Odyssey quantitative fluorescence imaging system

Manufactured by LI COR

Sourced in Germany

The Odyssey Quantitative Fluorescence Imaging System is a laboratory instrument designed for the detection and quantification of fluorescent signals. It utilizes near-infrared fluorescence technology to provide sensitive and accurate measurements of protein and nucleic acid samples.

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Lab products found in correlation

Polyacrylamide gel, by Bio-Rad (3 mentions) Criterion precast gel, by Bio-Rad (3 mentions) Anti β actin antibody, by Merck Group (3 mentions) Trans blot turbo transfer system, by Bio-Rad (3 mentions) Protein assay, by Bio-Rad (3 mentions) Halt phosphatase inhibitor cocktail, by Thermo Fisher Scientific (1 mentions) Iblot system, by Thermo Fisher Scientific (1 mentions) Mab318, by Abcam (1 mentions) Nupage novex bis tris 4 12 gradient gels, by Thermo Fisher Scientific (1 mentions) Irdye fluorescent secondary antibodies, by LI COR (1 mentions) Polyvinylidene difluoride membrane, by Cytiva (1 mentions) Western blotting detection reagent, by Cytiva (1 mentions) Hrp linked secondary antibody, by Bio-Rad (1 mentions) Complete protease inhibitor, by Roche (1 mentions) Sc 8432 hrp, by Santa Cruz Biotechnology (1 mentions) Sc83 18, by Santa Cruz Biotechnology (1 mentions) Anti gapdh antibody, by Abcam (1 mentions) Lucifer yellow, by Merck Group (1 mentions)

Close spelling variants of this product

Odyssey imaging system (2037 citations) Odyssey system (784 citations) Odyssey fluorescence imaging system (15 citations) Quantitative fluorescence imaging system (4 citations)

6 protocols using odyssey quantitative fluorescence imaging system

Western Blot Analysis of Synaptophysin

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Protein was extracted with 1 × RIPA buffer (CST #9806) with 1× Calbiochem Protease Inhibitor Cocktail Set I (Cat. No. 539131) and 1× Halt* Phosphatase Inhibitor Cocktail (Thermo Scientific 78240). The cell lysate was then centrifuged at 13k rpm for 10 min at 4°C. BCA (bicinchoninic acid) protein assay reagents were used to determine protein concentration in the supernatant using a kit from Pierce (#23225). The supernatant was denatured in 4× LDS buffer (Invitrogen) at 75 °C for 10 minutes. Protein was then subjected to 4-12% Criterion SDS-PAGE gel (Bio-Rad) and transferred onto PVDF membranes using the iBlot system ((Invitrogen) under program 4 for 7 minutes. Primary antibody against synaptophysin (EMD Millipore, 1:1000) and β-actin (CST, 1:1000) was incubated overnight at 4°C. These primary antibodies are reactive to human, rat and mouse antigen. The synaptophysin protein sequences are highly homologous among these three species. A secondary antibody from LiCor (IR800 for β-actin or IR680 for synaptophysin) was used accordingly for each primary antibody. Immunoreactive bands were scanned by the ODYSSEY® Quantitative Fluorescence Imaging System (LiCor).

Bai X, & Strong R. (2014). Expression of synaptophysin protein in different dopaminergic cell lines. Journal of biochemical and pharmacological research, 2(4), 185-190.

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Protein Extraction and Analysis from Mouse Retinas

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For protein extraction, whole retinas were isolated from 1- month-old mice (C57BL6/J, ATF4^+/-, T17M and T17M ATF4^+/-) by surgical excision. Total protein was extracted via sonication in a protein extraction buffer containing 25 mM sucrose, 100 mM Tris-HCl, pH = 7.8, and a mixture of protease inhibitors (PMSF, TLCK, aprotinin, leupeptin, and pepstatin). Protein concentrations were determined using BioRad Protein Assays based on the Bradford method for protein quantitation. Proteins (30–40 μg) were separated in 4–20% Criterion Precast gels and 5% polyacrylamide gels (BioRad), transferred to a polyvinylidene difluoride (PVDF) membrane using the Trans-Blot Turbo Transfer System (BioRad) and incubated with primary antibodies overnight at 4°C under agitation. After washing, the membranes were incubated for 1.5 h with respective (anti-mouse, anti-rabbit or anti-goat immunoglobulin) Fluorescence or HRP conjugated secondary antibody (LI-COR Odyssey). For HRP tagged antibody blots were developed with enhanced chemiluminescence (ECL) according to manufacturer’s instructions (Amersham Bioscience). β-actin was used as a gel loading control and was detected using an anti-β-actin antibody (1:5000, Sigma-Aldrich, #A1978). The developed membrane was imaged using the LI-COR Odyssey Quantitative Fluorescence Imaging System. For list of primary antibodies and dilutions see S1 Table.

Bhootada Y., Kotla P., Zolotukhin S., Gorbatyuk O., Bebok Z., Athar M, & Gorbatyuk M. (2016). Limited ATF4 Expression in Degenerating Retinas with Ongoing ER Stress Promotes Photoreceptor Survival in a Mouse Model of Autosomal Dominant Retinitis Pigmentosa. PLoS ONE, 11(5), e0154779.

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Protein Extraction and Western Blot Analysis

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The total protein was extracted via sonication in a protein extraction buffer containing 970 uL of RIPA, 10 uL of 100 mM PMSF, 10 uL of 100 mM EGTA, and a mixture of protease inhibitors (PMSF, TLCK, aprotinin, leupeptin, and pepstatin). The protein concentrations were determined using BioRad Protein Assays and based on the Bradford method of protein quantitation. Next, the proteins (30 ug) were separated in 4–20% Criterion Precast gels and 5% polyacrylamide gels (BioRad), transferred to a polyvinylidene difluoride (PVDF) membrane using the trans-Blot Turbo Transfer System (BioRad), and incubated with primary antibodies overnight at 4° C under agitation. Mouse anti-αS (1:5000; BD Transduction Laboratories, Zymed Laboratories #610787), mouse anti-TH (1:2000; Millipore #MAB318), anti-ATF4 (1:1000; Abcam #ab50546) primary antibodies were used. Goat anti-rabbit (1:10,000, #926-68021), donkey anti-goat (1:10000, #926-32214), and donkey anti-mouse (1:10000, #926-32210) secondary antibodies were used (LI-COR Odyssey). In addition, β-actin was used as the gel loading control, and was detected using an anti-β-actin antibody (1:5000, Sigma-Aldrich, #A1978). Finally, the developed membrane was imaged using the LI-COR Odyssey Quantitative Fluorescence Imaging System.

Gully J.C., Sergeyev V.G., Bhootada Y., Mendez-Gomez H., Meyers C.A., Zolotukhin S., Gorbatyuk M.S, & Gorbatyuk O.S. (2016). Up-regulation of activating transcription factor 4 induces severe loss of dopamine nigral neurons in a rat model of Parkinson’s disease. Neuroscience letters, 627, 36-41.

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Western Blot Analysis of Cell Signaling

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Cell lysates were prepared by scraping cells in lysis buffer (50 mM Tris HCl (pH 8), 150 mM NaCl, 1% Nonidet P40, 0.5% sodium deoxycholate, and 0.1% SDS) containing complete protease inhibitors (Roche) and phosphatase inhibitors (10 mM Sodium Floride and 5 mM Sodium Orthovanadate). Protein concentration was measured by using BCA Protein Assay kit (Pierce). An equal amount of protein (20 μg) was separated by NuPAGE Novex Bis-Tris 4–12% gradient gels (Invitrogen) and then transferred onto a polyvinylidene difluoride membrane (Amersham). Antibodies against FRS2 (sc-8318) were purchased from Santa Cruz Biotechnology. Antibodies for PARP (#9532), phospho-ERK1/2 (#9101), ERK1/2(#9102) were purchased from Cell Signaling Technology and antibody specific for β-actin was obtained from Santa Cruz (sc-8432-HRP).
After incubation with the appropriate HRP-linked secondary antibodies (Bio-Rad), signals were visualized by enhanced chemiluminescence plus Western blotting detection reagents (Amersham). Alternatively, membrane was incubated with IRDye fluorescent secondary antibodies (LI-COR) and visualized by Odyssey quantitative fluorescence imaging system (LI-COR).

Luo L.Y., Kim E., Cheung H.W., Weir B.A., Dunn G.P., Shen R.R, & Hahn W.C. (2014). The tyrosine kinase adaptor protein FRS2 is oncogenic and amplified in high-grade serous ovarian cancer. Molecular cancer research : MCR, 13(3), 502-509.

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Retinal Protein Extraction and Western Blot Analysis

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For the protein extraction, whole retinas were isolated from the enucleated eyes using surgical excision. The total protein was extracted via sonication in a protein extraction buffer containing 970 uL of RIPA, 10 uL of 100 mM PMSF, 10 uL of 100 mM EGTA, and a mixture of protease inhibitors (PMSF, TLCK, aprotinin, leupeptin, and pepstatin). The protein concentrations were determined using BioRad Protein Assays and based on the Bradford method of protein quantitation. Next, the proteins (30–120 ug) were separated in 4–20% Criterion Precast gels and 5% polyacrylamide gels (BioRad), transferred to a polyvinylidene difluoride (PVDF) membrane using the Trans-Blot Turbo Transfer System (BioRad), and incubated with primary antibodies overnight at 4°C under agitation. Goat anti-rabbit (1:10,000, #926-68021), donkey anti-goat (1:10000, #926-32214), and donkey anti-mouse (1:10000, #926-32210) secondary antibodies were used (LI-COR Odyssey). In addition, β-actin, GAPDH, or Tubulin was used as the gel loading control, and was detected using an anti-β-actin antibody (1:5000, Sigma-Aldrich, #A1978) or anti-GAPDH antibody (1:1000, Abcam, #ab9485). Finally, the developed membrane was imaged using the LI-COR Odyssey Quantitative Fluorescence Imaging System.

Lenox A.R., Bhootada Y., Gorbatyuk O., Fullard R, & Gorbatyuk M. (2015). Unfolded Protein Response is Activated in Aged Retinas. Neuroscience letters, 609, 30-35.

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In vitro Permeability Assay of pMBMEC Monolayers

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In vitro permeability of the pMBMEC monolayers was assessed by measuring the clearance of Alexa Fluor 680-labeled 3 kDa dextran (Thermo Fisher Scientific, Carlsbad, CA, USA) and of 0.45 kDa Lucifer Yellow (Sigma-Aldrich Chemie GmbH, Buchs, Switzerland), exactly as described previously (Cecchelli et al., 2014 (link), 1999 (link); Coisne et al., 2005 (link); Steiner et al., 2010 (link)). In brief, the fluorescent tracers diffusing across the pMBMEC monolayers were collected from the bottom well every 20 min for a total of 60 min. Fluorescence intensity for Alexa Fluor 680-labeled 3 kDa dextran and Lucifer Yellow was measured by infrared imaging (Odyssey Quantitative Fluorescence Imaging System, LI-COR, Bad Homburg, Germany) and with a Tecan Infinite M1000 multi-well reader (Tecan Trading AG), respectively. The endothelial permeability coefficient (Pe) was calculated using the clearance principle to obtain a concentration-independent transport parameter, as previously described in detail (Coisne et al., 2005 (link)). The experiments were performed in triplicates for each condition.

Castro Dias M., Odriozola Quesada A., Soldati S., Bösch F., Gruber I., Hildbrand T., Sönmez D., Khire T., Witz G., McGrath J.L., Piontek J., Kondoh M., Deutsch U., Zuber B, & Engelhardt B. (2021). Brain endothelial tricellular junctions as novel sites for T cell diapedesis across the blood–brain barrier. Journal of Cell Science, 134(8), jcs253880.

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