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Odyssey fc machine

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The Odyssey Fc machine is a fluorescence imaging system designed for a variety of applications, including Western blotting, multiplex fluorescence, and chemiluminescence detection. The system utilizes high-sensitivity, long-life fluorescence detection and supports a range of fluorescent dyes and labels. It provides accurate and quantitative analysis of protein and nucleic acid samples.

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Lab products found in correlation

Mcf 7, by American Type Culture Collection (2 mentions) Proteinase inhibitor, by Thermo Fisher Scientific (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Ripa buffer, by Thermo Fisher Scientific (2 mentions) Ab37185, by Abcam (1 mentions) A5441, by Merck Group (1 mentions) Zr 75 1, by American Type Culture Collection (1 mentions) Mda mb 436, by American Type Culture Collection (1 mentions) Hcc1500, by American Type Culture Collection (1 mentions) Nc membrane, by Thermo Fisher Scientific (1 mentions) Ppaxillin, by Thermo Fisher Scientific (1 mentions) P fak, by Abcam (1 mentions) Claudin 1, by Cell Signaling Technology (1 mentions) Lysis buffer, by Roche (1 mentions) Anti β actin, by Abcam (1 mentions) Ab5176, by Abcam (1 mentions) Immobilon western substrate, by Merck Group (1 mentions) Ab11174, by Abcam (1 mentions) Immobilon p, by Merck Group (1 mentions) Sc 1615, by Abcam (1 mentions)

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Odyssey Fc (329 citations) Odyssey machine (29 citations)

14 protocols using odyssey fc machine

1

Mitotic Chromosome Isolation from HeLa Cells

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For the analysis of mitotic chromosomes, HeLa cells were synchronized with 2 mM thymidine for 18 h. Cells were released from thymidine into fresh medium, and 6 h later, 0.1 µg/ml nocodazole was added to cells. 4 h after nocodazole addition, mitotic cells were collected by mitotic shake-off and released with 7 µM ICRF-193–containing fresh medium for 20 min. For mitotic chromosome isolation, cells were lysed with lysis buffer (250 mM sucrose, 20 mm Hepes, 100 mM NaCl, 1.5 mM MgCl2, 1 mM EDTA, 1 mM EGTA, 0.2% Triton X-100, 1:2,000 lysophosphatidylcholine, and 15 mM iodoacetic acid), and lysed cells were layered on a 40% glycerol cushion as for chromosome isolation from XEEs. Later, isolated mitotic chromosomes were boiled in SDS-PAGE sample buffer, resolved on 8–16% gradient gels, and subjected to immunoblotting with the indicated antibodies. Signals were acquired using a LI-COR Odyssey Fc machine.
Pandey N., Keifenheim D., Yoshida M.M., Hassebroek V.A., Soroka C., Azuma Y, & Clarke D.J. (2019). Topoisomerase II SUMOylation activates a metaphase checkpoint via Haspin and Aurora B kinases. The Journal of Cell Biology, 219(1), e201807189.
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2

SLC7A11 Antibody Specificity Validation

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SLC7A11 primary antibody specificity (Rabbit monoclonal, Ab37185, Abcam, UK) was determined using Western blotting in cell line lysates: HCC1500, ZR-751, MDA-MB-436, MCF7 and T47D (American Type Culture Collection; Rockville, MD, USA at a dilution of 1:2000. Donkey anti-rabbit (1:15,000, IRDye680 CW, 926–32213, LI-COR Bioscience) was used as a fluorescent secondary antibody. Mouse monoclonal anti-β-actin primary antibody (1:5,000, A5441, Sigma-Aldrich) with donkey anti-mouse fluorescent secondary (1:15,000, IRDye 800CW, 926–68072, LI-COR Bioscience) was used as a control. The Odyssey Fc machine (LI-COR Bioscience) was used to visualize blots showing specific bands at the predicted size of approximately 55 KDa (Supplementary Figure S1).
Nath P., Alfarsi L.H., El-Ansari R., Masisi B.K., Erkan B., Fakroun A., Ellis I.O., Rakha E.A, & Green A.R. (2023). The amino acid transporter SLC7A11 expression in breast cancer. Cancer Biology & Therapy, 25(1), 2291855.
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3

Protein Expression Analysis of Cell Lines

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Cells were lysed with lysis buffer (Roche), with 10% phosphor STOP and 10% protease inhibitor cocktail. Cell lysates were then collected after centrifugation at 12,000 rpm for 10 m at 4°C. 30μg of lysate protein was loaded and total cellular protein was separated with 8% SDS-polyacrylamide gel electrophoresis, then transblotted onto NC membrane (Life Technology). The membrane was probed with anti-ZIP4 (Proteintech, 1:2000), ZO-1, claudin-1, ZEB1(Cell signaling Technology 1:500), pFAK, FAK (Abcam, 1:1000), pPaxillin, Paxillin (Life tech, 1:1000), and anti-β-actin (Abcam, 1:10000) antibody at 4 °C overnight, and then washed three times with 0.1% Tween 20-TBS and incubated with horseradish peroxidase-linked or NIR-coupled secondary antibody (1:5000) for 2 h at room temperature. The membrane was washed three times with 0.1% Tween 20-TBS. The immunoreacted bands were detected using an enhanced chemiluminescent (ECL) plus reagent kit. We are using the Li-COR Odyssey Fc machine to detect both ECL and the NIR-labeled 2nd antibodies.
Liu M., Yang J., Zhang Y., Zhou Z., Cui X., Zhang L., Fung K.M., Zheng W., Allard F.D., Yee E.U., Ding K., Wu H., Liang Z., Zheng L., Fernandez-Zapico M.E., Li Y.P., Bronze M.S., Morris K.T., Postier R.G., Houchen C.W., Yang J, & Li M. (2018). ZIP4 Promotes Pancreatic Cancer Progression by Repressing ZO-1 and claudin-1 through a ZEB1-Dependent Transcriptional Mechanism. Clinical cancer research : an official journal of the American Association for Cancer Research, 24(13), 3186-3196.
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4

Immunoblot Analysis of Bim, PTEN in Stimulated B Cells

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WEHI-control and WEHI-miR148a cells stimulated with 2 µg/ml anti-IgM for 14 h or left unstimulated were washed twice with PBS, and cell extracts were made by resuspending cell pellets in 1% NP-40 buffer containing 1% Nonidet P-40, 150 mM NaCl, 50 mM Tris-Cl (pH 8.0), 1 mM sodium orthovanadate, 1 mM DTT, and proteinase inhibitors (Thermo). 10 µg protein extract per sample was resolved in 10–12.5% gels by SDS-PAGE, transferred onto PVDF membranes, and detected with antibodies specific for murine Bim (Cell Signaling, 2933), Pten (Cell Signaling, 9559), and β-actin (Sigma clone AC-74). Images of the immunoblots were acquired on an Odyssey Fc machine (Li-cor).
Gonzalez-Martin A., Adams B.D., Lai M., Shepherd J., Salvador-Bernaldez M., Salvador J.M., Lu J., Nemazee D, & Xiao C. (2016). The microRNA miR-148a functions as a critical regulator of B cell tolerance and autoimmunity. Nature immunology, 17(4), 433-440.
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5

Western Blot Immunodetection Protocol

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Proteins were resolved by Mini Gel SDS-PAGE (Biorad® system) and transferred to PVDF membrane (Immobilon-P®- Millipore®) according to standard procedures. Blocking and antibody incubations were performed in TBS - 0.2% Tween-20® 5% milk (Marvel®). The following primary antibodies were used: anti-Ku80, (1:1000)38 (link), anti-actin (1:5000, Santa-Cruz® sc-1615), anti-H2AX-P (1:1000, Abcam® ab11174), anti-H3 (1:2000, Abcam® ab12079), anti-flag (1:2000, SIGMA® F1804 and F2425), anti-mono-ADPr AbD33205 (1:1000)34 (link), Anti-H3S10-p (1:1000, Bethyl® A301-844A-T, and Abcam® ab5176). Global ADP-ribosylation sigma was detected using the reagent anti-PAN-ADPr (1:2000, Merk® MABE1016). Appropriate HRP-conjugated secondary antibodies were used anti-mouse (1;10000, DAKO®), anti-rabbit (1;10000, DAKO®), anti-goat (1;10000, DAKO®) and anti-human (1:5000)34 (link). Immuno-reactive bands were detected by chemo-luminescence induced by Immobilon® western substrate (Millipore®), detected with the LI-COR® Odyssey-Fc machine and quantified using Image-Studio® software.
Brustel J., Muramoto T., Fumimoto K., Ellins J., Pears C.J, & Lakin N.D. (2022). Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones. Nature Communications, 13, 185.
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6

Validating CDC42 Antibody Specificity

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For validation of CDC42 antibody specificity, Western blotting was performed on whole cell lysates of MCF-7, SKBr3 and MDA-MB231 human breast cancer cell lines (obtained from the American Type Culture Collection; Rockville, MD, USA) using CDC42 antibody (clone PA1-092) at 1:1000 dilution and fluorescent secondary antibodies at 1:15,000 were used (IR Dye 800CW donkey anti-rabbit and 680RD donkey anti-mouse, LI-COR Biosciences, UK). 5% milk (Marvel original dried skimmed milk, Premier Food Groups Ltd, St Albans, UK) was used for blocking. Mouse β-Actin (A5441, Sigma-Aldrich; Clone AC-15; Sigma, UK) at 1:5000 was used as a house-keeping protein. A protein ladder (PageRuler Plus Prestained Protein Ladder, ThermoScientific, Waltham, MA, USA) was included. The fluorescence was then detected using the LI-COR Odyssey Fc machine to visualise the bands, with wavelengths 600, 700 and 800.
Chrysanthou E., Gorringe K.L., Joseph C., Craze M., Nolan C.C., Diez-Rodriguez M., Green A.R., Rakha E.A., Ellis I.O, & Mukherjee A. (2017). Phenotypic characterisation of breast cancer: the role of CDC42. Breast Cancer Research and Treatment, 164(2), 317-325.
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7

Quantification of Hif-1α and Hsp70 in M. amblycephala

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Total proteins from M. amblycephala liver, spleen, brain, gill, and kidney (n = 5 for each group) were quantified and separated on 8% SDS-PAGE, then transferred to nitrocellulose membranes. The membranes were incubated for 2 h with polyclonal antibodies, Hif-1α (1:500) and Hsp70 (1:200) (Boster, China), respectively, and then anti-rabbit IRDye 800CW-labeled secondary antibody (1:10,000) at room temperature for 1 h, and observed using Odyssey Fc machine (Licor Biosciences, USA). Gray values of every band were further calibrated and measured by ImageJ 1.46r (NIH, USA).
Chen N., Wu M., Tang G.P., Wang H.J., Huang C.X., Wu X.J., He Y., Zhang B., Huang C.H., Liu H., Wang W.M, & Wang H.L. (2017). Effects of Acute Hypoxia and Reoxygenation on Physiological and Immune Responses and Redox Balance of Wuchang Bream (Megalobrama amblycephala Yih, 1955). Frontiers in Physiology, 8, 375.
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8

Immunoblot Analysis of Bim, PTEN in Stimulated B Cells

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WEHI-control and WEHI-miR148a cells stimulated with 2 µg/ml anti-IgM for 14 h or left unstimulated were washed twice with PBS, and cell extracts were made by resuspending cell pellets in 1% NP-40 buffer containing 1% Nonidet P-40, 150 mM NaCl, 50 mM Tris-Cl (pH 8.0), 1 mM sodium orthovanadate, 1 mM DTT, and proteinase inhibitors (Thermo). 10 µg protein extract per sample was resolved in 10–12.5% gels by SDS-PAGE, transferred onto PVDF membranes, and detected with antibodies specific for murine Bim (Cell Signaling, 2933), Pten (Cell Signaling, 9559), and β-actin (Sigma clone AC-74). Images of the immunoblots were acquired on an Odyssey Fc machine (Li-cor).
Gonzalez-Martin A., Adams B.D., Lai M., Shepherd J., Salvador-Bernaldez M., Salvador J.M., Lu J., Nemazee D, & Xiao C. (2016). The microRNA miR-148a functions as a critical regulator of B cell tolerance and autoimmunity. Nature immunology, 17(4), 433-440.
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9

Biotinylated Protein Identification via Immunoblotting

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The APEX2 reaction was performed as described above and lysed in RIPA. Aliquots were taken for input, post-streptavidin flow-through, and StrePD. Proteins were separated on an SDS-PAGE gel and transferred to nitrocellulose for Western blotting with the indicated reagents/antibodies. Detection reagents used were streptavidin-HRP (1:1,000; GE Healthcare; RPN1231V), rabbit anti-lamin-B1 (1:10,000; Abcam; ab16048), mouse anti-lamin-A/C (1:5,000; Active Motif; 39287), rabbit anti-emerin (1:5,000; Santa Cruz; sc-15378), mouse anti-SC-35 (1:2,500, Sigma-Aldrich; S4045), rabbit anti-HNRNPA1 (1:2,500; ProteinTech; 11176-1-AP), and rabbit anti-SRSF1 (1:2,500; ProteinTech; 12929-2-AP). Imaging for streptavidin-HRP was done on a Licor Odyssey Fc machine. All other Western blots were imaged with a Licor Odyssey CLx machine.
Tran J.R., Paulson D.I., Moresco J.J., Adam S.A., Yates JR I.I.I., Goldman R.D, & Zheng Y. (2020). An APEX2 proximity ligation method for mapping interactions with the nuclear lamina. The Journal of Cell Biology, 220(1), e202002129.
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10

BRCA1 and RHA1 Protein Detection

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Protein was extracted from cells using 0.1% NP-40, 50 mM Hepes, pH 7.4, 0.15 M NaCl, 5 mM EDTA, 10% glycerin. Protein samples were quantified through Bradford assay then subjected to electrophoresis on 5 or 6% fixed SDS-PAGE gel. Samples were then transferred onto PVDF membrane that had been activated with methanol before transfer. Primary antibodies used were BRCA1 (1:500) [25 (link)] and RHA1 (1:20,000) [25 (link)] in PBS with 1% BSA. Secondary antibody was diluted into 5% milk in blocking buffer, anti-rabbit (1:5000) HRP-conjugated secondary antibody (Cytiva) and visualized under chemiluminescent setting on LiCOR Odyssey Fc machine.
Nagy G., Diabate M., Banerjee T., Adamovich A.I., Smith N., Jeon H., Dhar S., Liu W., Burgess K., Chung D., Starita L.M, & Parvin J.D. (2023). Multiplexed assay of variant effect reveals residues of functional importance in the BRCA1 coiled-coil and serine cluster domains. PLOS ONE, 18(11), e0293422.
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