X omat

Manufactured by Kodak

Sourced in United States, United Kingdom

The X-Omat is a photographic processing equipment designed and manufactured by Kodak. It is a self-contained unit that automates the development, fixing, washing, and drying of photographic films and prints. The X-Omat is capable of processing a variety of film and paper sizes, providing a consistent and reliable solution for photographic processing needs.

Automatically generated - may contain errors

Lab products found in correlation

Anti rabbit secondary antibody, by GE Healthcare (4 mentions) Immobilon p membrane, by Merck Group (4 mentions) Hyperfilm ecl, by Cytiva (3 mentions) P akt, by Cell Signaling Technology (3 mentions) Chemiluminescence detection reagent, by Cytiva (3 mentions) Polyvinylidene difluoride pvdf membrane, by Bio-Rad (3 mentions) In vitro transcription kit, by BD (2 mentions) Rnase protection assay kit, by BD (2 mentions) Rnaqueous midi kit, by Thermo Fisher Scientific (2 mentions) P s6 ribosomal protein, by Cell Signaling Technology (2 mentions) α tubulin, by Cell Signaling Technology (2 mentions) Cleaved parp, by Cell Signaling Technology (2 mentions) P 4ebp1, by Cell Signaling Technology (2 mentions) Enhanced chemiluminescence plus reagent, by Cytiva (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Caspase 3, by Cell Signaling Technology (2 mentions) Ecl western blotting system, by GE Healthcare (2 mentions) Mini protean tgx precast polyacrylamide gel, by Bio-Rad (2 mentions) Donkey anti rabbit or mouse hrp, by Jackson ImmunoResearch (2 mentions) Supersignal west pico chemiluminescent substrate, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

M35-A X-OMAT processor (11 citations) X-OMAT 2000 (10 citations) X-Omat AR (10 citations) X-OMAT X-ray film (9 citations) X-Omat TL film (7 citations) X-Omat Blue XB-1 film (5 citations) X-Omat developer (4 citations) X-OMAT blue films (4 citations) X-OMAT LS (4 citations) X-OMAT V (3 citations)

41 protocols using x omat

Quantitative Analysis of RNA Expression

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Example 15

Total RNA was extracted from tissues using the “RNAqueous-Midi kit” (Ambion Inc., Austin, Tex.). Ten μg of RNA were hybridized with a mix of 32P-labeled RNA probes. The 32P-labeled RNA probe mix was prepared by in vitro transcription using the “In vitro transcription kit”, CK-3, and custom template sets were provided by BD Biosciences/Pharmingen (San Diego, Calif.). The hybridized RNAs were treated with RNAse, using the “RNAse protection Assay kit” (BD Biosciences), precipitated and the protected fragments were resolved on vertical sequencing (10% acrylamide) gels. Following electrophoresis, the gels were dried and exposed to X-ray film (Kodak-X-Omat) and Phosphorlmager screen (Molecular Dynamics, Sunnyvale, Calif.). The signals on the screen were analyzed by Phosphorlmager Image-Quant software. The RNAse protection assay was performed using RNA samples of at least 3 to 5 individual mice per each virus. At least two independently prepared virus stocks were used for RNA levels analysis.

US11364306B2. Detargeted adenovirus variants and related methods (2022-06-21). ADCURE BIOTECHNOLOGIES, LLC. [US]. Inventors: Dmitry M. Shayakhmetov [US], Nelson C. Di Paolo [US].

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RNA Expression Analysis via RNAse Protection Assay

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Example 15

Total RNA was extracted from tissues using the “RNAqueous-Midi kit” (Ambion Inc., Austin, Tex.). Ten μg of RNA were hybridized with a mix of 32P-labeled RNA probes. The 32P-labeled RNA probe mix was prepared by in vitro transcription using the “In vitro transcription kit”, CK-3, and custom template sets were provided by BD Biosciences/Pharmingen (San Diego, Calif.). The hybridized RNAs were treated with RNAse, using the “RNAse protection Assay kit” (BD Biosciences), precipitated and the protected fragments were resolved on vertical sequencing (10% acrylamide) gels. Following electrophoresis, the gels were dried and exposed to X-ray film (Kodak-X-Omat) and PhosphorImager screen (Molecular Dynamics, Sunnyvale, Calif.). The signals on the screen were analyzed by PhosphorImager Image-Quant software. The RNAse protection assay was performed using RNA samples of at least 3 to 5 individual mice per each virus. At least two independently prepared virus stocks were used for RNA levels analysis.

US10376549B2. Detargeted adenovirus variants and related methods (2019-08-13). None [US], None [US], ADCURE BIOTECHNOLOGIES, LLC. [US]. Inventors: Dmitry M. Shayakhmetov [US], Nelson C. Di Paolo [US].

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Metastatic Activity Monitoring in Balb/c Nude Mice

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A549-ONECUT2, A549-ONECUT2 (ΔDBD) or A549-E.V. cells (2 × 10⁵) in PBS were injected into the left ventricle of 6-week-old male Balb/c nude mice to study metastatic activity. BLI was acquired with a NightOWL II LB 983 Imaging System (Berthold) every week. Bone damage was detected by X-ray radiography. The mice were anesthetized, arranged in a prone position on single-wrapped films (X-OMAT Kodak) and exposed for 180 s at 24 kV with a Faxitron instrument (Faxitron Bioptics). In vivo micro-computed tomography (micro-CT) images were obtained using a Skyscan-1076 micro-CT scanner (Skyscan) while the animals were anesthetized. The micro-CT scanner was operated at 55 kV and 181 μA with a 0.5 mm Al filter and a scan resolution of 17.4 μm. The cross-sections were reconstructed using NRecon software (Skyscan).

Ma Q., Wu K., Li H., Li H., Zhu Y., Hu G., Hu L, & Kong X. (2019). ONECUT2 overexpression promotes RAS-driven lung adenocarcinoma progression. Scientific Reports, 9, 20021.

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Western Blot Analysis of Cell Signaling

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Cell and tumour lysates were analysed by western blotting, as described previously (Han et al, 2008 (link)). Cell and tumour lysate protein was transferred onto Immobilon-P membranes (Millipore; Bedford, MA, USA). Blots were incubated with caspase-3 antibody (Cell Signaling, Beverly, MA, USA), cleaved-PARP (Cell Signaling), MCT-1 (Millipore), p4E-BP1 (Cell Signaling), S6 ribosomal protein (Cell Signaling), pS6 ribosomal protein (Cell Signaling) or LC3B antibody (Cell Signaling). The membranes were then incubated with anti-rabbit secondary antibody (GE Healthcare, Little Chalfont, UK). α-Tubulin (Cell Signaling) and β-actin (Cell Signaling) were used as loading controls. Specific-binding antibody–target protein interactions were detected using enhanced chemiluminescence plus reagents (Amersham Biosciences, Chalfont St Giles, UK) and exposure to either Hyperfilm ECL (Amersham) or X-OMAT Kodak (Kodak, Rochester, NY, USA) autoradiography film.

Lin G., Hill D.K., Andrejeva G., Boult J.K., Troy H., Fong A.C., Orton M.R., Panek R., Parkes H.G., Jafar M., Koh D.M., Robinson S.P., Judson I.R., Griffiths J.R., Leach M.O., Eykyn T.R, & Chung Y.L. (2014). Dichloroacetate induces autophagy in colorectal cancer cells and tumours. British Journal of Cancer, 111(2), 375-385.

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Western Blot Analysis of Tumor Lysates

Cited 1 time

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Tumor lysates were analyzed by western blotting, as described previously [43 (link)]. Tumor lysate protein was transferred onto Immobilon-P membranes (Millipore; Bedford, MA, USA). Blots were incubated with Glut4 (1F8) Mouse mAb, AceCS1(D19C6) Rabbit mAb, caspase-3 antibody, cleaved-PARP, or LC3B antibody. GAPDH was used as a loading control. (All above antibodies from Cell Signaling, Beverly, MA, USA). The membranes were then incubated with the anti-rabbit secondary antibody (GE Healthcare, Little Chalfont, UK). Specific-binding antibody–target protein interactions were detected using enhanced chemiluminescence plus reagents (Amersham Biosciences, Chalfont St Giles, UK) and exposure to either Hyperfilm ECL (Amersham) or X-OMAT Kodak (Kodak, Rochester, NY, USA) autoradiography film. Tumors with 3 days post-irradiation in the irradiated and non-irradiated groups were removed, frozen and embedded, sliced and stained with hematoxylin and eosin stain [43 (link)]. In a separate group of mice, 3 tumors of each group were included.

Chung Y.H., Tsai C.K., Wang C.C., Chen H.M., Lu K.Y., Chiu H., Lin Y.C., Yen T.C, & Lin G. (2017). Early Response Monitoring Following Radiation Therapy by Using [18F]FDG and [11C]Acetate PET in Prostate Cancer Xenograft Model with Metabolomics Corroboration. Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, 22(11), 1946.

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Western Blotting Protein Expression Analysis

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As described previously [34 (link)], protein expressions on tumor lysates were analysed by western blotting. 15ug tumor protein lysate was transferred onto Immobilon-P membranes (Millipore: Bedford, MA, USA) and the blots incubated with pS6 ribosomal protein (Cell Signalling 9205), p-AKT (Cell Signalling 9271) and Cho-K (Sigma HPA024153). b-actin (Cell Signalling 4967) was used as loading control. The membranes were then incubated with anti-rabbit secondary antibody (GE Healthcare, UK). Specific-binding antibody-target protein interactions were detected using enhanced chemiluminescence (Amersham Biosciences, UK) and exposure to X-OMAT Kodak (Kodak, USA) autoradiography film. For in vitro analysis cells were lysed in Pierce RIPA buffer (Thermo Scientific), supplemented with protease inhibitor cocktail (Roche), and PhosSTOP phosphatase inhibitor (Roche). Antibodies were diluted in 5% milk-PBS-Tween and signal detected using SuperSignal West Dura HRP substrate followed by visualization on a Syngene ChemiGenius Imager.
Antibodies used for p70S6K (CST 9202, 1:1000); p70S6K pT389 (CST 9205, 1:500); AKT (CST 9272, 1:1000), pAKT S473 (CST 9271, 1:500), S6 (CST 2317, 1:1000), pS6 S235/236 (CST 4858, 1:000), PDCD4 (CST 9535, 1:1000), vinculin (Sigma V9131, 1:5000).

Wong Te Fong A.C., Thavasu P., Gagrica S., Swales K.E., Leach M.O., Cosulich S.C., Chung Y.L, & Banerji U. (2017). Evaluation of the combination of the dual m-TORC1/2 inhibitor vistusertib (AZD2014) and paclitaxel in ovarian cancer models. Oncotarget, 8(69), 113874-113884.

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Western Blot Analysis of Signaling Proteins

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Cell lysates were analyzed by western blotting as described previously [22] (link). Cell lysate protein was transferred onto Immobilon-P membranes (Millipore; Bedford MA, USA). Blots were blocked in 5% non-fat milk or 5% bovine albumin and then incubated with primary antibody for pS6RP (Cell Signaling), S6RP (Cell Signaling), p4E-BP1 (Cell Signaling), total 4E-BP1 (Cell Signaling), pAkt (Cell Signaling), total Akt (Cell Signaling), cleaved PARP (Cell Signaling), caspase 3 (Cell Signaling), LC3 (Cell Signaling), MCT-1 (Millipore) or MCT-4 (Santa Cruz Biotechnology). The membranes were then incubated with anti-rabbit secondary antibody (GE Healthcare). Western blots for α-tubulin (Cell Signaling) provided a loading control. Specific binding antibody-target protein interactions were detected using enhanced chemiluminescence plus reagents (Amersham Biosciences, Buckingham-shire, UK) and exposure to either Hyperfilm ECL (Amersham) or XOMAT Kodak (Rochester NY, USA) autoradiography film.

Lin G., Andrejeva G., Wong Te Fong A.C., Hill D.K., Orton M.R., Parkes H.G., Koh D.M., Robinson S.P., Leach M.O., Eykyn T.R, & Chung Y.L. (2014). Reduced Warburg Effect in Cancer Cells Undergoing Autophagy: Steady- State 1H-MRS and Real-Time Hyperpolarized 13C-MRS Studies. PLoS ONE, 9(3), e92645.

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Protein Expression Analysis in RCC Cells

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The RCC cells were treated with DMSO/Vehicle (Control) or indicated dose and time of the noted compound. Cells were harvested and lysed in RIPA buffer (50 mM Tris-HCI, pH 8.0, 150 mM sodium chloride, 1.0% NP-40, 0.5% sodium deoxycholate, 0.1% sodium dodecyl sulphate (SDS), and 0.1% of protease inhibitor cocktail) for 20 min at 4°C. The lysates were then centrifuged at 14,000 rpm at 4 °C for 15 min to get rid of debris. We then determined the protein concentrations of whole cell lysates using the Bradford Protein Assay Kit. Supernatant proteins, 50μg from each sample, were separated by SDS-10% polyacrylamide gel electrophoresis (SDSPAGE) and transferred to polyvinylidene difluoride (PVDF) membrane (Bio-Rad, Hercules, CA) by standard procedures. The membranes were hybridized with primary antibodies followed by incubation with appropriate secondary antibodies. The antibody-bound proteins were visualized by treatment with the chemiluminescence detection reagent (Amersham Biosciences) according to the manufacturer’s instructions, followed by exposure to X-ray film (Kodak X-Omat). The same membranes were then re-probed with the anti-β actin antibody, which was used as an internal control for protein loading.

Alsaab H.O., Sau S., Alzhrani R.M., Cheriyan V.T., Polin L.A., Vaishampayan U., Rishi A.K, & Iyer A.K. (2018). Tumor Hypoxia Directed Multimodal Nanotherapy for Overcoming Drug Resistance in Renal Cell Carcinoma and Reprogramming Macrophages. Biomaterials, 183, 280-294.

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Phosphokinase Profiling of Suramin-Treated KATO-III Cells

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A membrane-based antibody array (R&D Systems, Raffles, China) that determines the relative levels of 45 different human phosphorylated protein kinases was used according to the manufacturer’s instructions. Briefly, equal amounts of cell lysates of KATO-III cell line treated with or without 200 µM Suramin (Sigma Chemical Co, St. Louis, MO, USA) into FBS free IMDM medium along with control for 5 hrs were incubated overnight with the phosphokinase array membrane. The array was washed to remove unbound proteins followed by incubation with a mixture of biotinylated detection antibodies. Streptavidin-HRP and chemiluminescent detection reagents were applied to visualize the signal produced at each capture spot corresponding to the amount of phosphorylated protein bound with densitometry by using a photosensitive film (Kodak, X-OMAT, AR, USA).

Shah S., Fourgeaud C., Derieux S., Mirshahi S., Contant G., Pimpie C., Lo Dico R., Soria J., Pocard M, & Mirshahi M. (2018). The close relationship between heparanase and epithelial mesenchymal transition in gastric signet-ring cell adenocarcinoma. Oncotarget, 9(73), 33778-33787.

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Antibodies for Protein Localization and Detection

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Antibodies against Sec61 were as described (132 (link)). H. D. Schmitt provided anti-Emp47 antibodies. We derived monoclonal anti-HA antibodies from hybridoma cells (12CH5). We purchased anti-PGK (A6457, Molecular Probes), anti-GST (600-101-200, Rockland), polyclonal anti-GFP for immunoprecipitation (A6455, Molecular Probes), monoclonal anti-GFP for immunodetection (JL-8, Clontech), anti-Myc (M5546, Sigma–Aldrich), anti-FLAG (M2, F3165, Sigma–Aldrich), and anti-GAPDH (MAB374, Sigma–Aldrich). Horseradish peroxidase–coupled secondary antibodies (Sigma–Aldrich) were used to visualize immunoblots by Western Lightning Plus ECL (PerkinElmer Life Sciences) and autoradiography films (X-Omat, Kodak). For immunogold labelings, a rabbit anti-GFP antibody (Abcam, ab6556; diluted 1:100) and a 12-nm colloidal gold goat anti-rabbit secondary antibody (Dianova, 111-205-144; diluted 1:30) were used.

Meusser B., Purfuerst B, & Luft F.C. (2021). HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region. The Journal of Biological Chemistry, 295(52), 17950-17972.

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