Canoscan 9000f

Manufactured by Canon

Sourced in Japan

The CanoScan 9000F is a flatbed scanner designed for high-quality image capture. It features a 4800 x 9600 dpi resolution and can scan film, slides, and photographic prints up to 8.5 x 11.7 inches in size. The scanner utilizes Canon's proprietary image processing technology to deliver accurate color reproduction.

Automatically generated - may contain errors

Lab products found in correlation

S246 phospho hdac4 s259 phospho hdac5, by Cell Signaling Technology (2 mentions) Pen strep, by Thermo Fisher Scientific (2 mentions) α mem, by Thermo Fisher Scientific (2 mentions) Supersignal west dura extended duration substrate, by Thermo Fisher Scientific (2 mentions) Gapdh, by Santa Cruz Biotechnology (2 mentions) Totallab software, by Cleaver Scientific (1 mentions) Simplyblue safestain, by Thermo Fisher Scientific (1 mentions) Dimethyl sulfoxide (dmso), by Tokyo Chemical Industry (1 mentions) Donkey anti rabbit hrp, by Jackson ImmunoResearch (1 mentions) Clarity reagent, by Bio-Rad (1 mentions) Donkey anti chicken hrp, by Jackson ImmunoResearch (1 mentions) Donkey anti mouse hrp, by Jackson ImmunoResearch (1 mentions) Atr ftir, by PerkinElmer (1 mentions) Jsm 6480lv, by JEOL (1 mentions) Amira software, by Visage Imaging (1 mentions)

Close spelling variants of this product

CanoScan 9000F Mark II CanoScan 9000F Mark II scanner CanoScan 9000F scanner

17 protocols using canoscan 9000f

Lateral Flow Immunoassay Protocol

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LFIA was performed at room temperature. The test strip was immersed in a vertical position with its lower end for 1 min in an aliquot of the sample (model solution of the analyte or blood serum), after which it was placed on a horizontal surface. The intensity of TZ coloration was assessed after 10 min (or from 2 to 12 min with an interval of 30 s when studying the kinetics of the binding). The coloration was recorded using a CanoScan 9000F (Canon; Tokyo, Japan) scanner, after which the images were digitally processed by TotalLAB software (Cleaver Scientific; Rugby, UK).
The visual LOD (cutoff) was defined as a minimum analyte concentration at which the visually perceptible stained band was visible in the TZ. The instrumental LOD was defined as an analyte concentration at which the TZ staining intensity exceeded 3 times standard deviation for background staining of the TZ (samples without analyte).

Taranova N.A., Byzova N.A., Pridvorova S.M., Zherdev A.V, & Dzantiev B.B. (2021). Comparative Assessment of Different Gold Nanoflowers as Labels for Lateral Flow Immunosensors. Sensors (Basel, Switzerland), 21(21), 7098.

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Quantitative SDS-PAGE Protein Analysis

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Proteins were analysed by SDS-PAGE. SDS-PAGE gels used for whole cell protein analysis were lab-poured 15% polyacrylamide Tris/Glycine gels prepared as (Wyre and Overton, 2014b (link)). Cell pellets equivalent to 1 mL·OD₆₅₀ were collected by centrifugation (13 000 g, 5 min) and resuspended in 60 μL of sample buffer, boiled for 10 min, and 10 μL of each sample was loaded onto the gel. Gels were run at 110 V for 2 h at room temperature. A molecular weight ladder was run on all gels (5 μL of 0.2 mg mL⁻¹ Blue Prestained Protein Standards ladder, New England BioLabs, United States).
To visualise protein bands, gels were stained with SimplyBlue™ Safe Stain (ThermoFisher Scientific, UK), then destained with water, and imaged on a flatbed scanner CanoScan 9000F (Canon, UK) at 4800 dpi resolution. The images were analysed densitometrically using ImageJ software (Schneider et al., 2012 (link)). Firstly, images were subjected to background subtraction (default settings) followed by lane description. GFP/TNFα-GFP proteins peaks were defined and the areas under the peak were calculated. To estimate the percentage of protein that was GFP/TNFα-GFP, the corresponding peak intensity was compared to the intensity of the total lane.

Zulkifly N.A., Selas Castiñeiras T, & Overton T.W. (2023). Optimisation of recombinant TNFα production in Escherichia coli using GFP fusions and flow cytometry. Frontiers in Bioengineering and Biotechnology, 11, 1171823.

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Hypocotyl Elongation Assay in Arabidopsis

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Seeds were surface sterilized, stratified at 4°C for 2 d, and plated on half-strength Murashige and Skoog (MS) medium containing 0.8% (w/v) agar and supplemented with 1 μM BRZ from a 10 mM stock solution in 100% DMSO (Tokyo Chemical Industry) or, for the controls, with 0.1% (v/v) DMSO. Following a 1-h light exposure to induce germination, we wrapped the plates in aluminum foil and incubated them in the dark at 22°C for 5 d. We then scanned the plates at 600 dots per inch resolution on a regular flatbed scanner (CanoScan 9000F; Canon), measured hypocotyl lengths using Fiji (Schindelin et al., 2012 (link)), and analyzed the results in R version 3.6.1 (R Core Team, 2014 ) using the packages mratios (Kitsche and Hothorn, 2014 (link)) and multcomp (Hothorn et al., 2008 (link)). Rather than P-values, we report unadjusted 95% confidence limits for fold-changes. We used a mixed-effects model for the ratio of a given line to the wild-type Col-0, allowing for heterogeneous variances, to analyze log-transformed end point hypocotyl lengths. To evaluate treatment-by-mutant interactions, we calculated the 95% two-sided confidence intervals for the relative inhibition (Col-0: untreated versus BRZ-treated hypocotyl length)/(any genotype: untreated versus BRZ-treated hypocotyl length) for the log-transformed length.

Hohmann U., Ramakrishna P., Wang K., Lorenzo-Orts L., Nicolet J., Henschen A., Barberon M., Bayer M, & Hothorn M. (2020). Constitutive Activation of Leucine-Rich Repeat Receptor Kinase Signaling Pathways by BAK1-INTERACTING RECEPTOR-LIKE KINASE3 Chimera. The Plant Cell, 32(10), 3311-3323.

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Extraction and Quantification of Cellular Lipids

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Extraction of total cellular lipids was performed as previously described by Bligh and Dyer [60 (link)] with minor modifications. In brief, cells (approximately 3 × 10⁷ cells) were harvested by centrifugation at 6000g at room temperature for 5 min. The pellets were mixed with 400 µl methanol:chloroform (1:1, v/v) and vortexed for 5 min. The suspension was mixed with 120 μl PAK buffer (1 M KCl, 0.2 M phosphate acid). The mixture was centrifuged at 12,000g for 5 min and the lower chloroform phase was transferred to a new glass tube. Finally, additional chloroform was added into the organic phase until the constant volume was 20 µl.
For thin-layer chromatography, equal volume of total cellular lipid extract was loaded as a spot on 10 × 20 cm silica gel GF254 TLC plates (Haiyang, China). Neutral lipids in the samples were separated using a hexane/diethylether (3/1, v/v) solvent mixture. Then, the silica gel plates were dried under the hood and stained by iodine vapor at 37 °C for 10 min. Finally, the triacylglycerol bands were visualized by CanoScan 9000F (Canon, Japan) and analyzed by Quantity One software. All data were normalized to positive control.

Cheng X., Liu G., Ke W., Zhao L., Lv B., Ma X., Xu N., Xia X., Deng X., Zheng C, & Huang K. (2017). Building a multipurpose insertional mutant library for forward and reverse genetics in Chlamydomonas. Plant Methods, 13, 36.

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Western Blotting of MYO19 Protein

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Samples were loaded onto a 4-12% Bis-Tris NuPAGE gels and then transferred to nitrocellulose. Transfer was verified by Ponceau staining (0.5% Ponceau Red-S, 2% Acetic acid in H₂O). Membranes were blocked in TBST (50mM Tris-HCl, pH 7.5, 150mM NaCl, 0.1% Tween-20) with 5% powdered milk (blocking buffer) for 1 hour, incubated with primary antibody diluted in blocking buffer for 1h, and washed in TBST. Membranes were exposed to the appropriate secondary antibody diluted in blocking buffer for 1 hour, and washed in TBST prior to incubation with Bio-Rad Clarity reagent and exposure to film. Films were scanned in using a Canon CanoScan 9000F with a transparency adaptor. MYO19 was detected in HeLa cells using 0.3 μg/ml chicken anti-human MYO19 [Quintero et al. 2009 (link)] and 80ng/ml donkey anti-chicken HRP (Jackson Immuno Research). MYO19 was detected in B16F1 samples using 0.17 μg/ml rabbit anti-mouse MYO19 [Rohn et al. 2014 (link)] and 40ng/ml donkey anti-rabbit HRP (Jackson Immuno Research). Porin was detected in all samples using 5ng/ml mouse anti-human porin (LifeTechnologies, A31855), and 10 ng/ml donkey anti-mouse HRP (Jackson Immuno Research).

Hawthorne J.L., Mehta P.R., Singh P.P., Wong N.Q, & Quintero O.A. (2016). Positively charged residues within the MYO19 MyMOMA domain are essential for proper localization of MYO19 to the mitochondrial outer membrane. Cytoskeleton (Hoboken, N.J.), 73(6), 286-299.

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Characterization of Membrane Samples using ATR-FTIR, Conductivity, and SEM

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Attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR; PerkinElmer, Billerica, MA, USA) was used to analyse the functional groups of samples. The membrane conductivity was measured using a four-point probe conductivity meter (RM3000, JANDEL) in a sheet resistance mode. The morphologies of the samples were imaged by scanning electron microscopy (SEM; JSM-6480 LV, JEOL, Oberkochen, Germany). The cross-sections of the membrane were prepared by fracturing in liquid nitrogen. The membrane samples were sputter coated with gold before being imaged with SEM. The acceleration voltage was 3 kV and 10 kV for graphite samples and membrane samples, respectively. Red, green and blue (RGB) were used to give a quantitative evaluation of the colour of the membrane. The samples were scanned by a digital scanner (CanoScan 9000F, Canon, Tokyo, Japan) and Image J software was used to calculate the RGB value. The detailed calculation of RGB has been previously described [15 (link)].

Xu L., Wang K., Wang J, & Patterson D.A. (2021). Linking the Tuneability and Defouling of Electrically Conductive Polyaniline/Exfoliated Graphite Composite Membranes. Membranes, 11(8), 631.

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TPTD and ABL Regulate HDAC4/5

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After 14 days of culture in α-MEM, 10% FBS, and 1% Pen/Strep (all Life Technologies) at 37°C, Ocy454 cells were treated with TPTD 5 nM, ABL 5 nM, or vehicle for 5 minutes to 3 hours. The Ocy454 cells were obtained from Paola Divieti Pajevic from the MGH Center for Skeletal Research, Boston, Massachusetts, USA. Total proteins (10 μg) were resolved by SDS-PAGE under reducing conditions. Immunodetection was performed with S246 phospho-HDAC4/ S259 phospho-HDAC5 (Cell Signaling Technology 3443), phospho-CRCT2 (Abcam, ab203187), HDAC4 (Abcam, ab12172), HDAC5 (Abcam, ab55403), or GAPDH (Santa Cruz Biotechnology, SC-32233). GAPDH was used as loading control. Immunoreactive proteins were detected using SuperSignal West Dura Extended Duration Substrate (Thermo Fisher Scientific, 34075). Films were scanned (Canon, CanoScan 9000F) and saved as 600 dpi color images.

Lv Z., Zhang J., Liang S., Zhou C., Hu D., Brooks D.J., Bouxsein M.L., Lanske B., Kostenuik P., Gori F, & Baron R. (2023). Comparative study in estrogen-depleted mice identifies skeletal and osteocyte transcriptomic responses to abaloparatide and teriparatide. JCI Insight, 8(20), e161932.

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Thin Layer Chromatography of Lipids

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Lipids were separated on silica coated plates using a solvent system consisting of chloroform, methanol and acetic acid (65:25:10, v/v). The TLC plates were sprayed with 10% sulfuric acid in 100% ethanol and visualized by charring (heating) at 180 °C for approximately 30 s. The plate was cooled and immediately imaged using a Canon CanoScan 9000F.

Herndon J.L., Peters R.E., Hofer R.N., Simmons T.B., Symes S.J, & Giles D.K. (2020). Exogenous polyunsaturated fatty acids (PUFAs) promote changes in growth, phospholipid composition, membrane permeability and virulence phenotypes in Escherichia coli. BMC Microbiology, 20, 305.

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Phospholipid Extraction and Separation

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The method of Bligh [37 (link)] and Dyer was used to extract phospholipids from 14 ml of bacterial culture. Isolated phospholipids were deposited onto Silica Gel 60 TLC plates and subsequently separated using a solvent system consisting of chloroform, methanol and acetic acid (65:25:10 v/v/v). Visualization of phospholipids was achieved by charring plates with a solution of 10% sulfuric acid in 100% ethanol followed by heating to 150 °C for approximately 1 m. Plates were scanned using a Canon CanoScan 9000F.

Baker L.Y., Hobby C.R., Siv A.W., Bible W.C., Glennon M.S., Anderson D.M., Symes S.J, & Giles D.K. (2018). Pseudomonas aeruginosa responds to exogenous polyunsaturated fatty acids (PUFAs) by modifying phospholipid composition, membrane permeability, and phenotypes associated with virulence. BMC Microbiology, 18, 117.

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Carotenoid and Insecticide Compound Database

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KEGG COMPOUND (release 29) was used as a source of 2D structure dataset. This dataset has almost 12,000 compounds. A picture of octadehydro-beta-carotene was taken from “Carotenoids Handbook” edited by Britton et al. (published by Birkhauser). Pictures of samples for chemical literature data extraction were taken from “Insecticides of Natural Origin” edited by Dev and Koul published by Harwood Academic Publishers. Pictures were scanned by Canoscan 9000F (Canon Inc., Tokyo, Japan) and converted to PDF files.

, & Maeda M.H. (2015). Current Challenges in Development of a Database of Three-Dimensional Chemical Structures. Frontiers in Bioengineering and Biotechnology, 3, 66.

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