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Chemdoc xrs

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The ChemDoc XRS is a compact and versatile gel documentation system designed for imaging and analyzing various types of gels, blots, and samples. It features a high-resolution camera, selectable UV and white light sources, and advanced software for image capture and analysis. The ChemDoc XRS enables users to document, quantify, and analyze a wide range of samples in a laboratory setting.

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Lab products found in correlation

Quantity one software, by Bio-Rad (5 mentions) Cary eclipse fluorescence spectrophotometer, by Agilent Technologies (5 mentions) Chirascan cd spectrometer, by Applied Photophysics (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Multiskan sky, by Thermo Fisher Scientific (3 mentions) Goat anti rabbit igg hrp, by Santa Cruz Biotechnology (2 mentions) Na934v, by GE Healthcare (2 mentions) Nxa931, by GE Healthcare (2 mentions) Polyvinylidene difluoride membrane, by Merck Group (2 mentions) Image pro plus 6.0 analysis software, by Media Cybernetics (2 mentions) Nanodrop 1000 spectrophotometer, by Thermo Fisher Scientific (2 mentions) Lsm780 confocal laser scanning microscope, by Zeiss (2 mentions) Bca protein assay kit, by Beyotime (2 mentions) F 7000 spectrometer, by Hitachi (2 mentions) Electrophoresis analyzer, by Bio-Rad (2 mentions) Ecl plus, by Yeasen (2 mentions) Nanodrop 1000, by Thermo Fisher Scientific (2 mentions) Mini gel system, by Bio-Rad (2 mentions) Wet blotter system, by Bio-Rad (2 mentions) Ab56416, by Abcam (1 mentions)

Close spelling variants of this product

ChemDoc XRS system (15 citations) ChemDoc (12 citations) ChemDoc XRS+ imaging system (6 citations)

46 protocols using chemdoc xrs

1

Western Blot Analysis of Autophagy and Inflammatory Markers

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Western blot analysis was performed as described previously[9 (link)]. Briefly, cultured cells were homogenized in a lysis buffer containing a protease inhibitor cocktail. After SDS-PAGE, the proteins on the gel were transferred to a polyvinylidene membrane. Then, the membrane was stained with the desired antibodies. The membrane was visualized with ImmobilonWestern (Millipore, Hayward, CA), and the image was captured with ChemDoc XRS (Bio-Rad, Hercules, CA). Primary antibodies used for Western blotting: microtubule-associated protein 1 light chain 3 (LC3) rabbit polyclonal antibody (PM036; MBL, Nagoya, Japan), p62 mouse monoclonal antibody (ab56416; Abcam, Cambridge, UK), PARP1 rabbit polyclonal antibody (9542S; Cell Signaling Technology, Danvers, MA), phospho-NF-kB p65 rabbit monoclonal antibody (Ser536) (3033S; Cell Signaling Technology), NF-kB p65 rabbit polyclonal antibody (sc-372; Santa Cruz Biotech, Dallas, TX), phosphor-extracellular signal–regulated kinase (ERK) rabbit polyclonal antibody (9101S; Cell Signaling Technology), ERK rabbit monoclonal antibody (4695S; Cell Signaling Technology), tubulin rabbit monoclonal antibody (ab176560; Abcam). Goat anti-rabbit IgG-HRP (sc-2030; Santa Cruz) or goat anti-mouse IgG-HRP (sc-2005; Santa Cruz) were used as secondary antibodies.
Kubota M., Kakimoto K., Nakagawa T., Koubayashi E., Nakazawa K., Tawa H., Hirata Y., Okada T., Kawakami K., Asai A., Hosomi S., Takeuchi T., Fukunishi S., Inoue T., Asahi M, & Higuchi K. (2019). Autophagy deficiency exacerbates colitis through excessive oxidative stress and MAPK signaling pathway activation. PLoS ONE, 14(11), e0225066.
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2

Caspase-3 Activity Assay in Cell Lysates

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For ABP labelling of caspase-3 in cell lysates, 75 μg of lysates
were incubated with the ABP (f.c. 1 and 10 μM, 37°C, 500 rpm, 1
hr). Positive controls for CS1-NP western blot analysis was made by incubating
apoptotic cell lysates with 10 μM CS1 for 1 hr, at 37°C, with
shaking at 500 rpm. Samples were denatured with 5x Laemmli buffer (0.3 M TRIS,
20 % glycerol, 25 % P-mercaptoethanol, 10 % SDS, 0.1% bromophenol blue) and
incubated at 95°C for 10 min. Samples were resolved in 12 %, 15 %, or
17.5 % acrylamide gels, proteins were transferred to a polyvinylidene fluoride
membrane (PVDF, Immobilon-P, 0.45 μm pore size, Merck Millipore) by
semi-dry transfer (PowerPac 1000, Biorad) and blocked with 5 % bovine serum
albumin in TBS-T (50 mM TRIS, 150 mM NaCl, 0.1 % tween-20, pH 7.4–7.6)
for 2 hr, at RT, shaking. For western blot analysis of ABP labelling of
caspase-3, membranes were incubated with streptavidin-HRP (1:2,000; 30–45
min; RT; shaking). For immunoblot analysis, membranes were incubated in primary
antibody (1:1,000) overnight and in secondary antibody (1:10,000; 1 hr; RT;
shaking) the following day. Proteins were detected by incubating the membranes
in the dark with ECL plus for 5 minutes and imaged with ChemDoc XRS+
(Biorad).
Cogo F., Poreba M., Rut W., Groborz K., Smyth P., Johnston M.C., Williams R., Longley D.B., Burden R.E., Salvesen G.S., Drag M, & Scott C.J. (2019). Development of an advanced nanoformulation for the intracellular delivery of a caspase-3 selective activity-based probe. Nanoscale, 11(2), 742-751.
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3

Biophysical Characterization of Fluorescent Compounds

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Absorption spectra were recorded on a Cary 300 UV-VIS Spectrophotometer (Agilent). Gel electrophoresis was performed on a mini-PROTEAN system (Bio-Rad) and imaged on a Bio-Rad ChemDoc XRS. Fluorescence spectra were measured on an F-7000 spectrofluorophotometer (Hitachi) with a TC125 temperature control (Quantum Northwest). The dynamic light scanning (DLS) measurements of TPE-N3 in DMSO/H2O (v/v, 1/399) and O1-DTPE in H2O were performed on a 90Plus Particle Size Analyzer (Brookhaven Instruments Corporation). Circular dichroism (CD) measurements were obtained at 25 °C using 1 mm path length cuvettes (Hellma) on a Chirascan CD spectrometer (Applied Photophysics). Stopped-flow spectroscopic analyses were performed on a Chirascan spectrometer equipped with a stopped-flow accessory. The 1H spectra were collected on an Avance 850 MHz spectrometer (Bruker) equipped with a triple resonance 5 mm HCN-cryoprobe at 25 °C.
Zhu L., Zhou J., Xu G., Li C., Ling P., Liu B., Ju H, & Lei J. (2018). DNA quadruplexes as molecular scaffolds for controlled assembly of fluorogens with aggregation-induced emission †Electronic supplementary information (ESI) available: Supporting figures and tables. See DOI: 10.1039/c8sc00001h. Chemical Science, 9(9), 2559-2566.
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4

Feasibility Assessment of CHA Technique

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To assess the feasibility of CHA, we used fluorescence measurement and agarose gel electrophoresis. The bio-barcode SH-DNA was centrifuged at 4000 rpm for 30-60 s, dissolved in sterile water to 50 μM, and then diluted to 10-105 different multiples of bio-barcode SH-DNA by adding 5 μM H1 5 μL and 5 μM H2 15 μL and reacted at 37°C for 90 min. The fluorescence readings were detected at 489/521 nm excitation/emission wavelengths.
In agarose gel electrophoresis analysis, 3% agarose gel solution was prepared and stained with a diluted top red solution. After solidification, 9 μL of the sample was mixed with 1 μL 10×DNA loading buffer into each channel separately, at 110 mV in 1×TAE buffer (40 mM Tris-acetate, 1 mM EDTA, pH 8.0) for 40 min. Bio-Rad ChemDoc XRS imaged the gel.
Wang Y., El-Aty A.M., Chen G., Jia H., Cui X., Xu L., Cao Z., She Y., Jin F., Zhang Y., Hacimuftuoglu A., Lamu S., Wang J., Zheng L., Jin M, & Hammock B.D. (2022). A competitive immunoassay for detecting triazophos based on fluorescent catalytic hairpin self-assembly. Mikrochimica acta, 189(3), 114.
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5

Western Blot Analysis of Protein Expression

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The tissue and cell samples were washed with ice-cold PBS and incubated for 30 min on the ice in lysis buffer. The supernatant was retained after centrifugation. Protein concentration was determined using the BCA protein assay kit (Pierce). For Western blot analysis, 100 μg total protein from each sample was separated on SDS-PAGE gel and transferred onto PVDF membranes. The membranes were blocked with 5% milk blocking buffer and incubated with the designed primary antibodies overnight at 4°C. The primary antibodies are listed in Table 2. After 3 washes with TBS, the membranes were incubated with HRP-conjugated secondary antibody at 37°C for 2 h. Bound secondary antibodies were visualized using an enhanced chemiluminescence (ECL) kit (Bio-Rad) with ChemDoc XRS and Quantity One software (Bio-Rad).
Chen Y., Zhu L., Ji L., Yang Y., Lu L., Wang X, & Zhou G. (2018). Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 24, 9007-9018.
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6

Characterization of Exosome Nanoparticles

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Fluorescence detections were carried out on a Cary Eclipse Fluorescence Spectrophotometer (Agilent Technologies, United States, https://www.agilent.com). Transmission Electron Microscope (TEM) image, Nanoparticle Tracking Analysis (NTA), the SDS-PAGE and gel imaging analysis for the characterization of tumor cell-derived exosomes was supported by H-7500 transmission electron microscope (Hitachi High-Technologies Co., Japan, https://www.hitachihightech.com), ZetaView (Particle Metrix, Germany, https://www.particle-metrix.com), electrophoresis analyzer and ChemDoc XRS (Bio-Rad, United States, https://www.bio-equip.com), respectively.
Chen W., Zhang Y., Di K., Liu C., Xia Y., Ding S., Shen H, & Li Z. (2022). A Washing-Free and Easy-to-Operate Fluorescent Biosensor for Highly Efficient Detection of Breast Cancer-Derived Exosomes. Frontiers in Bioengineering and Biotechnology, 10, 945858.
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7

Lipid-binding Properties of Acetylated Atg3

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WT Atg3 (expressed or semi-synthetic) or semi-synthetic Atg3 K19ac-K48ac (10 μM) was incubated with liposomes containing 20 or 55% DOPE (1 mM lipids) in Tris-HCl buffer at 30 °C for 90 min in a total volume of 300 μl. The mixtures were adjusted to 40% (w/v) Nycodenz by adding with 300 μl 80% (w/v) Nycodenz in Tris-HCl buffer. The resulting mixture was overlaid with 1300 μl Tris-HCl buffer containing 30% (w/v) Nycodenz and 100 μl Tris-HCl buffer without Nycodenz. The samples were centrifuged at 200,000g in a TCL-55 rotor (Beckman) for 4 h. The liposomes and lipid-anchored proteins were collected from the top 100 μl of the mixtures and analysed by SDS–PAGE. Protein bands were detected by Coomassie Brilliant Blue staining and band intensities on SDS–PAGE were quantified by using Image software on ChemDocXRS+ (Bio-Rad). Student's t-test was used to calculate P values and evaluate the significance of difference between recovered Atg3 WT and Atg3 K19ac-K48ac.
Li Y.T., Yi C., Chen C.C., Lan H., Pan M., Zhang S.J., Huang Y.C., Guan C.J., Li Y.M., Yu L, & Liu L. (2017). A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation. Nature Communications, 8, 14846.
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8

Western Blotting of Brain Tissue Proteins

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Brain tissue samples were homogenized in a buffer containing 40 mM Tris-HCl (pH 7.0), 1% Triton X-100, 0.2% SDS, 1.0 mM sodium deoxycholate, 1.0 mM EGTA, 1.0 mM EDTA, 1.0 mM Na3VO4, 50 mM NaF, 1.0 mM PMSF, and 2.0 μg/ml each of aprotinin, leupeptin and pepstatin. The homogenates were centrifuged at 16,000 rpm for 15 min, and the supernatants were stored in aliquots at -80°C until use. The tissue extracts were separated in SDS-polyacrylamide gels and then transferred onto polyvinylidene difluoride membrane (Millipore, CA). Nonspecific binding sites on the membrane were blocked by 5% bovine serum albumin in 0.1% TBS/Tween-20 (TBST) for 1 h. The membrane was then incubated with specific primary antibodies (Table 1) overnight at 4°C. After washing with TBST, the membrane was incubated with horseradish peroxidase-conjugated secondary antibody (1:2000; Cell signaling Technology, Beverly, MA) for 2 hours at room temperature. Immunoreactive bands were visualized by using the Super Signal West Pico Chemi-luminescent Substrate (Pierce Biotechnology, Rockford, IL) and Chem Doc XRS with Quantity One software (BioRad, USA). The protein bands were scanned and the intensities of the bands were measured using Image-pro Plus 6.0 analysis software (Media Cybernetics, Rockville, MD, USA).
Xu W., Liu J., Ma D., Yuan G., Lu Y, & Yang Y. (2017). Capsaicin reduces Alzheimer-associated tau changes in the hippocampus of type 2 diabetes rats. PLoS ONE, 12(2), e0172477.
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9

Validating Novel Fluorescent Biosensor

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Native polyacrylamide gel electrophoresis (PAGE) on 8% polyacrylamide gel was used to validate the designed novel fluorescent biosensor. Electrophoresis was conducted with 1× TBE buffer (89 mM Tris, 89 mM boric acid, and 2 mM EDTA) at pH 8.3 and 100 V constant voltage for 40 min. After this, the gel was stained with GV I for 30 min and then imaged using a Bio-Rad ChemDoc XRS (Bio-Rad, USA).
Ma H., Guo B., Yan X., Wang T., Que H., Gan X., Liu P, & Yan Y. (2019). A smart fluorescent biosensor for the highly sensitive detection of BRCA1 based on a 3D DNA walker and ESDR cascade amplification. RSC Advances, 9(34), 19347-19353.
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10

Western Blot Analysis of Klotho Protein

Cited 2 times
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Western blot analysis was performed as we described in our recent studies.13 (link), 14 (link), 25 (link) Briefly, an equal amount of serum from AKR/J and SAMP1 mice was diluted, treated with 4X Laemmli Sample buffer (Bio-RAD, Hercules, and CA) and loaded on a 4%–20% Express Plus™ PAGE gel (GenScript, NJ). The protein was transferred onto nitrocellulose filters after separation in the gel. Blots were blocked in 1% BSA in TBST for 1 hour at room temperature, and the membranes were incubated with Klotho primary antibody (R&D systems, AF1819) at 4°C overnight. The membranes were incubated with HRP-conjugated secondary antibodies for 1 hour at room temperature. Proteins were visualized, examined and quantified by densitometry using ChemDoc XRS with Quantity One Software (Bio-RAD, Hercules, and CA). Membranes were incubated in Ponceau Stain for internal loading control.
Chen J., Fan J., Wang S, & Sun Z. (2018). Secreted Klotho Attenuated Inflammation-Associated Aortic Valve Fibrosis in Senescence Accelerated Mice P1 (SAMP1). Hypertension (Dallas, Tex. : 1979), 71(5), 877-885.
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