24 hr at 70% confluency with PolyJet (SignaGen) or polyethylenimine (PEI). Cells were harvested after 24 hr (for expression studies) or 48 hr (for large-scale protein expression). For analysis of protein expression, cells were washed with phosphate buffered saline (PBS), pelleted at 1000 × g for 5 min at 4°C, and lysed by resuspension in lysis buffer (150 mM NaCl, 50 mM Tris-HCl pH 7.4, 1 mM EDTA, 0.5% NP-40, and protease inhibitor [Roche]) with rotation at 4°C for 30 min. Lysates were clarified by centrifugation at 21,000 × g for 10 min at 4°C. Lysate (20–33 μg) was used for SDS-PAGE and western blotting in Tris-buffered saline and 0.2% Tween 20 (TBST) using Strep-Tag II HRP (1:2500; EMD Millipore), rabbit anti-ORF68 (1:1000, Gardner and Glaunsinger, 2018 (link)), and rabbit anti-vinculin (1:1000; Abcam). Following incubation with primary antibodies, membranes were washed with TBST and imaged (for Strep-Tag II HRP) or incubated with goat anti-rabbit-HRP (1:5000; Southern Biotech).
Didychuk A.L., Gates S.N., Gardner M.R., Strong L.M., Martin A, & Glaunsinger B.A. (2021). A pentameric protein ring with novel architecture is required for herpesviral packaging. eLife, 10, e62261.
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4

Detecting MUC17 Protein via Antibodies

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MUC17-3TR was detected using an anti-MUC17C1 polyclonal antibody raised in rabbit against C-terminal peptide CSLRHIDPETKIRIQRPQVMTTSF or a monoclonal mouse anti-Myc antibody from 9E10.2 hybridoma cells (CRL-1729, ATCC). For immunoprecipitation, anti-MUC17C1 polyclonal antibody was used. Actin was detected with a primary mouse-anti-Actin C4 antibody (Millipore, MAB1501R). Bacteria were stained with goat anti-Lipid A (ThermoFisher, PA1-73178). Secondary antibodies for immunostaining and FACS were from ThermoFisher: goat anti-mouse Alexa Fluor 488 (A-11029), donkey anti-goat Alexa Fluor 488 (A-11055), donkey anti-mouse Alexa Fluor 647 (A-31571). Horseradish peroxidase (HRP) secondary antibodies for immunoblotting were from Southern Biotech: goat-anti-mouse HRP (1034-05), goat anti-rabbit HRP (4030-05).
Schneider H., Berger E., Dolan B., Martinez-Abad B., Arike L., Pelaseyed T, & Hansson G.C. (2019). The human transmembrane mucin MUC17 responds to TNFα by increased presentation at the plasma membrane. Biochemical Journal, 476(16), 2281-2295.
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5

ELISA for Trimer-Specific Antibodies

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To monitor trimer specific responses, ELISA microtiter plates were coated with trimeric C.1086 UFO-v2-RQH173 protein at 2μg/ml (in PBS), overnight at 4°C. The plates were blocked with 5% BSA + 4% Whey in PBS, RT, 1hr. The plates were incubated with serially diluted serum at RT, 2hrs, followed by incubation with goat anti-rabbit HRP (SouthernBiotech, catalog no 4010–05, dilution 1:4000), RT, 1hr. The plates were washed with PBS containing 0.05%Tween-20 (6 times) after each incubation step and developed as described above. To monitor C.1086 V3 responses, ELISA plates coated overnight with V3 peptide (res. 297–330, 1μg/ml in PBS) were used. gp70 V1V2 specific responses were monitored by using plates coated with 2μg/ml His-tag purified gp70 C.1086 V1V2 RQH (K166R/H170Q/H173) and RQY (K166R/H170Q/H173Y) (Zolla-Pazner et al., 2014 (link)) proteins. A450nm recorded from the developed ELISA plates were analyzed to measure end-point titre associated with the serum responses.
Sahoo A., Hodge E.A., LaBranche C.C., Styles T.M., Shen X., Cheedarla N., Shiferaw A., Ozorowski G., Lee W.H., Ward A.B., Tomaras G.D., Montefiori D.C., Irvine D.J., Lee K.K, & Amara R.R. (2022). Structure-guided changes at the V2 apex of HIV-1 clade C trimer enhance elicitation of autologous neutralizing and broad V1V2-scaffold antibodies. Cell reports, 38(9), 110436.
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6

PDGF-DD Stimulation of IL-2 Cultured NK Cells

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IL-2 cultured NK cells were serum-starved in RPMI 1640 medium for two hours at 37Ό prior to stimulation with 250 ng/ml PDGF-DD for the indicated time points. Following PDGF-DD stimulation, NK cells were placed on ice, washed once in ice cold PBS before resuspending in ice cold lysis buffer (50 mM Tris pH 8.0, 150 mM NaCl, 1% Triton X-100) containing 1 mM PMSF, 1 mM Na3VO4, leupeptin and apoprotinin (1 μg/ml each), and 1× phosphatase inhibitor cocktail 3 (Sigma Aldrich Cat. Number P0044) on ice for 10 mins. After centrifugation at 13,000 rpm for 15 mins at 4°C to pellet cellular debris, sample supernatants were removed and 4× SDS-PAGE loading buffer (200 mM Tris-HCl pH 6.8, 8% sodium dodecyl sulfate, 0.4% bromophenol blue, 40% glycerol and 400 mM dithiothreitol) added. Lysates were heated to 95°C for 10 minutes and run on a 4-12% bis-tris gel (Nupage). Proteins were transferred to nitrocellulose and blocked for 1 hour at RT in 5% BSA in TBS-T. Membranes were incubated in primary antibody overnight at 4°C. Membranes were subsequently washed and incubated in Goat anti-rabbit HRP (Southern Biotech) for 1 hour at RT, washed, and developed using SuperSignal West Pico Chemiluminescent Substrate.
Barrow A.D., Edeling M.A., Trifonov V., Luo J., Goyal P., Bohl B., Bando J., Kim A.H., Walker J., Andahazy M., Bugatti M., Melocchi L., Vermi W., Fremont D.H., Cox S., Cella M., Schmedt C, & Colonna M. (2017). Natural Killer cells control tumor growth by sensing a growth factor. Cell, 172(3), 534-548.e19.
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7

Western Blot Analysis of Exosome Proteins

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Western Blots were performed using 10% Bis-Tris gels and a mini gel system (Life Technologies). Equal amounts of exosome protein (20 µg) were loaded. NuPage MES SDS Running Buffer and NuPAGE MES Transfer Buffer were used according to manufacturer’s instructions. After electrophoresis and transfer to nitrocellulose paper, blocking was performed using 5% powdered milk solution/0.05% v/v Tween-20 (two hours) followed by the primary antibody incubation (1 hour minimum) followed by HRP secondary antibody. Antibodies used were as follows: Mouse anti-mouse MHCII H2-I/Adβ (5K43) (Santa Cruz); Rabbit anti-mouse IgE (Fc specific) (Acris); goat anti-rabbit HRP (Southern Biotech); Rabbit anti-mouse CD23 as described [18] (link); Rabbit anti-CD9 (polyclonal) (Sigma).
Martin R.K., Brooks K.B., Henningsson F., Heyman B, & Conrad D.H. (2014). Antigen Transfer from Exosomes to Dendritic Cells as an Explanation for the Immune Enhancement Seen by IgE Immune Complexes. PLoS ONE, 9(10), e110609.
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8

Western Blot Analysis of Muc17 Glycosylation

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Samples were separated on 5% or 10% polyacrylamide gels and transferred to PVDF membranes (Millipore) using semi-dry blotting procedures. For detection of Muc17, membranes were blocked in 5% (w/v) solution of powdered milk and incubated with primary antibodies, anti-Muc17C1 (1/1,000) or anti-Muc17S1 (1/1,000)26 (link) at 4 °C overnight. Secondary antibody incubation was conducted for 2 h at RT with goat-anti-rabbit HRP (1/10,000, Southern Biotech) and the membranes were developed using a chemiluminescent HRP substrate, Immobilon (Millipore). For detection of GalNAz labeled products, membranes were blocked with 3% (w/v) BSA solution, incubated with alkaline phosphatase conjugated streptavidin (1/5,000, Southern Biotech) for 2 h at RT and blots developed with NBT-BCIP color reagent (Promega).
Schneider H., Pelaseyed T., Svensson F, & Johansson M.E. (2018). Study of mucin turnover in the small intestine by in vivo labeling. Scientific Reports, 8, 5760.
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9

ELISA for Trimer-Specific Antibodies

Cited 1 time
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To monitor trimer specific responses, ELISA microtiter plates were coated with trimeric C.1086 UFO-v2-RQH173 protein at 2μg/ml (in PBS), overnight at 4°C. The plates were blocked with 5% BSA + 4% Whey in PBS, RT, 1hr. The plates were incubated with serially diluted serum at RT, 2hrs, followed by incubation with goat anti-rabbit HRP (SouthernBiotech, catalog no 4010–05, dilution 1:4000), RT, 1hr. The plates were washed with PBS containing 0.05%Tween-20 (6 times) after each incubation step and developed as described above. To monitor C.1086 V3 responses, ELISA plates coated overnight with V3 peptide (res. 297–330, 1μg/ml in PBS) were used. gp70 V1V2 specific responses were monitored by using plates coated with 2μg/ml His-tag purified gp70 C.1086 V1V2 RQH (K166R/H170Q/H173) and RQY (K166R/H170Q/H173Y) (Zolla-Pazner et al., 2014 (link)) proteins. A450nm recorded from the developed ELISA plates were analyzed to measure end-point titre associated with the serum responses.
Sahoo A., Hodge E.A., LaBranche C.C., Styles T.M., Shen X., Cheedarla N., Shiferaw A., Ozorowski G., Lee W.H., Ward A.B., Tomaras G.D., Montefiori D.C., Irvine D.J., Lee K.K, & Amara R.R. (2022). Structure-guided changes at the V2 apex of HIV-1 clade C trimer enhance elicitation of autologous neutralizing and broad V1V2-scaffold antibodies. Cell reports, 38(9), 110436.
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10

Western Blot Analysis of Human BCL2

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For the detection of human BCL2, we used wildtype mice as negative controls and the FL DoHH2 cell line as a positive control. Analyzed mouse samples included samples from transgenic (3′RR-BCL2) mice and from both homozygous (Igκ-BCL2/Igκ-BCL2) and hemizygous (Igκ-BCL2/+) Igκ knock-in mice.
A amount of 10 μg of total proteins were extracted (using 2× Laemmli buffer, Biorad, Catalog number # 161-0737, Composition: 65.8 mM Tris-HCl PH 6.8, 26.3% (w/v) glycerol, 2.1% SDS, 0.01% bromophenol blue) and denatured/reduced using β-mercaptoethanol (2.5% final) at 95 °C for 5 min.
After electrophoresis on a 12% polyacrylamide gel (Biorad, Hercules, CA, USA), proteins were transferred onto PVDF membranes (GE Healthcare). The human BCL2 protein was detected using the same mouse anti-human BCL2 antibody we use for flow cytometry, followed by an HRP-linked anti-mouse Ig antibody (eBioscience, San Diego, CA, USA), #18-8817-30).
Actin was stained as a housekeeping control protein with rabbit anti-actin antiserum (Sigma-Aldrich, Saint-Quentin, France A2066) followed by goat anti-rabbit-HRP (Southern Biotech, Birmingham, AL, USA, 4050-05).
Membranes were developed by enhanced chemiluminescence for a high-sensitivity detection system according to the manufacturer’s instructions (Bio-Rad, Marnes-ma-Coquette, France).
Zawil L., Marchiol T., Brauge B., Saintamand A., Carrion C., Dessauge E., Oblet C., Le Noir S., Mourcin F., Brousse M., Derouault P., Alizadeh M., Makhour Y.E., Monvoisin C., Saint-Vanne J., Léonard S., Durand-Panteix S., Tarte K, & Cogné M. (2022). Distinct B-Cell Specific Transcriptional Contexts of the BCL2 Oncogene Impact Pre-Malignant Development in Mouse Models. Cancers, 14(21), 5337.
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