Odyssey ir imaging system

Manufactured by LI COR

Sourced in United States, United Kingdom, Niger

The Odyssey IR Imaging System is a high-performance near-infrared fluorescence imaging platform designed for a wide range of applications in life science research. It features dual-channel detection capabilities, allowing for the simultaneous visualization and quantification of two target molecules within a single experiment. The system utilizes infrared fluorescence technology to provide sensitive and specific detection, enabling researchers to obtain precise and reliable data.

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Lab products found in correlation

Pierce bca protein assay kit, by Thermo Fisher Scientific (24 mentions) Odyssey blocking buffer, by LI COR (10 mentions) 0.2 μm nitrocellulose membrane, by Bio-Rad (8 mentions) Blocking buffer, by LI COR (6 mentions) Nitrocellulose membrane, by Bio-Rad (5 mentions) Ripa buffer, by Merck Group (5 mentions) Irdye 680, by LI COR (5 mentions) β actin, by Cell Signaling Technology (5 mentions) β actin, by Merck Group (5 mentions) Irdye 800 dye, by LI COR (4 mentions) Irdye 800cw goat anti rabbit igg, by LI COR (3 mentions) Ib401001, by Thermo Fisher Scientific (3 mentions) Protease and phosphatase inhibitor, by Merck Group (3 mentions) Protease inhibitor, by Roche (3 mentions) Irdye 800cw, by LI COR (3 mentions) Pierce ecl western blotting substrate kit, by Thermo Fisher Scientific (3 mentions) Immune blot pvdf membrane, by Bio-Rad (3 mentions) Mini protean tgx gel, by Bio-Rad (3 mentions) Goat anti rabbit igg hrp, by Southern Biotech (3 mentions) Irdye 680lt goat anti mouse igg, by LI COR (2 mentions)

Close spelling variants of this product

LI-COR Odyssey IR Imaging System V3.0 Odyssey IR imaging system and software Two-channel (red and green) Odyssey CLx near-IR fluorescence imaging system Odyssey CLx near-IR fluorescence imaging system Odyssey infrared (IR) imaging system Odyssey CLx IR Imaging System Two-channel (red and green) IR fluorescent Odyssey CLx imaging system Odyssey imaging system Odyssey system

133 protocols using odyssey ir imaging system

Exosomal Protein Markers and Telomerase Analysis

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Verification of the extracted exosomes was determined by Western blotting using antibodies against well-characterized exosomal protein markers: CD63, CD9 and TSG101. Extracted exosomes were resuspended in RIPA buffer, sonicated and quantified using Pierce BCA Protein Assay Kit (Thermo Scientific, MA, USA). 50μg of protein was subjected to 10% Sodium Dodecyl Sulfate Poly Acrylamide gel electrophoresis (SDS-PAGE) and transferred to a nitrocellulose membrane. The membrane was then hybridized for 16h at 4°C with antibodies against exosomal markers: anti-CD63, anti-CD9 (1:1000, Santa Cruz Biotech, TX, USA) and anti-TSG101 (1:500, Abcam MA, USA). In the following day the membrane was subjected to fluorescent labeled secondary antibodies. Visualization was done by the Odyssey analysis software (Odyssey IR imaging system; LI-COR).
The levels of telomerase in pHFF cell line were evaluated by Western blotting as well. The cells were grown for 72hr in the presence of Jurkat derived exosomes. 50 μg of protein were separated by 10% SDS-PAGE, transferred to nitrocellulose membrane and hybridized for 16h at 4°C with specific antibodies: anti-telomerase (1:500, Abcam, MA, USA) Signals were visualized after exposing the membranes to 2^nd fluorescent antibodies and quantified by the Odyssey analysis software (Odyssey IR imaging system; LI-COR).

Gutkin A., Uziel O., Beery E., Nordenberg J., Pinchasi M., Goldvaser H., Henick S., Goldberg M, & Lahav M. (2016). Tumor cells derived exosomes contain hTERT mRNA and transform nonmalignant fibroblasts into telomerase positive cells. Oncotarget, 7(37), 59173-59188.

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Protein Extraction and Western Blot

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Lysates were collected in 1% NP-40, 150 mM NaCl, 50 mM Tris-HCl pH 8.0,
10% glycerol, 0.1% SDS, and 0.5% Na-deoxycholate supplemented with the protease
and phosphatase inhibitor HALT (Thermo Fisher Scientific). Pre-aliquoted SDS and
DTT from New England Biolabs (B7703) were added to the lysate, and proteins were
denatured at 100˚C for five minutes. Proteins were then separated by
SDS-PAGE and transferred to a nitrocellulose membrane via either the iBlot dry
transfer system (Invitrogen) or overnight at 30 V in transfer buffer containing
10% MeOH and 1× Tris-Glycine. Antibody binding was detected using the
LI-COR Odyssey IR imaging system (LI-COR Biosciences).

Cai D., Choi P.S., Gelbard M, & Meyerson M. (2019). Identification and characterization of oncogenic SOS1 mutations in lung adenocarcinoma. Molecular cancer research : MCR, 17(4), 1002-1012.

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Detecting Cav2.2-α Protein in Small Samples

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Due to the limitation of small AVG samples (1‐2 mg wet weight), we could not detect the expression of Ca_v2.2‐α protein using regular Western blot analyses and instead employed a modified reverse‐phase protein microarray, which is highly sensitive and needs about 1 μg protein.31 Briefly, total protein concentration of AVG samples was determined using a bicinchoninic acid protein assay kit (Pierce, Rockford, IL). Fifty nanoliters of each protein sample was loaded onto nitrocellulose‐coated glass slides by an 8‐pin arrayer. After protein samples were sequentially incubated with primary antibodies (rabbit anti‐Ca_v2.2‐α antibody and mouse anti‐β‐actin antibody) and LI‐COR fluorescence‐conjugated secondary antibodies (IRDye 800CW goat anti‐rabbit IgG and IRDye 680LT goat anti‐mouse IgG), the protein signals were scanned with a LI‐COR Odyssey IR imaging system (LI‐COR, Lincoln, NE). Before reverse‐phase protein microarray was performed, Western blot analysis was used to validate target specificity of Ca_v2.2‐α antibody by blocking with antigen peptide to confirm elimination of specific signal and testing against tissues known to express (rat brain) or not express Ca_v2.2‐α protein (rat gastrocnemius muscle) (Figure 2).

Zhang D., Tu H., Cao L., Zheng H., Muelleman R.L., Wadman M.C, & Li Y. (2018). Reduced N‐Type Ca2+ Channels in Atrioventricular Ganglion Neurons Are Involved in Ventricular Arrhythmogenesis. Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 7(2), e007457.

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Western Blot Analysis of HAS2 in AoSMCs

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Proteins were collected from treated or untreated AoSMCs by using RIPA buffer supplemented with 10% of protease inhibitors (Sigma) and separated on precast 4–12% gradient acrylamide gels (Genscript) at 120 V in 1× Mops Buffer (Genscript). Protein samples were transferred to nitrocellulose membrane at 250 mA for 1 h at 4 °C, blocked in 5% BSA, 0.1% TBS-Tween 20 for 1 h, and incubated with primary antibody overnight at 4 °C. After extensive washing, the membranes were incubated with primary antibody and with horseradish peroxidase–conjugated secondary antibody. Chemiluminescence was detected using the LiteAblot® turbo chemiluminescent substrate (Euroclone), and bands were revealed using the LI-COR Odyssey® IR imaging system (LI-COR Biosciences). Western blotting experiments were done using antibodies against HAS2 (polyclonal Y14, sc34068, Santa Cruz Biotechnology), GAPDH (polyclonal V18, sc20357, Santa Cruz Biotechnology), and α-tubulin (monoclonal 11H10, Cell Signaling).

Caon I., Bartolini B., Moretto P., Parnigoni A., Caravà E., Vitale D.L., Alaniz L., Viola M., Karousou E., De Luca G., Hascall V.C., Passi A, & Vigetti D. (2020). Sirtuin 1 reduces hyaluronan synthase 2 expression by inhibiting nuclear translocation of NF-κB and expression of the long-noncoding RNA HAS2–AS1. The Journal of Biological Chemistry, 295(11), 3485-3496.

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Immunofluorescent Staining of CXCL4

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Following treatments, cells were fixed with 4% NBF for 15 minutes before incubation with blocking buffer (phosphate-buffered saline, normal goat serum, water, and Triton X-100). Cells were treated with rabbit polyclonal anti-CXCL4 (1:25; Abcam) and mouse monoclonal anti–β-tubulin (1:1000; Sigma-Aldrich) antibodies overnight at 4°C. Cells were washed before incubation with goat anti-rabbit IRDye 800CW (Molecular Probes, Eugene, OR) and goat anti-mouse Alexa Fluor 680 (LI-COR Biosciences, Lincoln, NE). The LI-COR Odyssey IR Imaging System was used to analyze results.

Maybin J.A., Thiruchelvam U., Madhra M., Saunders P.T, & Critchley H.O. (2017). Steroids Regulate CXCL4 in the Human Endometrium During Menstruation to Enable Efficient Endometrial Repair. The Journal of Clinical Endocrinology and Metabolism, 102(6), 1851-1860.

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Sensitive Protein Detection in Microgram Samples

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Due to the limitation of small AVG samples (1–2 mg wet weight), we could not detect the expression of catalase protein using regular Western blot analyses and instead employed a modified reverse–phase protein microarray, which is highly sensitive and needs about 1 μg of protein (23 (link), 67 (link)). AVGs were rapidly removed, immediately frozen in liquid nitrogen, and stored at −80°C until analyzed. Proteins in AVG homogenates were extracted with a lysing buffer (10 mM Tris, 1 mM EDTA, 1% SDS; pH 7.4) plus protease inhibitor cocktail (100 μl/ml, Sigma). After centrifugation at 12,000 g for 20 min at 4°C, the protein concentration in the supernatant was determined using a bicinchoninic acid protein assay kit (Pierce, Rockford, IL, USA). Fifty nanoliters of each protein sample were loaded onto nitrocellulose–coated glass slides by an 8–pin arrayer. Protein samples were then sequentially incubated with primary antibodies (rabbit anti-Catalase (D5N7V) antibody, #14097s, Cell Signaling; rabbit anti-CACNA1B (CaV2.2-α) antibody, #ACC-002, Alomone Labs; and mouse anti–β-actin antibody, Sc-4778, Santa Cruz Biotechnology) and LI–COR fluorescence–conjugated secondary antibodies (IRDye 800CW goat anti–rabbit IgG, and IRDye 680LT goat anti–mouse IgG). The protein signals were scanned with a LI–COR Odyssey IR imaging system (LI–COR, Lincoln, NE, USA).

Zhang D., Tu H., Hu W., Duan B., Zimmerman M.C, & Li Y.L. (2022). Hydrogen Peroxide Scavenging Restores N-Type Calcium Channels in Cardiac Vagal Postganglionic Neurons and Mitigates Myocardial Infarction-Evoked Ventricular Arrhythmias in Type 2 Diabetes Mellitus. Frontiers in Cardiovascular Medicine, 9, 871852.

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Western Blot Protein Detection

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Samples were loaded onto 8% SDS-polyacrylamide gels or 4–12% Tris/HEPES-SDS Bolt^TM precast gels (Thermo-Invitrogen) for electrophoresis. The size-separated proteins were then transferred to nitrocellulose membranes (Bio-Rad). Primary antibodies (described above) and IRdye800-conjugated secondary antibodies were used to detect target proteins. Signal was detected using the LI-COR Odyssey IR imaging system (LI-COR Biosciences). Quantification of the intensity of the bands was obtained using Odyssey 2.0 software (LI-COR Biosciences).

Sarkar S.K., Foo A.C., Matyas A., Asikhia I., Kosenko T., Goto N.K., Vergara-Jaque A, & Lagace T.A. (2020). A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles. The Journal of Biological Chemistry, 295(8), 2285-2298.

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Western Blot Analysis of Cellular Proteins

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Western blot analysis was performed as described previously (28 (link)). Cells were lysed in RIPA buffer (R0278; Sigma-Aldrich, Merck Millipore, Darmstadt, Germany) and the total cellular protein was resolved on denaturing polyacrylamide gels, transferred to nitrocellulose membranes (Bio-Rad Laboratories, Inc., Hercules, CA, USA), and blotted with primary antibodies. The dilution and catalog no. of primary antibodies used in the present study are listed in Table II. Protein-antibody complexes were visualized using secondary antibodies conjugated with Cy5.5 (catalog. no. RPN998; 1:10,000 dilution; GE Healthcare Life Sciences) and visualized by LI-COR Odyssey IR Imaging System (LI-COR Biosciences, Lincoln, NE, USA).

Lv J., Zhu P., Zhang X., Zhang L., Chen X., Lu F., Yu Z, & Liu S. (2017). PCDH9 acts as a tumor suppressor inducing tumor cell arrest at G0/G1 phase and is frequently methylated in hepatocellular carcinoma. Molecular Medicine Reports, 16(4), 4475-4482.

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Peritoneal Macrophage Cultures: COX2 Detection

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Peritoneal macrophage cultures were also extracted for protein analysis to detect PGS2/COX2. Cultures of 5 × 10⁶ lavage cells were incubated for 1 hour at 37°C/5% CO₂ to allow for macrophage adhesion. Nonadherent cells were washed off with sterile 1 × PBS and the adherent cells extracted by sonication in SDS lysis buffer (Upstate/Millipore) + protease inhibitors (Roche). Extracts were frozen at −80°C until analysis. Thawed extracts were resuspended with 5 × Leammli sample buffer (Tris–HCL [pH 6.5], 50% glycerol, 1% SDS, 1% 2-mercaptoethanol, 0.1% bromophenol blue, made with reagents from Fisher Scientific, Pittsburgh, PA, USA) and heated to 100°C for 3 minutes. Fifty microliters of each sample was run on 4%–20% acrylamide gels and transferred to Odyssey polyvinylidene floride (PVDF) membranes for western blot analysis using anti-COX2 polyclonal antibodies from Cayman Chemicals (Ann Arbor, MI, USA) and detection using the Li-Cor anti-Rabbit IR700 dye conjugates fluorescence at 700 nm on a Li-Cor Odyssey IR Imaging system (Li-Cor Biosciences, Lin-coln, NE, USA).

Garrigan E., Belkin N.S., Seydel F., Han Z., Carter J., McDuffie M., Morel L., Peck A.B., Clare-Salzler M.J., Atkinson M., Wasserfall C., Davoodi-Semiromi A., Shi J.D., Haskell-Luevano C., Yang L.J., Alexander J.J., Cdebaca A., Piliant T., Riggs C., Amick M, & Litherland S.A. (2015). Csf2 and Ptgs2 Epigenetic Dysregulation in Diabetes-prone Bicongenic B6.NODC11bxC1tb Mice. Genetics & Epigenetics, 7, 5-17.

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Immunoblotting for Protein Analysis

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Cells were treated with various drug concentrations, as indicated in the figure legends. Samples were isolated at the indicated times and SDS–PAGE and immunoblotting was performed as described in Booth et al. (2014a (link),b (link),c (link),d) (link). Immunoblots were observed by using an Odyssey IR imaging system (LI-COR Biosciences, Lincoln, NE).

Booth L., Roberts J.L., Tavallai M., Nourbakhsh A., Chuckalovcak J., Carter J., Poklepovic A, & Dent P. (2015). OSU‐03012 and Viagra Treatment Inhibits the Activity of Multiple Chaperone Proteins and Disrupts the Blood–Brain Barrier: Implications for Anti‐Cancer Therapies. Journal of Cellular Physiology, 230(8), 1982-1998.

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