Irdye 800 conjugated goat anti rabbit

Manufactured by LI COR

Sourced in United States

The IRDye 800-conjugated goat anti-rabbit is a secondary antibody used for detection and visualization in various applications. It is composed of a goat-derived antibody that specifically binds to rabbit primary antibodies, with the IRDye 800 fluorescent label attached. This product can be used to amplify and detect the signal from rabbit primary antibodies in techniques such as Western blotting, immunohistochemistry, and immunocytochemistry.

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Lab products found in correlation

Irdye 680 conjugated goat anti mouse, by LI COR (7 mentions) Nitrocellulose membrane, by Bio-Rad (4 mentions) Odyssey blocking buffer, by LI COR (4 mentions) Odyssey infrared imaging system, by LI COR (3 mentions) Odyssey infrared imager, by LI COR (2 mentions) Odyssey imaging system, by LI COR (2 mentions) Anti β actin, by Merck Group (1 mentions) Odyssey fc imaging system, by LI COR (1 mentions) Na k atpase, by Abcam (1 mentions) β actin, by Abcam (1 mentions) Laminin b, by Santa Cruz Biotechnology (1 mentions) Nupage 4 12 bis tris mini gel, by Thermo Fisher Scientific (1 mentions) Odyssey blocking buffer, by Merck Group (1 mentions) Irdye680 conjugated donkey anti mouse, by LI COR (1 mentions) Anti beta 3 tubulin, by Promega (1 mentions) Gs 800tm calibrated, by Bio-Rad (1 mentions) Pierce ecl western blot substrate, by Thermo Fisher Scientific (1 mentions) Gradi gel gradient analysis kit, by Elpis Biotech (1 mentions) Mouse monoclonal anti β actin, by Merck Group (1 mentions) Immobilon fl membrane, by Merck Group (1 mentions)

Close spelling variants of this product

IRDye 800 (256 citations) Goat anti-rabbit IRDye 800 (56 citations) Anti-rabbit IRDye 800 (35 citations) Goat anti-rabbit 800 (20 citations) IRDye 800-conjugated goat anti-rabbit IgG (17 citations) IRDye goat anti-rabbit (11 citations) IRDye 800 CW conjugated goat anti-rabbit IgG (H+L) antibody (4 citations) IRDye 800-conjugated affinity purified goat anti-rabbit IgG F(c) (3 citations) IRDye 800-conjugated anti-rabbit (2 citations) IRDye 800-conjugated goat anti-rabbit secondary antibody (2 citations)

11 protocols using irdye 800 conjugated goat anti rabbit

Western Blot Protocol for Protein Detection

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Samples separated by SDS-PAGE were transferred to nitrocellulose membranes (Bio-Rad). Membranes were incubated with the following primary antibodies: rabbit polyclonal anti-PI4KA (Cell Signaling), rabbit polyclonal anti-PI4KB (Upstate), rabbit polyclonal anti-OSBP (ProteinTech), rabbit polyclonal anti-EMCV capsid (kind gift from Ann Palmenberg) and mouse monoclonal anti-β-actin (Sigma). Secondary antibodies included IRDye 680-conjugated goat anti-mouse or IRDye 800-conjugated goat anti-rabbit (LI-COR). Images of blots were acquired with an Odyssey Fc Imaging System (LI-COR).

Dorobantu C.M., Albulescu L., Harak C., Feng Q., van Kampen M., Strating J.R., Gorbalenya A.E., Lohmann V., van der Schaar H.M, & van Kuppeveld F.J. (2015). Modulation of the Host Lipid Landscape to Promote RNA Virus Replication: The Picornavirus Encephalomyocarditis Virus Converges on the Pathway Used by Hepatitis C Virus. PLoS Pathogens, 11(9), e1005185.

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Subcellular Fractionation and Immunoblotting

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Subcellular heart protein lysates of membrane, cytoplasmic and nuclear extracts were prepared using the Subcellular Protein Fractionation kit for tissues (Thermo Scientific, Pierce Biotechnology, Rockford, IL). Equal amounts of proteins (30 μg) were resolved by 10% SDS–PAGE and semi-dry transferred to nitrocellulose membranes (BIO-Rad), which undergone blocking for 2 hrs with Odyssey Blocking Buffer (LI-COR Biosciences, Lincoln, NE), then probed overnight at 4°C with a mixture of ERα (1:500, Abcam, Cambridge, MA), NA/K ATPase (1:2000, Abcam, Cambridge, MA), β-actin (1:5000, Abcam), and Laminin B (1:2000, Santa Cruz Biotechnology, Santa Cruz, CA) antibody, respectively. The membranes were then incubated for 60 min with a mixture containing IRDye680-conjugated goat anti-mouse and IRDye800-conjugated goat anti-rabbit (1:15,000, LI-COR Biosciences). Bands were detected by Odyssey Infrared Imager and quantified by integrated intensities with Odyssey application software version 5.2 (LI-COR Biosciences).

Steagall R.J., Yao F., Shaikh S.R, & Abdel-Rahman A.A. (2017). Estrogen Receptor α Activation Enhances its Cell Surface Localization and Improves Myocardial Redox Status in Ovariectomized Rats. Life sciences, 182, 41-49.

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Western Blot Analysis of UPB1 Expression

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Cell supernatants containing 5 μg protein were fractionated on NuPAGE® 4–12 % Bis-Tris Mini Gels (Life technologies) and transferred to nitrocellulose membranes. Membranes were blocked using Odyssey blocking buffer (LI-COR). Subsequently, blots were incubated for one hour with a 1:1000 dilution of rabbit anti-UPB1 (Anti-UPB1 AV42467-100UG, Sigma-Aldrich) and 1:5000 dilution of mouse anti-alpha-tubulin antibodies in blocking buffer (50 % Odyssey blocking buffer, 50 % PBS and 0.1 % Tween). Membranes were washed three times and then incubated for one hour with a 1:10,000 dilution of IRDye800 conjugated goat anti-rabbit and IRDye680 conjugated donkey anti-mouse (both LI-COR) secondary antibodies, in the same blocking buffer as used for primary antibodies, with 0.01 % SDS. Blots were scanned and band intensities analysed using the LI-COR Odyssey infrared imaging system.

Nakajima Y., Meijer J., Dobritzsch D., Ito T., Meinsma R., Abeling N.G., Roelofsen J., Zoetekouw L., Watanabe Y., Tashiro K., Lee T., Takeshima Y., Mitsubuchi H., Yoneyama A., Ohta K., Eto K., Saito K., Kuhara T, & van Kuilenburg A.B. (2014). Clinical, biochemical and molecular analysis of 13 Japanese patients with β-ureidopropionase deficiency demonstrates high prevalence of the c.977G > A (p.R326Q) mutation. Journal of Inherited Metabolic Disease, 37(5), 801-812.

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Quantification of SNAP-25 in Mouse Brain

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Western blot was carried out as previously described.^{21 (link)} Homogenates of hippocampi and prefrontal cortex from SNAP-25^+/− mice (immediately after VLP withdrawal and after 3 weeks) were separated by electrophoresis, blotted on nitrocellulose membrane and analysed using monoclonal antibodies against SNAP-25 (Sternberger Monoclonals, Lutherville, MD, USA; 1:100 000) and anti-beta-III-tubulin (Promega, Madison, WI, USA, 1:4000). Membranes were washed and incubated for 1 h at room temperature with the secondary antibody IRDye 680-conjugated goat anti-mouse (LI-COR Biosciences, Lincoln, NE, USA; diluted 1:10 000) or IRDye 800-conjugated goat anti-rabbit (LI-COR Biosciences; diluted 1:10 000) and then scanned using an Odyssey Infrared Imaging System (LI-COR Biosciences). Alternatively, immunoreactive bands were detected using the Pierce ECL Western Blot Substrate (Thermo Fisher Scientific, Rockford, IL, USA), scanned with GS-800TM calibrated densitometer (Bio-Rad Laboratories, Segrate, Italy), and analysed with Image J Software (National Institutes of Health, Bethesda, MD, USA). For each sample, SNAP-25/beta-III-tubulin pixel values were normalized to the average of SNAP-25^+/+ controls.

Braida D., Guerini F.R., Ponzoni L., Corradini I., De Astis S., Pattini L., Bolognesi E., Benfante R., Fornasari D., Chiappedi M., Ghezzo A., Clerici M., Matteoli M, & Sala M. (2015). Association between SNAP-25 gene polymorphisms and cognition in autism: functional consequences and potential therapeutic strategies. Translational Psychiatry, 5(1), e500-.

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Immunoblotting of Proteins in Gradient Gel

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Proteins were separated with 10% gradient PAGE using the Gradi-Gel gradient analysis kit (Elpis Biotech). Samples were transferred to nitrocellulose membranes (Bio-Rad). After the membrane was cut at the 15-kDa band of the marker, one membrane (proteins larger than 15 kDa) was incubated with primary antibodies against mouse monoclonal anti-β-actin (Sigma) and rabbit polyclonal anti-GFP described previously (44 (link)), which also recognizes GFP(S1-10). The membrane with proteins smaller than 15 kDa was incubated with rabbit polyclonal anti-3A described previously (44 (link)). Secondary antibodies included IRDye 680-conjugated goat anti-mouse or IRDye 800-conjugated goat anti-rabbit (LI-COR). Images of blots were acquired with Odyssey imaging system (LI-COR).

van der Schaar H.M., Melia C.E., van Bruggen J.A., Strating J.R., van Geenen M.E., Koster A.J., Bárcena M, & van Kuppeveld F.J. (2016). Illuminating the Sites of Enterovirus Replication in Living Cells by Using a Split-GFP-Tagged Viral Protein. mSphere, 1(4), e00104-16.

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Quantitative Western Blot Analysis of GFP Expression

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Striatal punch samples were homogenized on ice in 2% SDS. Total protein concentration was determined by the Bradford protein assay. Samples were prepared at 25ng total protein samples. Western blot protocol was completed as previously described (Piltonen et al, 2009 (link)). Samples were run using SDS-PAGE and transferred to Immobilon-FL membranes (Millipore, Bedford, MA). Membranes were incubated in primary GFP antisera (AbCam, Cambridge, MA; rabbit polyclonal IgG, Ab290, 1:1,000) and β-tubulin antisera (Cell Signaling, Danvers, MA; mouse monoclonal IgG, 4466, 1:1,000) overnight. IRDye800 conjugated goat anti-rabbit (LI-COR Biosciences; 926-32211, 1:15,000) and IRDye680 conjugated goat anti-mouse (LI-COR Biosciences, 926-68020, 1:15,000) were used as secondary antibodies. All antibody dilutions were made in LI-COR specific blocking buffer (LI-COR Biosciences, 927-40000). Multiplexed signal intensities were imaged with both 700 and 800 nm channels in a single scan with a resolution of 169μm using the Odyssey infrared image system (LI-COR Biosciences). Reported integrated intensity measurements of GFP expression were normalized according to the corresponding β-tubulin densitometry measurements. The representative image was produced in Photoshop 7.0 (San Jose, CA).

Polinski N.K., Gombash S.E., Manfredsson F.P., Lipton J.W., Kemp C.J., Cole-Strauss A., Kanaan N.M., Steece-Collier K., Kuhn N.C., Wohlgenant S.L, & Sortwell C.E. (2014). Recombinant adeno-associated virus 2/5-mediated gene transfer is reduced in the aged rat midbrain. Neurobiology of aging, 36(2), 1110-1120.

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Quantitative Analysis of Receptor Tyrosine Kinase Signaling

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Low passage log-phase cells were plated into 6-well plates and incubated overnight. Cells were incubated with 1ml 100nM antibodies or DVD-Ig proteins for 24 hours in the presence of 3nM HRG. Cells were then harvested and lysed with RIPA buffer (Sigma-Aldrich, MO) supplemented with protease and phosphatase inhibitor cocktail tablet according to the manufacturer's instructions (Roche Diagnostics, IN). Cell lysate proteins were resolved by SDS-PAGE and immunoblots were probed with antibodies against phosphorylated EGFR(Tyr¹⁰⁶⁸; Cat#3777), ErbB2(Tyr^1221/1222; Cat#2243), and ErbB3(Tyr¹¹⁹⁷; Cat#4561) (Cell Signaling, MA), EGFR (NeoMarker,Thermo Fisher, CA), ErbB2 and ErbB3 (Cell Signaling, MA), phosphorylated extracellular signal-regulated kinase (pERK) 1/2 (Thr²⁰²/Tyr²⁰⁴; Cat#4370) (Cell Signaling, MA), ERK1/2, AKT (Santa Cruz, CA), ErbB2 (Cell Signaling, CA), phosphorylated AKT (pAKT; Ser⁴⁷³; Cat#4060) (Cell Signaling, MA), followed by incubation with IRDye 700 conjugated goat anti-mouse and IRDye 800 conjugated goat anti-rabbit (LI-COR, NE). Total protein was normalized with anti-PCNA (Santa Cruz, CA) followed by IRDye680 CW conjugated goat anti-mouse (LI-COR, NE). Blots were visualized using an Odyssey Imaging system (LI-COR, NE).

Gu J., Yang J., Chang Q., Liu Z., Ghayur T, & Gu J. (2015). Identification of Anti-EGFR and Anti-ErbB3 Dual Variable Domains Immunoglobulin (DVD-Ig) Proteins with Unique Activities. PLoS ONE, 10(5), e0124135.

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Quantification of Phosphorylated ERK1/2 in LV Tissue

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We followed the protocols described in our studies (Yao and Abdel-Rahman, 2016 (link), Ibrahim et al., 2014 (link), Yao and Abdel-Rahman, 2017 (link)). The supernatant (40 µg of protein) of the homogenized LV tissue was separated in a 4–12% gel electrophoresis (Novex Tis-Glycine gel, Life Technologies, CA), and transferred to nitrocellulose membrane, and then incubated with a primary antibody (mouse anti-p-ERK1/2 and rabbit anti ERK1/2; 1:500, Cell Signaling, Danvers, MA). Thereafter, the membrane was incubated with a secondary antibody (IRDye680-conjugated goat anti-mouse and IRDye800-conjugated goat anti-rabbit, 1:15000, LI-COR Biosciences, Lincoln, NE), and the protein bands were detected and quantified by Odyssey Infrared Imager (LI-COR Biosciences, Lincoln, NE).

Yao F, & Abdel-Rahman A.A. (2017). Combined Catalase and ADH Inhibition Ameliorates Ethanol-induced Myocardial Dysfunction Despite Causing Oxidative Stress in Conscious Female Rats. Alcoholism, clinical and experimental research, 41(9), 1541-1550.

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Filter-Trap Dot Blot Analysis of Huntingtin

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The filter-trap dot blot was modified from methods published previously [36 (link)]. Animals were aged 1–2 days, collected and homogenized in 1X PBS (2.7 mM KCl, 137 mM NaCl, 2 mM NaH₂PO₄, 10 mM Na₂HPO₄; pH 7.4) supplemented with cOmplete mini Protease Inhibitors (Roche Diagnostics), and diluted to 1 μg/μl; wells were loaded as indicated. Samples were diluted 1:2 in 1% SDS, 1X PBS, boiled for 5 min., and filtered through a cellulose acetate membrane (Whatman, 0.2μm pore) using a 96-well vacuum dot blot apparatus. Positive controls were collected from PC12 cells transfected with a construct expressing huntingtin “exon1” bearing a stretch of 97 glutamines and C-terminally tagged with EGFP. The membrane was washed four times with 1% SDS-PBS, blocked with Odyssey Blocking Buffer (LiCor), and primary antibodies applied in Odyssey Blocking Buffer. Blots were incubated with anti-TPI (1: 5000) and anti-GFP (1: 5000; rabbit polyclonal; FL; Santa Cruz Biotechnology). The membranes were then washed and incubated with the secondary antibody IRDye 800-conjugated goat anti-rabbit (LiCor) at 1: 20,000 in Odyssey Blocking Buffer. Direct-to-scanner detection and blot visualization were performed using a LiCor Odyssey scanner. Filter-trap experiments were performed twice.

Roland B.P., Zeccola A.M., Larsen S.B., Amrich C.G., Talsma A.D., Stuchul K.A., Heroux A., Levitan E.S., VanDemark A.P, & Palladino M.J. (2016). Structural and Genetic Studies Demonstrate Neurologic Dysfunction in Triosephosphate Isomerase Deficiency Is Associated with Impaired Synaptic Vesicle Dynamics. PLoS Genetics, 12(3), e1005941.

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Western Blot Analysis of Cellular Proteins

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Cells were lysed in Tris-glycine SDS sample buffer (Thermo Fisher Scientific) with 2.5% 2-mercaptoethanol, and the lysates were subjected to SDS-PAGE and Western blotting on nitrocellulose membranes (Bio-Rad Laboratories). After blocking (Odyssey blocking buffer; LI-COR Biosciences), the membranes were incubated with the following primary antibodies: mouse anti-RABGDI α/β (E-5; sc-374649; Santa Cruz Biotechnology, Inc.), mouse anti–β-tubulin E7 antibody (deposited to the Developmental Studies Hybridoma Bank by M. Klymkowsky; DSHB Hybridoma Product E7), rabbit anti-ICMT (51001-2-AP; Proteintech), rabbit anti-RAB8 (D22D8; 6975; Cell Signaling Technology), rabbit anti-RAB7 (EPR7589; ab137029; Abcam), rabbit anti-EGFR (D38B1; 4267; Cell Signaling Technology), rabbit anti-CIMPR (EPR6599 ab124767; Abcam), rabbit anti-GFP (A6455; Thermo Fisher Scientific), rabbit anti–cleaved NOTCH1 (D3B8; 4147; Cell Signaling Technology), and rabbit anti-NOTCH1 (D1E11; 3608; Cell Signaling Technology). Secondary antibodies were IRDye 800–conjugated goat anti–rabbit or IRDye 680–conjugated goat anti–mouse (926-32211 and 926-68070; LI-COR Biosciences). Blots were visualized with the Odyssey infrared imaging system (LI-COR Biosciences) and quantified using Odyssey software.

Court H., Ahearn I.M., Amoyel M., Bach E.A, & Philips M.R. (2017). Regulation of NOTCH signaling by RAB7 and RAB8 requires carboxyl methylation by ICMT. The Journal of Cell Biology, 216(12), 4165-4182.

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