Theodyssey infrared imaging system

Manufactured by LI COR

The Odyssey Infrared Imaging System is a lab equipment product designed for high-performance infrared imaging. It captures and analyzes infrared signals, enabling researchers to visualize and quantify a variety of biological and chemical samples.

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Lab products found in correlation

Odyssey software, by LI COR (2 mentions) P stat5, by Cell Signaling Technology (1 mentions) Stat5, by Cell Signaling Technology (1 mentions) Antibodies against mcl 1, by Santa Cruz Biotechnology (1 mentions) 4e bp1, by Cell Signaling Technology (1 mentions) P akt, by Cell Signaling Technology (1 mentions) Bcl xl, by Cell Signaling Technology (1 mentions) P 4ebp1, by Cell Signaling Technology (1 mentions) P erk, by Cell Signaling Technology (1 mentions) Polyvinylidene fluoride membrane, by Thermo Fisher Scientific (1 mentions) Alexa fluor 680 fluorophore, by Thermo Fisher Scientific (1 mentions) Nupage novex bis tris gel, by Thermo Fisher Scientific (1 mentions) Precision plus protein kaleidoscope standard, by Bio-Rad (1 mentions) Anti gapdh, by LI COR (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Pierce s nitrosylation western blot kit, by Thermo Fisher Scientific (1 mentions) Phenylmethanesulfonyl fluoride pmsf, by Merck Group (1 mentions) Ripa lysis buffer, by Beyotime (1 mentions)

Close spelling variants of this product

TheOdyssey Imaging System Infrared imaging system

5 protocols using theodyssey infrared imaging system

Quantitative Western Blot Analysis of Signaling Pathways

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Western blot was performed as previously described (4 (link)). Antibodies against FAK (cat#13009s), p-STAT5
(cat#9351s), STAT5 (cat#9363s), p-AKT (cat#4060s), AKT (cat#2920s), BCL-XL
(cat#2764s), p-ERK (cat#4370s), 4EBP1 (cat#9644), and p-4EBP1 (cat#2855) were
purchased from Cell Signaling Technology (Danvers, MA). Antibodies against MCL-1
(cat#sc-819) and BCL-2 (cat#M0887) were purchased from Santa Cruz Biotechnology
(Santa Cruz, CA) and DAKO (Carpentaria, CA), respectively. β-actin or
α-tubulin was used as a loading control. Signals were detected using the
Odyssey Infrared Imaging System (LI-COR Biosciences, Lincoln, NE) and quantified
using Odyssey software (version 3.0, LI-COR Biosciences).

Wang X., Mak P.Y., Mu H., Tao W., Rao A., Visweswaran R., Ruvolo V., Pachter J.A., Weaver D.T., Andreeff M., Xu B, & Carter B.Z. (2020). Combinatorial inhibition of focal adhesion kinase and BCL-2 enhances anti-leukemia activity of venetoclax in acute myeloid leukemia. Molecular cancer therapeutics, 19(8), 1636-1648.

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Chrysin Modulates RANKL-induced Osteoclastogenesis

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BMMs were seeded in 6-well plates and maintained until >90% confluence. Cells were serum-starved for 2 h. The treatment group was treated with 20 μM CHR for 2 h, subsequent by stimulation with RANKL at a concentration of 100 ng/ml in time points (discarding RANKL at 5, 10, 20, 30, or 60 min). To explore the effect of Chrysin on RANKL-induced osteoclast signaling events, nuclear and cytoplasmic proteins were extracted from BMMs after combination of stimulation presence or absence 20 μM CHR for 1, 3, or 5 days together with RANKL. Untreated cells served as control. Total cellular protein from each sample was extracted using RIPA buffer contained with PMSF and phosphatase inhibitor. Next, 20 µg of total cellular protein lysate transfected with nitrocellulose membrane by 10% SDS-PAGE. Subsequently, the 5% BSA in TBST (50 mM Tris, pH 7.6; 150 mM NaCl; and 0.1% Tween-20) were used incubated with membrane for one and a half hours and incubated with primary antibody (1:1000) for 12–15 h at 4°C. Subsequently, the membranes were washed 3 times with TBST, and incubated with the IRDye fluorescent secondary antibody corresponding to the primary antibody for 1 h at room temperature. The immuno-reactive bands were analyzed using The Odyssey Infrared Imaging System (LI-COR).

Wu Z., Li C., Chen Y., Liu Q., Li N., He X., Li W., Shen R., Li L., Wei C., Shao S., Fu F., Ding J., Sun X., Wang D., Yuan G., Su Y., Zhao J., Xu J., Xu R., Xu X, & Xu F. (2022). Chrysin Protects Against Titanium Particle-Induced Osteolysis by Attenuating Osteoclast Formation and Function by Inhibiting NF-κB and MAPK Signaling. Frontiers in Pharmacology, 13, 793087.

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Biotinylated Protein Visualization

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Biotinylated
proteins were resolved using 10% NuPAGE Novex BisTris gel (Life Technologies,
Carlsbad, CA). Precision Plus Protein Kaleidoscope standards (10–250
kDa, Bio-Rad) were electrophoresed on the same gel for reference.
The proteins were transferred electrophoretically to a polyvinylidene
fluoride membrane (Life Technologies, Grand Island, NY) and probed
with streptavidin conjugated with the Alexa Fluor 680 fluorophore
(Life Technologies). Biotinylated proteins were visualized using the
Odyssey Infrared Imaging System and Odyssey software according to
the manufacturer (Licor, Lincoln, NE). Integrated intensities were
obtained using the Odyssey software.

Windsor K., Genaro-Mattos T.C., Miyamoto S., Stec D.F., Kim H.Y., Tallman K.A, & Porter N.A. (2014). Assay of Protein and Peptide Adducts of Cholesterol Ozonolysis Products by Hydrophobic and Click Enrichment Methods. Chemical Research in Toxicology, 27(10), 1757-1768.

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Protein Extraction and Detection

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Cell lysates were prepared by using a RIPA lysis buffer (Beyotime, Shanghai, China) supplemented with Protease Inhibitor Cocktail (PIC, Sigma-Aldrich), Phenyl-methane Sulfonyl Fluoride (PMSF, Sigma-Aldrich), and Phosphatase Inhibitor Cocktail (PhoIC A and B, Sigma-Aldrich). Equal amounts of protein of each sample were analyzed using SDS-PAGE, electrophoretic transfer, immunoblotting, and chemiluminescence detection. Either 10% or 12% SDS-PAGE was used to isolate proteins with different molecular weights. The proteins were transferred to a nitrocellulose filter membrane (PALL). Antibodies and dilutions were as follows: anti-VEGFD, 1:1000; anti-PECAM-1, 1:1000; anti-LYVE1, 1:1000; anti-FLK-1, 1:1000; anti-VEGFR3, 1:1000; anti-HA, 1:1000; anti-Flag, 1:500; anti-Myc, 1:1000; anti-GAPDH, 1:5000; anti-GSNOR, 1:2000; The Odyssey Infrared Imaging System (LI-COR Bioscience, Lincoln, Nebraska) was used to detect the immunoreactive signals. Western blot bands were quantified by measuring integrated density using the Image-J software (NIH, USA). Co-immunoprecipitation was performed through the cell lysates, and the supernatants were incubated with antibody and protein A/G PLUS-Agarose (Santa Cruz) overnight at 4℃. The bound proteins were eluted in the loading buffer and subjected to the SDS-PAGE. S-nitrosylated proteins were detected by Pierce™ S-nitrosylation Western Blot Kit (Thermo).

He Q., Qu M., Shen T., Xu Y., Luo J., Tan D., Xu C., Barkat M.Q., Zeng L.H, & Wu X. (2022). Suppression of VEGFD expression by S-nitrosylation promotes the development of lung adenocarcinoma. Journal of Experimental & Clinical Cancer Research : CR, 41, 239.

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LFA-1-Mediated Adhesion Dynamics

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Petri dishes were coated overnight with goat-anti human IgG and rICAM-1, or with
poly-L-lysine (control). Jurkat cells (3.5*10⁶ cells/group) were
washed, resuspended in CMF-PBS or LFA-1 activation buffer, and allowed to adhere
to the coated Petri dishes for various time points (0–60 min) at 37°C. Cells
were lysed in RIPA buffer (50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM NaF, 1 mM
NaVO₃, 0.1% SDS, 0.1% sodium deoxycholate, 1% NP40) containing
cOmplete mini protease inhibitor, and total protein was quantified by Bradford
assay (BioTek, Winooski, VT). 20 μg total protein, boiled for 5 min in loading
buffer, was subjected to SDS-PAGE. Membranes were stained with primary antibody
(1 μg) overnight at 4°C followed by Alexa 680- or IR800-conjugated secondary
antibody (1:10000) for 1 h at room temperature. Signals were detected with the
Odyssey infrared imaging system (LI-COR, Lincoln, NE).

Rao G.K., Wong A., Collinge M., Sarhan J., Yarovinsky T.O., Ramgolam V.S., Gaestel M., Pardi R, & Bender J.R. (2018). T cell LFA-1-induced proinflammatory mRNA stabilization is mediated by the p38 pathway kinase MK2 in a process regulated by hnRNPs C, H1 and K. PLoS ONE, 13(7), e0201103.

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