Odyssey device

Manufactured by LI COR

Sourced in United States

The Odyssey device is a high-performance imaging system designed for a variety of life science applications. It utilizes fluorescence detection technology to capture and analyze data from various sample types.

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Lab products found in correlation

Complete protease inhibitor, by Roche (2 mentions) Rhodamine red x, by Jackson ImmunoResearch (1 mentions) α tubulin antibodies clone b 5 1 2, by Merck Group (1 mentions) Infrared dye conjugated secondary antibodies, by Rockland Immunochemicals (1 mentions) Iblot transfer system, by Thermo Fisher Scientific (1 mentions) Np0004, by Thermo Fisher Scientific (1 mentions) Np0007, by Thermo Fisher Scientific (1 mentions) Nupage 4 12 bis tris gel, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Blocking reagent, by Roche (1 mentions) Ecl detection system, by Thermo Fisher Scientific (1 mentions) Iblot gel transfer device, by Thermo Fisher Scientific (1 mentions) Goat anti rabbit 800, by LI COR (1 mentions) Mouse anti tubulin, by Abcam (1 mentions) Iblot2, by Thermo Fisher Scientific (1 mentions) Goat anti mouse 680, by LI COR (1 mentions) Odyssey blocking buffer, by LI COR (1 mentions) Radioimmunoprecipitation assay buffer, by Merck Group (1 mentions) Donkey anti guinea pig irdye 800cw, by LI COR (1 mentions) Irdye 800cw goat anti mouse igg, by LI COR (1 mentions)

7 protocols using odyssey device

Comprehensive Antibody Database for Neuroscience Research

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The antibodies α-Cpx (Troy Littleton, MIT, Cambridge, MA; Huntwork and Littleton, 2007 (link)) and α-phospho-Mad (PS1; Peter ten Dijke, Leiden University Medical Center, Leiden, Netherlands; Dan Vasiliauskas, Susan Morton, Tom Jessell, and Ed Laufer, Columbia University Medical Center, New York, NY; Persson et al., 1998 (link)) have been described previously. α-Rab11 antibodies were obtained from BD Biosciences, San Jose, CA (clone 47; Khodosh et al., 2006 (link)), α-TDP-43 antibodies (10782-2-AP) from Proteintech, Rosemont, IL, and α-tubulin antibodies (clone B-5-1-2) from Sigma-Aldrich, St. Louis, MO. Rhodamine Red-X– and Alexa 647-conjugated α–horseradish peroxidase (HRP) antibodies were obtained from Jackson ImmunoResearch, West Grove, PA. α-Dlg (4F3), α-Futsch (22c10), α-Wit (23C7), α-actin (JLA20), α-eve (2B8), and α-synapsin (3C11) antibodies were obtained from the Developmental Studies Hybridoma Bank (University of Iowa, Iowa City, IA). Secondary antibodies for imaging were conjugated to Dylight 488 or Rhodamine Red-X (Jackson ImmunoResearch). Immunoblots were imaged using infrared dye–conjugated secondary antibodies (Rockland Immunochemicals, Pottstown, PA) on a LI-COR Odyssey device.

Deshpande M., Feiger Z., Shilton A.K., Luo C.C., Silverman E, & Rodal A.A. (2016). Role of BMP receptor traffic in synaptic growth defects in an ALS model. Molecular Biology of the Cell, 27(19), 2898-2910.

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Western Blot Protein Analysis Protocol

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Protein concentration was evaluated using the Micro BCA Protein assay kit, according to the manufacturer’s recommendations. Diluted proteins were mixed with Laemmli Buffer 4×. Samples and molecular standards (PageRuler) were loaded on a SDS-PAGE 12% acrylamide gel and then transferred on a nitrocellulose membrane by semi-dry transfer (Transblot Turbo). At the end of transfer, membranes were blocked for 1 h, under agitation, at RT with Odyssey Blocking Buffer. Then, membranes were incubated with the primary antibodies in the Odyssey Blocking Buffer overnight, at 4°C, under agitation. The following day, membranes were washed in PBS-0.1% Triton x-100 and incubated with secondary antibodies diluted in Odyssey Blocking Buffer for 2 h, at RT, under agitation. After few washes in PBS-0.1% Triton x-100, membranes were revealed with the LI-COR Odyssey device. The expression of the gene of interest was reported to β-actin expression for in vitro experiments and to β III-tubulin expression for in vivo experiments.

Jollé C., Déglon N., Pythoud C., Bouzier-Sore A.K, & Pellerin L. (2019). Development of Efficient AAV2/DJ-Based Viral Vectors to Selectively Downregulate the Expression of Neuronal or Astrocytic Target Proteins in the Rat Central Nervous System. Frontiers in Molecular Neuroscience, 12, 201.

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Western Blot Analysis of Sf9 Cell Lysates

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Sf9 transfected cells were pelleted, and the supernatant was removed. Pellets were re-suspended in 100 μL of lysis buffer (Tris/phosphate 25 mM, pH 7.8, Glycerol 15%, DTT 1 mM, EDTA 1 mM, MgCl₂ 8 mM, Triton 0.2%) with Protease inhibitor cocktail (04693116001; Roche). Samples were kept on ice for 30 min before being centrifuged at 10,000 rpm for 10 min. The supernatant (20 μL) was mixed with LDS 4 × (NP0007; Invitrogen) and 10 × reducing agent (NP0004; Invitrogen). Samples were then heated for 15 min at 94°C and were run on a polyacrylamide gel (NuPAGE 4–12% Bis-Tris Gel; Invitrogen). After migration, proteins were transferred onto a nitrocellulose membrane using the iBlot transfer system (Invitrogen), following the manufacturer's protocol. Membranes were incubated for 1 h with blocking buffer (Odyssey). Membrane blotting was made with first antibody immunoglobulin B1 at 1/250 dilution (65158; Progen) and secondary antibody 680 LT (925-68020; Li-cor) diluted 1/20,000, following the manufacturer's instructions, and the image was acquired with an Odyssey device (Li-cor).

Savy A., Dickx Y., Nauwynck L., Bonnin D., Merten O.W, & Galibert L. (2017). Impact of Inverted Terminal Repeat Integrity on rAAV8 Production Using the Baculovirus/Sf9 Cells System. Human Gene Therapy Methods, 28(5), 277-289.

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Cell Lysis, Protein Separation, and Detection

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Cells were lysed in RIPA buffer [50 mM Tris (pH 7.5), 150 mM NaCl, 1% Triton-X-100, 0.5% sodium deoxycholate, 0.1% SDS, 1 mM sodium orthovanadate, 10 mM sodium fluoride, and 20 mM β-glycerophosphate plus Complete protease inhibitors (Roche, Basel, Switzerland)] and lysates were clarified by centrifugation at 16,000 × g for 10 min. Proteins where separated by SDS-Page and transferred to a Nitrocellulose membrane using the iBlot Gel Transfer Device (Life Technologies). The membrane was blocked with 0.5% blocking reagent (Roche) in PBS containing 0.1% Tween-20 and then incubated with primary antibodies, followed by HRP- or IRDye-conjugated secondary antibodies. Visualization was carried out using the ECL detection system (Thermo Fischer) or the Odyssey device (LI-COR Bioscience).

Bischoff A., Bayerlová M., Strotbek M., Schmid S., Beissbarth T, & Olayioye M.A. (2015). A global microRNA screen identifies regulators of the ErbB receptor signaling network. Cell Communication and Signaling : CCS, 13, 5.

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Western Blot Analysis of PLD1 in Mouse Cortex

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Total protein was extracted from the cortex of PLD₁ KO mice and littermate controls by homogenization in radioimmunoprecipitation assay buffer (Sigma) with protease inhibitors. After homogenization, samples were spun for 20 min at 15,000g at 4°C. The supernatant was kept, and protein concentration was determined using a bicinchoninic acid protein assay (Pierce). Protein (50 µg per sample) was electrophoretically resolved using a 4 to 20% SDS polyacrylamide gel and transferred onto a nitrocellulose membrane using iBlot 2 (Thermo Fisher Scientific). The membrane was blocked with Odyssey blocking buffer (LI-COR) for 1 hour at room temperature. Membranes were incubated overnight at 4°C with the following primary antibodies: rabbit anti-PLD₁ (1:500 dilution; Cell Signaling Technology, 3832) and mouse anti-tubulin (1:5000; Abcam, ab44928). Membranes were washed with TBST (25 mM tris, 150 mM NaCl, and 0.05% Tween 20) and incubated with fluorescently labeled secondary antibodies (goat anti-rabbit 800 and goat anti-mouse 680; 1:5000; LI-COR) for 1 hour at room temperature. Blots were washed again and imaged with a LI-COR Odyssey device.

Moran S.P., Xiang Z., Doyle C.A., Maksymetz J., Lv X., Faltin S., Fisher N.M., Niswender C.M., Rook J.M., Lindsley C.W, & Conn P.J. (2019). Biased M1 receptor–positive allosteric modulators reveal role of phospholipase D in M1-dependent rodent cortical plasticity. Science signaling, 12(610), eaax2057.

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Quantitative Immunoblotting of VGLUT1

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Two days after transfection, the HEK293T cells were lysed for 30 min at 4°C in buffer containing 25 mM Tris, pH 7.5, 150 mM NaCl, 1% Triton X-100, 1 mM EDTA supplemented with complete protease inhibitor (Roche), the extract sedimented for 20 mins at 14000 g at 4°C and the pellet discarded. Five mg supernatant protein was separated by electrophoresis through 10% SDS-polyacrylamide and transferred to a nitrocellulose membrane. The membrane was blocked in 150 mM NaCl with 50 mM Tris, pH 7.4 (TBS) and 5% dry milk, incubated with guinea pig anti-VGLUT1 (1:2000, Millipore Sigma) or mouse anti-actin (1:3000, Sigma) in TBS + 0.1% Tween-20 overnight at 4°C, washed three times for 5 min each in TBS + 0.1% Tween-20, incubated for 30 min at room temperature with IRDye 800CW Donkey anti-Guinea Pig or IRDye 800CW Goat anti-Mouse IgG (1:20000, LI-COR) in blocking buffer + 0.1% Tween-20, washed three times for 10 min each in TBS + 0.1% Tween-20 and rinsed in TBS. The membrane was scanned using an Odyssey device (LI-COR) and the resulting images quantified in ImageJ.

Chang R., Eriksen J, & Edwards R.H. (2018). The dual role of chloride in synaptic vesicle glutamate transport. eLife, 7, e34896.

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Quantifying m6A RNA Modification

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Poly-A+ mRNA were isolated using a PolyATtract® mRNA Isolation Systems (Promega) in accordance with the instructions. First, the mRNA sample was applied to a N+ nylon membrane (RPN303B, BIOSHARP, China) and UV-crosslinked using a crosslinking device (CL-1000, UVP). Next, the membranes were incubated overnight using an anti-m⁶A antibody (1:500 dilution in PBS; Synaptic Systems, catalog number: 202003) after blocking in 5% milk for 1 h at room temperature. The membranes were then incubated with secondary antibodies and exposed using an Odyssey device (LI-COR Biosciences, Lincoln, NE, USA).

Han Z., Wang X., Xu Z., Cao Y., Gong R., Yu Y., Yu Y., Guo X., Liu S., Yu M., Ma W., Zhao Y., Xu J., Li X., Li S., Xu Y., Song R., Xu B., Yang F., Bamba D., Sukhareva N., Lei H., Gao M., Zhang W., Zagidullin N., Zhang Y., Yang B., Pan Z, & Cai B. (2021). ALKBH5 regulates cardiomyocyte proliferation and heart regeneration by demethylating the mRNA of YTHDF1. Theranostics, 11(6), 3000-3016.

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