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Irdye 800 conjugated anti mouse igg

Manufactured by Rockland Immunochemicals
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The IRDye 800-conjugated anti-mouse IgG is a laboratory reagent used for detection and quantification of mouse immunoglobulin G (IgG) in various immunoassays. It consists of an anti-mouse IgG antibody labeled with the near-infrared fluorescent dye IRDye 800. This product can be used to facilitate the visualization and measurement of mouse IgG in samples, such as in Western blotting, ELISA, and other similar applications.

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Lab products found in correlation

Odyssey infrared imaging system, by LI COR (7 mentions) Irdye 700dx conjugated anti rabbit igg, by Rockland Immunochemicals (4 mentions) Rabbit anti β actin antibody, by Bioworld Technology (2 mentions) Alexa fluor 680 goat anti rabbit igg, by Thermo Fisher Scientific (2 mentions) Odyssey infrared imager, by LI COR (1 mentions) Protease inhibitor cocktail tablet, by Roche (1 mentions) Nitrocellulose membranes 0.2 μm, by Bio-Rad (1 mentions) Irdye680 conjugated anti rabbit igg, by LI COR (1 mentions) Image studio lite version 3, by LI COR (1 mentions) Gradient gel, by Thermo Fisher Scientific (1 mentions) Nis elements br analysis software, by Nikon (1 mentions) Fitc labeled anti mouse igg, by Merck Group (1 mentions) Bis tris sds page, by Thermo Fisher Scientific (1 mentions) Protease inhibitor, by Merck Group (1 mentions) β actin, by Merck Group (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Mouse β actin, by Santa Cruz Biotechnology (1 mentions) Alexa fluor 680 conjugated anti rabbit igg, by Thermo Fisher Scientific (1 mentions) Ab9106, by Abcam (1 mentions) Ab22555, by Abcam (1 mentions)

12 protocols using irdye 800 conjugated anti mouse igg

1

Western Blot Analysis of α-SMA

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Western analysis of α-SMA was performed as described earlier [11 (link)]. Briefly, the cells were lysed in 50 mM Tris, 0.1 % Triton X-100, 0.9 % NaCl supplemented with a protease inhibitor cocktail tablet (Roche, Mannhaim, Germany) and 20 μg aliquots of samples were loaded and run on 12 % SDS–PAGE. The proteins were transferred onto nitrocellulose membrane (Protran, Schleicer and Schuell, Bioscience, Dassel, Germany). After blocking with milk, the membranes were incubated with a 1:1000 dilution of α-SMA antibody followed by 1:1000 diluted secondary antibody (IRDye 800 conjugated anti-mouse IgG, Rockland Immunochemicals, Gilbertsville, PA, USA). Protein intensities were detected and analyzed with an Odyssey infrared imager (Li-Cor Biosciences).
Lehtonen S.T., Veijola A., Karvonen H., Lappi-Blanco E., Sormunen R., Korpela S., Zagai U., Sköld M.C, & Kaarteenaho R. (2016). Pirfenidone and nintedanib modulate properties of fibroblasts and myofibroblasts in idiopathic pulmonary fibrosis. Respiratory Research, 17, 14.
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2

Western Blot Quantification Protocol

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Cell lysates were separated by SDS-PAGE (Novex 10–20% or 4–20% gradient gels (Invitrogen)) and transferred onto nitrocellulose membranes, 0.2 μm (Bio-Rad). The membranes were blocked for 1 hr at room temperature (5% nonfat dry milk in PBS, 0.1% Tween 20) and immunoblotted overnight at 4°C, with specific antibodies as indicated. Antibody binding was detected using IRDye800-conjugated anti-mouse IgG (catalog #610-102-041 RRID:AB_2614830; 1:10.000; Rockland) or IRDye680-conjugated anti-rabbit IgG (catalog #926–68021 RRID:AB_10706309; 1:10.000 LI-COR, Bioscience). Blots were analyzed and quantified using an Odyssey Infrared Imaging System (LI-COR Bioscience, Image Studio Lite version 3.1, RRID:SCR_013715). Anti-rabbit pS88 (G446), and anti-rabbit pS46 (RU1102) for ARPP-16 were detected using peroxidase-conjugated secondary antibody (catalog #PI-1000 RRID:AB_2336198; 1:300, Vector Laboratories,Inc.) coupled with a chemiluminescence detection system (Pierce, ThermoScientific).
Musante V., Li L., Kanyo J., Lam T.T., Colangelo C.M., Cheng S.K., Brody A.H., Greengard P., Le Novère N, & Nairn A.C. (2017). Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. eLife, 6, e24998.
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3

Serological Evaluation of Avian Leukosis Virus

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The two ELISA-positive samples selected from late and fast feathering chicken groups were also evaluated with Immunofluorescence assays (IFA) and Western blotting following our previously described method with ALV-J envelope protein specific monoclonal antibody JE9 (kindly provided by Dr. Kun Qian, Yangzhou University) (Venugopal et al., 1997 (link); Dai et al., 2016a (link)). IFA was performed using the FITC-labeled anti-mouse IgG (Sigma, USA) and analyzed by fluorescence microscope using NIS-Elements BR analysis software (Nikon, Japan). IRDye 800-conjugated anti-mouse IgG or IRDye 700DX-conjugated anti-rabbit IgG (1:10,000; Rockland Immunochemicals, USA) were as the secondary antibody in western blot analysis, and analyzed with an Odyssey infrared imaging system (LI-COR Biosciences, USA).
Feng M., Tan Y., Dai M., Li Y., Xie T., Li H., Shi M, & Zhang X. (2016). Endogenous Retrovirus ev21 Dose Not Recombine with ALV-J and Induces the Expression of ISGs in the Host. Frontiers in Cellular and Infection Microbiology, 6, 140.
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4

Temporal Dynamics of ALV-J Infection in Chicken MDM

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Chicken MDM were infected with a 105 TCID50/mL of ALV-J strain SCAU-HN06. DNA, RNA and total proteins were extracted from the ALV-J infected MDM at 3, 6, 12, 24 and 36 h post-infection (hpi). RT-PCR was employed to detect the ALV-J replication using specific PCR primers H5/H7 [12 (link)]. Western blotting was performed with ALV-J envelope protein specific mouse antibody JE9 (kindly provided by Dr Aijian Qin, Yangzhou University, Yangzhou, China) and rabbit anti-β-actin antibody (Bioworld, Louis Park, USA) according to the method described previously [13 (link)]. IRDye 700DX-conjugated anti-rabbit IgG and IRDye 800-conjugated anti-mouse IgG (Rockland Immunochemicals, Limerick, PA, USA) was used as the secondary antibody. Membranes were visualized and analyzed with an Odyssey infrared imaging system (LI-COR Biosciences, Lincoln, NE, USA). ALV-J provirus was detected by PCR with primers H5/H7 using DNA template.
Feng M., Xie T., Li Y., Zhang N., Lu Q., Zhou Y., Shi M., Sun J, & Zhang X. (2019). A balanced game: chicken macrophage response to ALV-J infection. Veterinary Research, 50, 20.
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5

Western Blot Analysis of ALV-J Envelope

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Western blotting was performed following our previously described method with ALV-J envelope protein specific mouse anti-monoclonal antibody JE9 (kindly provided by Dr. Aijian Qin, Yangzhou University, Yangzhou, China) and rabbit anti-β-actin antibody [22 (link)]. IRDye 700DX-conjugated anti-rabbit IgG and IRDye 800-conjugated anti-mouse IgG (Rockland Immunochemicals, Limerick, PA, USA) were used as the secondary antibody. Membranes were visualized and analyzed with an Odyssey infrared imaging system (LI-COR Biosciences, Lincoln, NE, USA).
Dai M., Feng M., Xie T., Li Y., Ruan Z., Shi M., Liao M, & Zhang X. (2017). ALV-J infection induces chicken monocyte death accompanied with the production of IL-1β and IL-18. Oncotarget, 8(59), 99889-99900.
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6

Immunoblotting Analysis of Phospho-p65

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The muscularis externae tissue was homogenized on ice in lysis buffer supplemented with protease inhibitors (Sigma-Aldrich, St. Louis, MO). The compositions of lysis buffer are (in mmol/L) 20 Tris-HCl, pH 7.5, 150 NaCl, 1 EDTA, 1 ethylene glycol-bis (β-aninoethyl ether)-N,N,N',N'-tetraacetic acid, 2.5 sodium pyrophosphate, 1 β-glycerolphosphate, 1 Na3VO4, and 1% Triton X-100, and 1 ug/mL leupeptin. The proteins in the homogenates were resolved by a standard immunoblotting method as described previously (25–27, 30–34). Equal quantities of total protein (10 µg) were loaded and run on premade 4–12% Bis-Tris SDS-PAGE (Invitrogen, Carlsbad, CA). They were transferred to nitrocellulose membranes (BIO-RAD, Hercules, CA) for incubation with primary and secondary antibodies. The following antibodies were used in the study: primary antibodies to phospho-p65 (1∶200; Santa Cruz Biotechnology Inc, Santa Cruz, CA); β-actin (1∶5,000, Sigma, St. Louis, MO). Secondary antibody IRDye 800-conjugated anti-mouse IgG (Rockland, Gilbertsville, PA), or Alexa Fluor 680 goat anti-rabbit IgG (Invitrogen, Carlsbad, CA) were used. β-actin was used as loading control. The detection was done by Odyssey Infrared Imaging System (LI-COR Biosciences, Lincoln, NE).
Lin Y.M., Li F, & Shi X.Z. (2014). Mechanical Stress Is a Pro-Inflammatory Stimulus in the Gut: In Vitro, In Vivo and Ex Vivo Evidence. PLoS ONE, 9(9), e106242.
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7

Cell culture protocol for glioblastoma, colon cancer, and normal fibroblasts

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Human glioblastoma cells Gli36, human colon carcinoma cells HCT116 and normal skin fibroblasts OSU2 were maintained according to established methods as described. Gli36 cell line was grown in DMEM supplemented with 10% fetal bovine serum (FBS) and antibiotics (50 units/ml penicillin and 50 μg/ml streptomycin). HCT116 cells were cultured in McCoy’s 5A medium supplemented with 10% FBS and antibiotics as above. Normal human skin OSU-2 fibroblasts were established and maintained in culture as described in previous studies (Venkatachalam et al., 1995 (link)). All cells were grown at 37°C in a humidified 5% CO2 atmosphere. The DC protein quantitation reagents were from Bio-Rad. Antibodies against the following proteins were diluted in blocking buffer: mouse β-actin (Santa Cruz Biotechnology, Santa Cruz, CA) diluted 1/3000; rabbit phospho-histone H2A.X, serine 139 (Millipore, Billerca, MA) diluted 1/3000. Alexa Fluor 680-conjugated anti-rabbit IgG (Molecular Probes) and IRDye800 conjugated anti-mouse IgG (Rockland, Gilbertsville, PA) were used as secondary antibodies. Texas red and FITC conjugated fluorescent antibodies were from Santa Cruz Biotechnology.
Rehmani N., Zafar A., Arif H., Hadi S.M, & Wani A.A. (2017). Copper-mediated DNA damage by the neurotransmitter dopamine and L-DOPA: A pro-oxidant mechanism. Toxicology in vitro : an international journal published in association with BIBRA, 40, 336-346.
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8

Western Blot Analysis of Cellular Proteins

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Cells were washed with cold PBS and lysed with RIPA Lysis Buffer (Beyotime Institute of Biotechnology, Nantong, China) with 0.1 mM PMSF, and then lysates were cleared by centrifugation at 12,000 g for 5 min at 4°C. Equal amounts of protein samples were separated by 10% SDS-PAGE and transferred onto nitrocellulose membranes (Millipore). The membranes were blocked with 5% skim milk for 1-2 h at room temperature and then incubated for 1 hour at room temperature with mouse anti-FLAG M2 MAb (1804, Sigma), rabbit anti-Myc polyclonal antibody (ab9106, Abcam), rabbit anti-IRF1 monoclonal antibody (ab186384, Abcam), rabbit anti-GADPH antibody (ab22555, Abcam), and mouse anti-FCV VP1 monoclonal antibody (made by our laboratory).
After three rinses in TBST buffer, the membranes were incubated at room temperature for 1 h with IRDye 800DX conjugated anti-rabbit IgG or IRDye 800-conjugated anti-mouse IgG (1:8000; Rockland Immunochemicals) diluted with TBST as a secondary antibody. After the third wash, membranes were visualized and analysed with an Odyssey infrared imaging system (LI-COR Biosciences).
Liu Y., Liu X., Kang H., Hu X., Liu J., Tian J, & Qu L. (2018). Identification of Feline Interferon Regulatory Factor 1 as an Efficient Antiviral Factor against the Replication of Feline Calicivirus and Other Feline Viruses. BioMed Research International, 2018, 2739830.
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9

Western Blotting of Avian Leukosis Virus

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Western blotting was performed with ALV-J envelope protein specific mouse anti-monoclonal antibody JE9 (kindly provided by Prof. Aijian Qin, Yangzhou University, Yangzhou, China), rabbit anti-β-actin antibody (Bioworld, Louis Park, MN, USA) and mouse anti-flag monoclonal antibody (Proteintech, Rosemont, CA, USA) according to our previously described method [26 (link)]. IRDye 800-conjugated anti-mouse IgG and IRDye 700DX-conjugated anti-rabbit IgG (Rockland Immunochemicals, Limerick, PA, PA, USA) were used as the secondary antibody. Results were visualized and analyzed with an Odyssey FC infrared imaging system (LICOR Biosciences, Lincoln, NE, USA).
Xie T., Feng M., Dai M., Mo G., Ruan Z., Wang G., Shi M, & Zhang X. (2019). Cholesterol-25-hydroxylase Is a Chicken ISG That Restricts ALV-J Infection by Producing 25-hydroxycholesterol. Viruses, 11(6), 498.
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10

Cdc42 and Cdc11 Protein Detection

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Total protein was extracted from 107 log-phase cells by TCA precipitation. Electrophoresis and Western blotting were performed as described [16 ]. Monoclonal anti-Cdc42 [16 ] and anti-GFP (Roche Applied Sciences) were used at 1:500 and 1:2000 dilution. Polyclonal anti-Cdc11 antibodies (Santa Cruz Biotechnologies) and secondary antibodies (IRDye800 conjugated anti-mouse IgG, Rockland Immunochemicals, or Alexa Fluor 680 goat anti-rabbit IgG, Invitrogen) were used at 1:5000 dilution. Western blots were visualized using the ODYSSEY imaging system (LI-COR Biosciences).
Woods B., Lai H., Wu C.F., Zyla T.R., Savage N.S, & Lew D.J. (2016). Parallel actin-independent recycling pathways polarize Cdc42 in budding yeast. Current biology : CB, 26(16), 2114-2126.
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