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Irdye 680rd goat anti rabbit igg

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IRDye 680RD goat anti-rabbit IgG is a secondary antibody conjugated with the near-infrared dye IRDye 680RD. It is designed for use in fluorescence-based detection and quantification of rabbit primary antibodies in various applications.

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Lab products found in correlation

Irdye 800cw goat anti mouse igg, by LI COR (56 mentions) Irdye 800cw goat anti rabbit igg, by LI COR (15 mentions) Irdye 680rd goat anti mouse igg, by LI COR (11 mentions) Odyssey blocking buffer, by LI COR (9 mentions) Odyssey infrared imaging system, by LI COR (8 mentions) Nitrocellulose membrane, by Bio-Rad (6 mentions) Ripa lysis buffer, by Thermo Fisher Scientific (6 mentions) Odyssey imaging system, by LI COR (6 mentions) Ripa buffer, by Thermo Fisher Scientific (6 mentions) Odyssey clx, by LI COR (5 mentions) β actin, by Merck Group (4 mentions) Image studio software, by LI COR (4 mentions) Odyssey clx imaging system, by LI COR (4 mentions) Protease inhibitor cocktail, by Merck Group (4 mentions) Irdye 800cw donkey anti mouse igg, by LI COR (3 mentions) Ripa buffer, by Cell Signaling Technology (3 mentions) General hrp conjugated secondary antibodies, by Southern Biotech (3 mentions) Irdye 800rd goat anti mouse igg, by LI COR (3 mentions) Trans blot turbo transfer system, by Bio-Rad (3 mentions) Mops buffer system, by Thermo Fisher Scientific (3 mentions)

80 protocols using irdye 680rd goat anti rabbit igg

1

Profiling Hypoxia-Induced Protein and Epigenetic Changes

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Cells were lysed in UTB (9 M urea, 75 mM Tris-HCl pH 7.5, 0.15 M β-mercaptoethanol) and briefly sonicated. Primary antibodies used: HIF-1a (BD Transduction Labs., 610959), KDM4A (Abcam, ab24545), CAIX (BioScience, AB1001), Glut1 (Abcam, ab14683), Actin (Santa Cruz, sc-69879), H3K9me3 (Millipore, 07-422), H3K36me3 (Abcam, ab9050), H3 (Cell Signaling, 36385), NFκB p52 (Millipore, 05-361), Sp1 (Millipore, 07-645), E2F-1 (Cell Signaling, 3742S), HIF-2a (Novus Biologicals, NB100-122). Secondary antibodies were IRDye® 680RD Goat anti-Mouse IgG (H+L), IRDye® 680RD Goat anti-Rabbit IgG (H+L), IRDye® 800CW Donkey anti-Mouse IgG (H+L) and IRDye® 800CW Donkey anti-Rabbit IgG (H+L) from LI-COR Biosciences. Odyssey IR imaging technology (LI-COR Biosciences) was used for imaging.
Dobrynin G., McAllister T.E., Leszczynska K.B., Ramachandran S., Krieg A.J., Kawamura A, & Hammond E.M. (2017). KDM4A regulates HIF-1 levels through H3K9me3. Scientific Reports, 7, 11094.
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2

EGFR and HO-1 Protein Analysis

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The following antibodies were used:
Rabbit monoclonal anti-EGFR (ab52894, Abcam, Cambridge, UK); mouse monoclonal anti-EGFR (sc-120, Santa Cruz Biotechnology, USA); mouse monoclonal anti-EGFRvIII (L8A4, Absolute Antibodies, UK); rabbit polyclonal anti-EGFR (ab5652, Abcam, UK); mouse monoclonal anti-HO-1 (ab13248, Abcam, UK); mouse monoclonal anti-β-actin (AC-15, Sigma-Aldrich, USA); IRDye® 800CW goat anti-mouse IgG (827-08364, LI-COR Biotechnology, Germany); IRDye® 680RD goat anti-rabbit IgG (926-68071, LI-COR Biotechnology, Germany).
Fontana A.O., Piffaretti D., Marchi F., Burgio F., Faia-Torres A.B., Paganetti P., Pinton S., Pieles U, & Reinert M. (2017). Epithelial growth factor receptor expression influences 5-ALA induced glioblastoma fluorescence. Journal of Neuro-Oncology, 133(3), 497-507.
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3

Western blot and immunofluorescence analysis

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Western blots were performed using standard procedures and the following reagents: RHAMM (GTX62573, GeneTex, Irvine), p53 (OP43, Calbiochem, Billerica), p38 (#9212, Cell Signaling Technologies, Danvers), pp38 (#9211, Cell Signaling Technologies, Danvers), β-tubulin (T7816, Sigma-Aldrich Chemie, München) and β-actin (A5316, Sigma-Aldrich Chemie, München). Binding protein for affinitycytochemistry of hyaluronan was biotinylated HABP (Calbiochem, Billerica) and as secondary antibody streptavidin-FITC (Dako, Glostrup) was used. Secondary antibodies for western blotting were IRDye® 800CW goat anti-rabbit IgG, IRDye® 800CW goat anti-mouse IgM, IRDye® 680RD goat anti-rabbit IgG and IRDye® 680LT goat anti-mouse IgM (LI-COR Biotechnology, Bad Homburg). Immunofluorescence secondary antibodies were AF488 goat anti-rabbit IgG (Life Technologies, Carsbad) and AF568 (Fab')2 fragment of goat anti-mouse IgG (H+L) (Life Technologies, Carsbad).
Schütze A., Vogeley C., Gorges T., Twarock S., Butschan J., Babayan A., Klein D., Knauer S.K., Metzen E., Müller V., Jendrossek V., Pantel K., Milde-Langosch K., Fischer J.W, & Röck K. (2016). RHAMM splice variants confer radiosensitivity in human breast cancer cell lines. Oncotarget, 7(16), 21428-21440.
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4

Cytosolic and Nuclear Protein Extraction from Jurkat Cells

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Jurkat cells were washed twice with ice-cold PBS. To extract cytosolic and nuclear protein, Nuclear and Cytoplasmic Protein Extraction Kit was used according to the manufacture's instructions (Beyotime, Haimen, China). Proteins from the extraction were resolved by electrophoresis, transferred to a PVDF membrane, and hybridized with antibodies for strep (GenScript, Nanjing, China, 1:2000), H3 (Abcam, Cambridge, UK, 1:4000), actin (GenScript, Nanjing, China, 1:2000), NFκB P65 (Sangon Biotech, Shanghai, China, 1:500), IKK and IκB (Beyotime, Shanghai, China, 1:1000). Next, the membranes were incubated in secondary antibody, IRDye® 800CW Goat anti-Mouse IgG and IRDye® 680RD Goat anti-Rabbit IgG (both from LI-COR Biosciences, Lincoln, NE) for 2 hours and the specific bands on the membranes were detected using Odyssey® Imaging Systems (LI-COR Biosciences, Lincoln, NE).
Zhang Y., Yu X., Lin D., Lei L., Hu B., Cao F., Mei Y., Wu D, & Liu H. (2017). Propiece IL-1α facilitates the growth of acute T-lymphocytic leukemia cells through the activation of NF-κB and SP1. Oncotarget, 8(9), 15677-15688.
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5

Western Blot Analysis of CD-NTase Expression

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CD-NTase in-cell expression levels were verified by Western blot of lysed cells. Confluent HEK293T cells were seeded 24 h prior to transfection at a dilution of 1:4 in a 6-well dish. Cells were transfected with 2 μg of plasmid using Lipofectamine2000. At 24 h post transfection cells were harvested by washing cells from the dish using Hanks Buffered Saline Solution, pelleted at low speed, and flash frozen. Pelleted cells were lysed by re-suspending the pellet in 400 μL 1x LDS buffer (ThermoFisher Scientific) + 5% β-mercaptoethanol, boiling for 5 min, and vigorously vortexing. Samples were separated by SDS-PAGE, transferred to nitrocellulose membrane, and probed with primary antibodies 1:5,000 Rabbit anti-MBP (Millipore Cat# AB3596, RRID:AB_91531) and 1:10,000 Mouse anti-Tubulin (Millipore Cat# MABT205, RRID:AB_11204167), followed by secondary antibodies at 1:10,000 IRDye 680RD Goat anti-Rabbit IgG (LI-COR Biosciences Cat# 925–68071, RRID:AB_2721181) and IRDye 800CW Goat anti-Mouse IgG (LI-COR Biosciences Cat# 925–32210, RRID:AB_2687825). Stained membrane was imaged using a LI-COR Odyssey CLx imager.
Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R., Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S., Mekalanos J.J, & Kranzusch P.J. (2019). Bacterial cGAS-like enzymes synthesize diverse nucleotide signals. Nature, 567(7747), 194-199.
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6

Steroid Hormone Receptor Expression Analysis

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Cells were treated with vehicle (ethanol), 10 nM E2, 100 nM P4, E2 plus P4, or 10 nM DHT for 48 h. Cell lysates were harvested in lysis buffer (50 mM Tris pH 7.4, 140 nM NaCl, 2 mM EGTA, 1% Tween-20) plus protease/phosphatase inhibitors. Primary antibodies were as follows: ERα (6F11, Santa Cruz Biotechnology (sc-56,836), 1:1000), PR (1294, 1:500), AR (441, 11,000, DAKO-Agilent, Santa Clara, CA), and α-tubulin (ST1568, 1:30,000, Sigma-Aldrich). Secondary antibodies were as follows: IRDye 800CW Goat-Anti-Mouse IgG and IRDye 680RD Goat-Anti-Rabbit IgG (all from Li-Cor Biosciences, Lincoln, NE). The Odyssey CLx Infrared Imaging System and Image Studio 5.2 (Li-Cor Biosciences) were used to capture images.
Finlay-Schultz J., Jacobsen B.M., Riley D., Paul K.V., Turner S., Ferreira-Gonzalez A., Harrell J.C., Kabos P, & Sartorius C.A. (2020). New generation breast cancer cell lines developed from patient-derived xenografts. Breast Cancer Research : BCR, 22, 68.
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7

Western Blot Analysis of Lipid Metabolism Proteins

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Protein lysates were prepared in RIPA lysis buffer (ThermoFisher Scientific) with cOmplete Mini EDTA-free Protease Inhibitor Cocktail (Roche). Western blot was performed using NuPAGE gel (ThermoFisher Scientific) with wet tank blotting (Bio-Rad) and Odyssey detection system (LI-COR). SREBF1 primary antibody (14088-1-AP, Proteintech), SCD (CD.E10) antibody (ab19862, Abcam), GAPDH (D16H11) XP rabbit monoclonal antibody (5174S, Cell Signaling), β-actin (8H10D10) mouse monoclonal antibody (3700S, Cell Signaling), and IRDye 800CW goat anti-mouse IgG (926-32210, LI-COR), IRDye 680RD goat anti-rabbit IgG (926-68071, LI-COR) secondary antibodies were used. Western blot was performed for cells cultured in different medium conditions. These include RPMI1640 with 10% FBS, with 10% delipidated FBS, with 10% human cerebrospinal fluid (991-19-P-5, Lee BioSolutions), or with 1% SM1 supplement (05711, STEMCELL Tech), or brain-slice-conditioned medium. Brain-slice-conditioned medium was prepared by submerging brain slices (150 μm) in RPMI1640 (no serum) for 48 h. Delipidated FBS was prepared as described51 (link).
Jin X., Demere Z., Nair K., Ali A., Ferraro G.B., Natoli T., Deik A., Petronio L., Tang A.A., Zhu C., Wang L., Rosenberg D., Mangena V., Roth J., Chung K., Jain R.K., Clish C.B., Vander Heiden M.G, & Golub T.R. (2020). A metastasis map of human cancer cell lines. Nature, 588(7837), 331-336.
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8

Western Blot Analysis of Drosophila Proteins

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Whole fly lysates were prepared by homogenizing the adult flies in RIPA buffer (50 mM Tris-HCl [pH 7.4], 150 mM NaCl, 1% [v/v] NP-40, 0.1% [w/v] SDS, 0.5% [w/v] sodium deoxycholate,1 mM EDTA, 5 mM DTT, and 0.5 mM PMSF). The homogenates were clarified by centrifugation at 21,000g at 4°C for 10 min, and the supernatant was used for Western blot. Ovary lysates and the immunoprecipitation samples were prepared as above. Mouse anti-HA (Sigma, H3663), rabbit anti-Tubulin (Sigma, T3526), rabbit anti-α-Tubulin (Abcam, ab52866), rat anti-Vasa (Developmental Studies Hybridoma Bank), mouse anti-Dicer-2 (Miyoshi et al. 2009 (link)), mouse anti-R2D2 (Nishida et al. 2013 (link)), mouse anti-Ago2 (Miyoshi et al. 2005 (link)) (kind gifts from Dr. Mikiko Siomi and Dr. Haruhiko Siomi), and rabbit anti-R2D2 (Liu et al. 2003 (link)) (kind gift from Dr. Qinghua Liu), were used as primary antibodies. IRDye 800CW goat anti-mouse IgG, IRDye 800CW goat anti-rat IgG, IRDye 800CW goat anti-rabbit IgG, and IRDye 680RD goat anti-rabbit IgG (Licor) were used as secondary antibodies. The membrane was scanned on an Odyssey imaging system (Licor).
Kandasamy S.K., Zhu L, & Fukunaga R. (2017). The C-terminal dsRNA-binding domain of Drosophila Dicer-2 is crucial for efficient and high-fidelity production of siRNA and loading of siRNA to Argonaute2. RNA, 23(7), 1139-1153.
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9

Western Blot Analysis of Prion Protein

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Dulbecco’s Phosphate Buffered Saline (DPBS), Phenylmethanesulfonyl fluoride (PMSF) and Proteinase K were from Sigma-Aldrich (St. Louis, MO, USA). Tween 20, 10X Tris/glycine, 10X Tris/Glycine/SDS, 2X Laemmli Sample Buffer, β –mercaptoethanol and Criterion 15 % Tris–HCl polyacrylamide precast gels were from Bio-Rad Laboratories (Hercules, CA, USA). Odyssey blocking buffer, Infrared Dye (IRDye) 800CW goat anti-mouse IgG (1 mg/ml), IRDye 680RD goat anti-rabbit IgG (1 mg/ml) and the Polyvinylidene difluoride (PVDF) membrane (Immobilon-FL) were from LI-COR Biosciences (Lincoln, NE, USA). The 3F4 monoclonal antibody to PrP residues 106–110 [21 (link), 22 (link)], 12B2 monoclonal antibody to PrP residues 89–93 (this epitope is not preserved in resPrPSc type 2) [23 (link)], and the polyclonal antibody Tohoku-2 to PrP residues 97–103 [24 (link)] were used in this study.
Cali I., Miller C.J., Parisi J.E., Geschwind M.D., Gambetti P, & Schonberger L.B. (2015). Distinct pathological phenotypes of Creutzfeldt-Jakob disease in recipients of prion-contaminated growth hormone. Acta Neuropathologica Communications, 3, 37.
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10

Characterization of Histone Methylation Markers by Western Blotting and Immunofluorescence

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For western blotting, antibodies specific for histone H3 (07-690, EMD Millipore), H3K9me3 (2F3)49 (link), H3K9me2 (6D1150 (link) and 39754, Active Motif), histone H3 for Supplementary Fig. 2g (96C10, Cell Signaling), SETDB1 (Cp10377, Cell Applications), SUV39H1 (#8729, CST), SUV39H2 (LS-116360, LSBio), G9a (A8620A)7 (link) and GLP (B0422B)7 (link) were used as primary antibody. For histone proteins, IRDye 800CW Goat anti-Mouse IgG (926-32210, LI-COR) and IRDye 680RD Goat anti-Rabbit IgG (926-68071, LI-COR) were used as secondary antibody. For non-histone proteins, HRP-linked anti-Rabbit IgG (NA934, GE Healthcare) and HRP-linked anti-Mouse IgG (NA931, GE Healthcare) were used as secondary antibody. For immunofluorescence analysis, H3K9me2 (6D11), H3K9me3 (39161, Active Motif) were used for primary antibody, and Goat anti-Mouse IgG Alexa Fluor 568 (A-11031, Invitrogen) and Goat anti-Rabbit IgG Alexa Fluor 488 (A-11034) were used for secondary antibody. For ChIP analysis, antibodies specific for H3K9me3 (2F3) and H3K9me2 (6D11) were used. Specificity of antibodies for H3K9me2 and H3K9me3 were previously reported49 (link),50 (link).
Fukuda K., Shimura C., Miura H., Tanigawa A., Suzuki T., Dohmae N., Hiratani I, & Shinkai Y. (2021). Regulation of mammalian 3D genome organization and histone H3K9 dimethylation by H3K9 methyltransferases. Communications Biology, 4, 571.
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