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Odyssey near infrared imager

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The Odyssey near-infrared imager is a versatile laboratory equipment designed for the detection and analysis of fluorescent and chemiluminescent signals. It utilizes near-infrared light to capture high-resolution images of a wide range of samples, including gels, blots, and microplates.

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Lab products found in correlation

Irdye fluorescently labeled secondary antibodies, by LI COR (4 mentions) Irdye fluorescently labelled secondary antibodies, by LI COR (4 mentions) 6xhis tag, by Abcam (2 mentions) Hybond, by Cytiva (2 mentions) Absorbance microplate reader, by Molecular Devices (2 mentions) Maxisorp microtiter plate, by Thermo Fisher Scientific (2 mentions) Licor dye 800 cw conjugated goat anti mouse, by LI COR (2 mentions) Mouse anti cd9, by Thermo Fisher Scientific (2 mentions) Mouse anti cd63, by Thermo Fisher Scientific (2 mentions) Mouse anti cd81, by Thermo Fisher Scientific (2 mentions) Non fat dry milk, by Bio-Rad (2 mentions) Bovine serum albumin (bsa), by Merck Group (2 mentions) Tween 20, by Merck Group (2 mentions) 0.45 μm nitrocellulose membrane, by Bio-Rad (2 mentions) Bio dot apparatus, by Bio-Rad (2 mentions) Image studio lite software, by LI COR (1 mentions) Irdye 800cw labeled anti rabbit, by LI COR (1 mentions) Irdye 680rd labeled anti mouse, by LI COR (1 mentions) Ab6267, by Abcam (1 mentions) Hybond c extra nitrocellulose, by GE Healthcare (1 mentions)

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Odyssey Imager (606 citations) Odyssey Infrared Imager (593 citations) Infrared imager (13 citations) Odyssey CLx near-infrared imager (6 citations)

20 protocols using odyssey near infrared imager

1

Quantitative Western Blot Analysis

Cited 2 times
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After separation by SDS-PAGE or native-PAGE (see above) the proteins were transferred onto PVDF membranes. The membranes were blocked with 5% (w/v) dried skimmed milk in TBS (25 mM Tris-HCl pH 7.5, 150 mM NaCl) and incubated with primary antibodies followed by IRDye fluorescently labeled secondary antibodies (LiCor). The membranes were scanned with an Odyssey near-infrared imager (LiCor). Primary antibodies and antisera against hamster BiP [chicken anti-BiP; 33 (link)], eIF2α [mouse anti-eIF2α; 34 (link)], and FICD [chicken anti-FICD 12 (link)] were used.
Preissler S., Rato C., Perera L., Saudek V, & Ron D. (2016). FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP. Nature structural & molecular biology, 24(1), 23-29.
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2

Western Blot Immunodetection Protocol

Cited 3 times
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After separation by SDS–PAGE or native-PAGE19 (link) proteins were transferred onto PVDF membranes. The membranes were blocked with 5% (w/v) dried skimmed milk in TBS (25 mM Tris–HCl pH 7.5, 150 mM NaCl) and incubated with primary antibodies diluted in 3% (w/v) BSA in TBS supplemented with 0.1% Tween-20 (TBST). Primary antibodies and antisera against hamster BiP [chicken anti-BiP68 (link)], eIF2α [mouse anti-eIF2α69 (link)] and FICD [chicken anti-FICD3 (link)] were used at a dilutions of 1/1000, 1/5000 and 1/1000 (v/v), respectively. Following the primary antibody incubation, the PVDF membrane was washed with TBST and then incubated with IRDye fluorescently labelled secondary antibodies (LI-COR) at a dilution of 1/2000 (v/v) in a solution of 3% (w/v) dried skimmed milk in TBS. The membranes were scanned with an Odyssey near-infra-red imager (LI-COR). Where applicable, IB band quantification was carried out with Image Studio Lite software (LI-COR).
Perera L.A., Preissler S., Zaccai N.R., Prévost S., Devos J.M., Haertlein M, & Ron D. (2021). Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD. Nature Communications, 12, 5004.
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3

Quantitative Western Blot Analysis

Cited 2 times
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After separation by SDS-PAGE or native-PAGE (see above) the proteins were transferred onto PVDF membranes. The membranes were blocked with 5% (w/v) dried skimmed milk in TBS (25 mM Tris-HCl pH 7.5, 150 mM NaCl) and incubated with primary antibodies followed by IRDye fluorescently labeled secondary antibodies (LiCor). The membranes were scanned with an Odyssey near-infrared imager (LiCor). Primary antibodies and antisera against hamster BiP [chicken anti-BiP; 33 (link)], eIF2α [mouse anti-eIF2α; 34 (link)], and FICD [chicken anti-FICD 12 (link)] were used.
Preissler S., Rato C., Perera L., Saudek V, & Ron D. (2016). FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP. Nature structural & molecular biology, 24(1), 23-29.
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4

Western Blot Analysis of DNM3 Protein

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Cell lysates containing protein (10 μg) were resolved by SDS-PAGE and transferred onto PVDF membranes. Immunoblotting was carried out using a rabbit polyclonal DNM3 antibody (LSBio LS-C409118) or mouse β-actin antibody (Abcam ab6267). Primary antibodies were used at 1:1000 dilution. Secondary antibodies (IRDye 800CW-labeled anti-rabbit; IRdye 680RD-labeled anti-mouse; LI-COR Biosciences) were used at 1:10,000 dilution following the manufacturer’s recommendation. Immunoblot images were generated using the LI-COR Odyssey near-infrared imager. Protein band density was quantified using LI-COR software.
Shepherdson J.L., Zheng H., Amarillo I.E., McAlinden A, & Shinawi M. (2020). Delineation of the 1q24.3 microdeletion syndrome provides further evidence for the potential role of non-coding RNAs in regulating the skeletal phenotype. Bone, 142, 115705.
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5

Western Blot Analysis of ER Stress Markers

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Proteins were separated by SDS-PAGE or native-PAGE and transferred to PVDF membranes. The membranes were blocked with 5% (w/v) dried skimmed milk in TBS (25 mM Tris-HCl pH 7.5, 150 mM NaCl) and probed with primary antibodies followed by IRDye fluorescently labeled secondary antibodies (Li-Cor, UK). The membranes were scanned with an Odyssey near-infrared imager (Li-Cor) and where indicated densitometric quantification of the immunoblot signals was performed with ImageJ (NIH). Primary antibodies and antisera against hamster BiP [chicken anti-BiP; (Avezov et al., 2013 (link))], eIF2α [mouse anti-eIF2α; (Scorsone et al., 1987 (link))], phosphorylated eIF2α [rabbit anti-eIF2α Phospho (pS51); Epitomics cat. # 1090-1, UK], and FICD [rabbit anti-FICD; LifeSpan BioSciences cat. # LS-C80941, UK or chicken anti-FICD (see below)] were used.
Preissler S., Rato C., Chen R., Antrobus R., Ding S., Fearnley I.M, & Ron D. (2015). AMPylation matches BiP activity to client protein load in the endoplasmic reticulum. eLife, 4, e12621.
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6

Western Blot Visualization of 6xHis-tagged Proteins

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Samples were resolved on Novex NuPage 10% Bis-Tris SDS-PAGE gels (Invitrogen) before transferring to Hybond-C Extra nitrocellulose (GE Healthcare). Membranes were probed with rabbit antiserum directed against 6xHis-tag (1:5000, Abcam), followed by goat anti-rabbit IRDye conjugated secondary antibody (1:7500, LI-COR Biotechnology). Blots were visualized using an Odyssey near-infrared imager (LI-COR Biotechnology).
Donahue E.H., Dawson L.F., Valiente E., Firth-Clark S., Major M.R., Littler E., Perrior T.R, & Wren B.W. (2014). Clostridium difficile has a single sortase, SrtB, that can be inhibited by small-molecule inhibitors. BMC Microbiology, 14, 219.
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7

Protein Detection by Western Blot

Cited 1 time
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Preparations were run on 12% Novex NuPAGE Bis-Tris SDS-PAGE gels (Life Technologies) before being transferred to Hybond-C Extra nitrocellulose membrane (GE Healthcare). Membranes were probed with mouse antiserum against 6xHisTag (1:5000, Abcam), or mouse antiserum against CD283120 (link), followed by goat anti-mouse IRDye conjugated secondary antibody (1:2000, LI-COR Biotechnology). Blots were visualised with an Odyssey near-infrared imager (LI-COR Biotechnology).
Shaw H.A., Khodadoost L., Preston M.D., Corver J., Mullany P, & Wren B.W. (2019). Clostridium difficile clade 3 (RT023) have a modified cell surface and contain a large transposable island with novel cargo. Scientific Reports, 9, 15330.
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8

Quantitative Analysis of UGDH Oligomerization

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SDS-PAGE gels from the crosslinking procedure were either stained with Gel Code Blue or analyzed by western blot probed with anti-UGDH rabbit polyclonal antibody. For western blots, indicated fractions were transferred to PVDF membranes and blocked with Pierce Superblock reagent before incubation with anti-UGDH primary at a dilution of 1:1000. Membranes were washed and proteins detected by secondary incubation with IRDye 800 conjugated anti-rabbit IgG (Rockland, Gilberstville, PA, 1:5000). Images were captured in the 800-channel of the Odyssey Near Infrared Imager and analyzed using the Image Studio Lite program (LI-COR Biosciences). We quantified the fluorescence intensity of bands representing monomeric and oligomeric UGDH. By dividing the total of each oligomeric species by the total intensity of all species, we obtained a normalized percentage of crosslinking efficiency. Dynamic range of the instrument was determined by similar analysis of a standard curve consisting of 12 concentrations of purified wild-type UGDH spanning 0.1 ng to 10 μg. All values for western imaging were analyzed in the linear range of the standard curve by adjusting the instrument settings appropriately and loading equal volumes from each sample such that the highest protein concentration per fraction loaded was ≤10 μg.
Grady G., Thelen A., Albers J., Ju T., Guo J., Barycki J.J, & Simpson M.A. (2016). Inhibiting hexamer disassembly of human UDP-glucose dehydrogenase by photoactivated amino acid crosslinking. Biochemistry, 55(22), 3157-3164.
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9

Western Blot Detection of Protein Markers

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After separation by SDS-PAGE, the proteins were transferred onto PVDF membranes. Membranes were blocked with 5% (w/v) dried skimmed milk in TBS (25 mM Tris-HCl pH 7.5, 150 mM NaCl) and incubated with primary antibodies followed by IRDye fluorescently labelled secondary antibodies (LI-COR). Membranes were scanned with an Odyssey near-infrared imager (LI-COR). Primary antibodies against hamster BiP (chicken anti-BiP, 1:2000;48 (link)), actin (mouse anti-actin, 1:2000; Abcam, cat. # AB3280), MANF (chicken anti-MANF, 1:1000; see below), FLAG-M1 (mouse anti-FLAG-M1, 1:1000; Sigma, cat. # F3040), and A1AT (mouse anti-A1AT monoclonal, 1:5000; Abcam, cat. # AB9399) were used.
Yan Y., Rato C., Rohland L., Preissler S, & Ron D. (2019). MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP. Nature Communications, 10, 541.
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10

Protein Separation and Immunoblot Analysis

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Purified acceptor proteins were separated by SDS-PAGE using NuPAGE™ Novex™ 4-12 % Bis-Tris protein gels (Invitrogen), transferred to nitrocellulose membrane and analysed by two colour immunoblot using anti-hexahistidine, anti-glycan and corresponding fluorescent-labelled secondary antibodies (Table III) using an Odyssey near-infrared imager (LiCOR biosciences).
Mills D.C., Jervis A.J., Abouelhadid S., Yates L.E., Cuccui J., Linton D, & Wren B.W. (2015). Functional analysis of N-linking oligosaccharyl transferase enzymes encoded by deep-sea vent proteobacteria. Glycobiology, 26(4), 398-409.
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