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Odyssey

Manufactured by Bio-Rad
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The Odyssey is a versatile laboratory instrument designed for fluorescence-based detection and quantification of proteins and other biomolecules. It utilizes near-infrared (NIR) fluorescence technology to provide sensitive and accurate analysis. The core function of the Odyssey is to perform Western blotting, ELISA, and other fluorescence-based assays.

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Lab products found in correlation

Pvdf membrane, by Solarbio (1 mentions) Ripa lysis buffer, by Beyotime (1 mentions) Bca protein assay kit, by Solarbio (1 mentions) Nbp1 96 752, by Santa Cruz Biotechnology (1 mentions) Wipi2, by Thermo Fisher Scientific (1 mentions) P62 sqstm1, by Merck Group (1 mentions) Sc 9996, by Cell Signaling Technology (1 mentions) Mini protean precast gel, by Bio-Rad (1 mentions) Tris glycine buffer, by Bio-Rad (1 mentions) Chemidoc, by Bio-Rad (1 mentions) Rabbit anti actin, by Abcam (1 mentions) Mouse anti flag m2, by Merck Group (1 mentions) Mouse anti myc 9e10, by Santa Cruz Biotechnology (1 mentions) Anti rabbit 800cw, by LI COR (1 mentions) Mouse anti pgk1, by Thermo Fisher Scientific (1 mentions) Anti mouse 680lt, by LI COR (1 mentions) Mouse anti ha, by Roche (1 mentions) H4034, by Merck Group (1 mentions) Np 40, by Merck Group (1 mentions) Clarity western ecl substrate solution, by Bio-Rad (1 mentions)

5 protocols using odyssey

1

Western Blot Analysis of TLR3 and IRF3

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Cells were first washed in phosphate-buffered saline (PBS) and lysed in RIPA lysis buffer (Beyotime, China). The samples were left on ice for 30 min and centrifuged at 14,000g for 5 min; the supernatant containing total extracts was collected and assayed for TLR3 and IRF3 protein. Protein concentrations in lysates were determined using the BCA protein assay kit (Solarbio, China). A total of 20 μL of each sample containing 50 μg of protein was run on an 8% SDS, tris-glycine-polyacrylamide gel, and transferred to a PVDF membrane (Solarbio). The membrane was treated with a blocking buffer for 12 h at 4 °C, followed by incubation with rabbit IgG anti-IRF-3 and goat IgG anti-TLR3 at a 1:200 dilution in TBS containing 5% fat-free milk overnight at 4 °C. Subsequently, the membrane was incubated in a 1:2000 dilution of biotin-labeled goat anti-mouse IgG, biotin-labeled donkey anti-goat IgG, or biotin-labeled goat anti-rabbit IgG for 2 h at room temperature (RT). The membrane was washed three times, then scanned with an Odyssey (BIO-RAD) infrared imaging system, and densitometry of individual bands was performed with the Odyssey (BIO-RAD) imaging software. Densitometry was expressed as fold increase of experimental conditions compared with that of the control.
Liu D., Chen Q., Zhu H., Gong L., Huang Y., Li S., Yue C., Wu K., Wu Y., Zhang W., Huang G., Zhang L., Pu S, & Wang D. (2017). Association of Respiratory Syncytial Virus Toll-Like Receptor 3-Mediated Immune Response with COPD Exacerbation Frequency. Inflammation, 41(2), 654-666.
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2

Western Blot Analysis of Autophagy Markers

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For western blot analysis, cells were harvested in 70 μL lysis buffer (3% SDS, 30 mM Tris base, pH 8.8, 5 mM EDTA, 30 mM NaF, 10% glycerol, 1 mM DTT) and 25–50 μg protein with 6x Laemmli buffer was loaded onto 4–20% Bio-Rad Mini- PROTEAN Precast Gels or 12% self-casted acrylamide/bisacrylamide (29:1) gels. After electrophoresis, the proteins were transferred to PVDF membranes with Bio-Rad Tris/Glycine buffer or self-made transfer buffer (25 mM Tris base, 190 mM glycine, 20% methanol, pH 8.3) and stained with the following antibodies: ubiquitin – FK2 clone Millipore, 04–263; mCherry – Novus Biologicals, NBP1-96,752; GFP – Santa Cruz Biotechnology, sc-9996; LC3B – Cell Signaling Technology, 2775; SQSTM1/p62 – Sigma-Aldrich, P0067; ZFTVE1/DFCP1 – Cell Signaling Technology; WIPI2 – Invitrogen; ACTN2 (actinin alpha 2) – Sigma-Aldrich, A2543 or A7811; RPS6 (ribosomal protein S6) – Cell Signaling Technology, 2771; GAPDH – HyTest, 5G4. Western blots were either detected with LI-COR Biosciences Odyssey (Figures 4A, E, G, M and 5D) or Biorad ChemiDoc (Figures 4C, I, J, K and 5E).
Singh S.R., Meyer-Jens M., Alizoti E., Bacon W.C., Davis G., Osinska H., Gulick J., Reischmann-Düsener S., Orthey E., McLendon P.M., Molkentin J.D., Schlossarek S., Robbins J, & Carrier L. (2020). A high-throughput screening identifies ZNF418 as a novel regulator of the ubiquitin-proteasome system and autophagy-lysosomal pathway. Autophagy, 17(10), 3124-3139.
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3

Liver and Cell Protein Analysis

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Protein samples (30-50 μg) were prepared from livers and cells and separated by SDS-PAGE, followed by transfer to polyvinylidene difluoride membranes as reported previously[21 (link)]. Blots were incubated with antibodies (1:1000) against AnxA1 (Abcam, cat: ab214486), α-SMA (50 μL, Affinity Biosciences, Jiangsu, cat: AF1032), β-catenin (50 mL, MedChemExpress, cat: 51067-2-AP) and GAPDH (Abcam, cat: ab181602), followed by incubation with a peroxidase-conjugated goat anti-mouse/rabbit IgG(H + L) (1:5000; Invitrogen, cat: TJ26211). Proteins were visualized using fluorescence scanner imaging system (Odyssey; Bio-Rad, Hercules, CA, United States).
Fan J.H., Luo N., Liu G.F., Xu X.F., Li S.Q, & Lv X.P. (2023). Mechanism of annexin A1/N-formylpeptide receptor regulation of macrophage function to inhibit hepatic stellate cell activation through Wnt/β-catenin pathway. World Journal of Gastroenterology, 29(22), 3422-3439.
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4

Analyzing Snf1 Phosphorylation in Yeast

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To prevent activation of SNF1 by processing of the cells (Wilson et al., 1996 (link)), cells were killed before centrifugation by addition of 1ml 100% TCA to 5ml of cells. Cells were vortexed with glass beads, pelleted, and resuspended in non-fluorescent sample buffer (Licor 928-40004). Protein concentration was determined by the Coomassie elution with SDS method (Marbach et al., 2001 (link)), except that destaining was done with water. Protein extracts were run on 10% (12% or 15% for Mms21-3HA) TGS gels (Biorad) and transferred to PVDF membranes. Phostag (Waco) was added at 0.15ml/10 mix when required. Membranes were probed with mouse anti-Myc (9E10, Santa Cruz), rabbit anti-S-tag (Abcam), rabbit anti-phospho-RxxS (Cell Signaling), mouse anti-HA (Roche or Santa Cruz), mouse anti-FLAG (M2, Sigma), with all antibodies diluted 1000-fold in blocking buffer (Rockland MB-070). Snf1 phosphorylated on T210 (P-Snf1) was detected using rabbit anti-phospho T172 AMPKα (Cell Signaling). Loading controls were detected with rabbit anti-actin (Epitomics, 500-fold diluted) or mouse anti-Pgk1 (Invitrogen, 10000-fold diluted) antibodies. Secondary antibodies were anti-mouse 680LT and anti-rabbit 800CW (LiCOR) or anti-mouse Dylight 488 and anti-rabbit Dylight 549 (Epitomics). Blots were visualized with a LiCOR odyssey or a Biorad imager. Quantifications were performed using NIH ImageJ.
Simpson-Lavy K.J., Bronstein A., Kupiec M, & Johnston M. (2015). Cross-talk between carbon metabolism and the DNA damage response in S. cerevisiae. Cell reports, 12(11), 1865-1875.
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5

Western Blot Protein Analysis

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Cells were washed with ice-cold PBS and lysed with 25 mM Hepes, pH 7.2 (H4034; Sigma-Aldrich), 125 mM potassium acetate (104820; Merck Millipore), 2.5 mM magnesium acetate (105819; Merck Millipore), 5 mM EGTA (E3889; Sigma-Aldrich), 0.5% NP-40 (I18896; Sigma-Aldrich), and 1 mM DTT (D0632; Sigma-Aldrich) supplemented with protease inhibitor cocktail (P9340; Sigma-Aldrich). Cell lysates were then subjected to SDS-PAGE on 10% (567-1034; Bio-Rad) or 4%–20% (567-1094; Bio-Rad) gradient gels and blotted onto Immobilon-P membranes (IPVH00010; Merck Millipore). Membranes incubated with fluorescently labeled secondary antibodies (IRDye680 and IRDye800; LI-COR) were developed by Odyssey infrared scanner (LI-COR). Membranes detected with HRP-labeled secondary antibodies were developed using Clarity Western ECL substrate solutions (Bio-Rad) with a ChemiDoc XRS+ imaging system (Bio-Rad). Quantification of immunoblots was performed using the Odyssey, Volume tools of Image Lab (Bio-Rad), or ImageJ software (National Institutes of Health).
Hong Z., Pedersen N.M., Wang L., Torgersen M.L., Stenmark H, & Raiborg C. (2017). PtdIns3P controls mTORC1 signaling through lysosomal positioning. The Journal of Cell Biology, 216(12), 4217-4233.
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