C600 imaging system

Manufactured by Azure Biosystems

Sourced in United States

The C600 imaging system is a versatile and high-performance instrument designed for a variety of imaging applications. It features a large field of view, high resolution, and advanced image capture capabilities. The system is capable of capturing detailed images and data, making it a valuable tool for various scientific and research applications.

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Lab products found in correlation

Pierce bca protein assay kit, by Thermo Fisher Scientific (6 mentions) Odyssey blocking buffer, by LI COR (4 mentions) Nupage mes running buffer, by Thermo Fisher Scientific (3 mentions) Trans blot semi dry and turbo transfer system, by Bio-Rad (3 mentions) Ecl plus western blot detection reagents, by Bio-Rad (3 mentions) Pvdf membrane, by Bio-Rad (3 mentions) Tris glycine gel, by Thermo Fisher Scientific (3 mentions) Pd l1, by ProSci (3 mentions) Lf pvdf, by Bio-Rad (3 mentions) Bioruptor, by Diagenode (3 mentions) Clarity western ecl substrate, by Bio-Rad (2 mentions) Ripa buffer, by Thermo Fisher Scientific (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions) Acetyl alpha tubulin, by Cell Signaling Technology (2 mentions) Alpha tubulin, by Cell Signaling Technology (2 mentions) Ne pertm nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (1 mentions) Anti mouse hrp conjugated secondary antibody, by Cell Signaling Technology (1 mentions) Mini protean tgx, by Bio-Rad (1 mentions) Popculture reagent, by Merck Group (1 mentions) T per extraction reagent, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Azure c600 imaging system (40 citations) Azure c600 Gel Imaging System (11 citations) Azure c600 Western blot imaging system (8 citations) C600 system (7 citations) C600 Western Blot Imaging System (5 citations) Azure c600 visible fluorescent western blot imaging system (3 citations)

21 protocols using c600 imaging system

Quantifying Villin Expression in Enteroids

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Differentiated LT-treated and control enteroid monolayers were lysed using NE-PER^TM nuclear and cytoplasmic extraction reagents (Thermo Scientific). Cell membrane pellets were solubilized in PBS containing 1% Triton X-100 supplemented with a protease inhibitor cocktail (Pierce^TM protease inhibitor mini, Thermo Scientific). Equal amounts of total protein were loaded on a 4–20% gradient SDS-PAGE gel (Mini Protean TGX, Bio-Rad), then blotted onto nitrocellulose membranes and probed with anti-villin mouse monoclonal antibody (1:1000; Cat# SC-66022; Santa Cruz Biotechnology) followed by detection with HRP-conjugated anti-mouse secondary antibody (1:1000; Cat# 7076 S; Cell Signaling Technology). Blots were developed with Clarity Western ECL substrate (Bio-Rad) and imaged with a c600 imaging system (Azure Biosystems). Relative Villin expression signals were then analyzed with respect to corresponding Coomassie-stained gel using ImageJ analysis software.

Sheikh A., Tumala B., Vickers T.J., Martin J.C., Rosa B.A., Sabui S., Basu S., Simoes R.D., Mitreva M., Storer C., Tyksen E., Head R.D., Beatty W., Said H.M, & Fleckenstein J.M. (2022). Enterotoxigenic Escherichia coli heat-labile toxin drives enteropathic changes in small intestinal epithelia. Nature Communications, 13, 6886.

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Immunoblot Analysis of Protein Complexes

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Cell lysates were subjected to SDS-PAGE and proteins were transferred onto PVDF membranes. The following primary antibodies were used for detection of proteins by immunoblot: Rabbit anti-HA, rabbit anti-FLAG, rabbit or mouse anti-V5, rabbit anti-RUVBL1, rabbit anti-RUVBL2, mouse anti-RPAP3, rabbit anti-PIH1D1, rabbit anti-GAPDH, and mouse anti-Calnexin. Blots were probed with primary antibodies either 1–2 h at room temperature or overnight at 4 °C. Secondary incubations were performed for 1–2 h at room temp using either goat anti-rabbit HRP or goat anti-mouse HRP. Radiance chemiluminescence substrate (Azure Biosystems; Dublin, CA, USA) was used to visualize protein on an Azure c600 imaging system.

Morwitzer M.J., Tritsch S.R., Cazares L.H., Ward M.D., Nuss J.E., Bavari S, & Reid S.P. (2019). Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein. Viruses, 11(4), 372.

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Western Blot Analysis of RpoA-NTD and ProQ

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Cell lysates from β-gal assays were normalized based on pre-lysis OD₆₀₀. Lysates were mixed with 6× Laemmli loading dye with PopCulture Reagent (EMD Millipore Corp), boiled for 10 min at 95°C and electrophoresed on 10–20% Tris–glycine gels (Thermo Fisher) in 1× NuPAGE MES Running Buffer (Thermo Fisher). Proteins were transferred to PVDF membranes (BioRad) using a semi-dry transfer system (BioRad Trans-blot Semi-Dry and Turbo Transfer System) according to manufacturer's instructions, and probed with 1:10 000 primary antibody (anti-RpoA-NTD; Neoclone or anti-ProQ; kindly provided by G. Storz) overnight at 4°C and then a horseradish peroxidase (HRP)-conjugated secondary antibody (anti-mouse IgG or anti-rabbit IgG; Cell Signaling, 1:10 000). Note that, throughout the paper, ‘anti-ProQ’ is written out rather than using the standard abbreviation of ‘α-ProQ.’ This is to avoid confusion with the fusion protein we call ‘α-ProQ’ consisting of the NTD of RpoA (α) fused in frame to ProQ. Chemiluminescent signal from bound peroxidase complexes was detected using ECL Plus western blot detection reagents (BioRad) and a c600 imaging system (Azure) according to manufacturer's instructions.

Pandey S., Gravel C.M., Stockert O.M., Wang C.D., Hegner C.L., LeBlanc H, & Berry K.E. (2020). Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ. Nucleic Acids Research, 48(8), 4507-4520.

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Protein expression analysis of BMP4 signaling

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Following transcardiac perfusion, the DG from one hemisphere was microdissected on ice and mechanically homogenized in T-Per extraction reagent (ThermoFisher Scientific, catalog #78510) containing Halt protease and phosphatase inhibitors (ThermoFisher Scientific, catalog #78420). Lysates were centrifuged at 10,000 rpm for 15 min at 4°C and supernatant collected for Western blot analysis. Primary antibodies used were: mouse anti-BMP4 (1:1000, UM500038, OriGene), rabbit anti-noggin (1:1000, AB5729, Millipore), rabbit anti-phospho-Smad1/5/8 (1:500, AB3848, Millipore), rabbit anti-Smad1/5/8 (1:1000, sc-6031, Santa Cruz), and mouse anti-GAPDH (1:4000, MAB374, Millipore). Blots were imaged using Azure Biosystems C600 imaging system and densitometry analysis performed using ImageJ. When appropriate, blots were stripped using stripping buffer (ThermoFisher Scientific, catalog #46430) following manufacturer’s protocol.

Bonds J.A., Tunc-Ozcan E., Dunlop S.R., Rawat R., Peng C.Y, & Kessler J.A. (2023). Why Some Mice Are Smarter than Others: The Impact of Bone Morphogenetic Protein Signaling on Cognition. eNeuro, 10(1), ENEURO.0213-22.2022.

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SDS-PAGE Protein Analysis and Detection

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In preparation for sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), protein samples were diluted, prepared in 1x Laemmli sample buffer and heated at 95 °C for 10 min. Samples were loaded and electrophoretically separated using 4–12% TruPAGE Precast Gels (Sigma-Aldrich) at 180 V for 45 min. For total protein level determination, the gel was stained with GelCode Blue Stain Reagent (Thermo Scientific) or “Blue silver” colloidal Coomassie formulation (10% phosphoric acid, 10% ammonium sulfate, 0.12% G-250 dye, and 20% methanol) (Candiano et al., 2004 (link)). Confirmation of C4C5 constructs was performed by Western blot analysis. Briefly, proteins were transferred to PVDF membranes and probed with anti-His-tag antibody (Santa Cruz Biotechnology Inc. AD1.1.10, catalog # sc-53073, 1:10,000). Membranes and gels were imaged using the Azure Biosystems c600 Imaging system. Densitometric quantifications were performed using the ImageJ software available from the U.S. National Institutes of Health, Bethesda, MD, USA (Schneider et al., 2012 (link)).

Doh C.Y., Bharambe N., Holmes J.B., Dominic K.L., Swanberg C.E., Mamidi R., Chen Y., Bandyopadhyay S., Ramachandran R, & Stelzer J.E. (2022). Molecular characterization of linker and loop-mediated structural modulation and hinge motion in the C4-C5 domains of cMyBPC. Journal of structural biology, 214(2), 107856.

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VEGFC Protein Expression Analysis

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The Triton-soluble fraction of the lysates and the supernatants were boiled in sample buffer, run on SDS-PAGE, and immunoblotted with antibodies in a dilution of 1:1,000 against GFP (Abcam, ab6673), VEGFC (R&D Systems, AF752), and β-actin (Sigma-Aldrich, A2228). HRP-labeled, anti-mouse, and anti-goat secondary antibodies were used in a dilution of 1:10,000 followed by the application of PICO (Thermo Scientific) or ECL (Amersham, GE Healthcare) with detection by an Azure Biosystems c600 imaging system.
VEGFC protein expression in cell lysates and supernatants of the in vitro experiments was determined at different time points including 8 hours, 1, 2, 4, 8, and 12 days using a VEGFC Rat ELISA Kit (Invitrogen, BMS626-2) following the instructions of the manufacturer. To determine VEGFC protein expression in vivo at 1, 5, 10, 15, and 20 days after intradermal Poly(C) mRNA-LNP or VEGFC mRNA-LNP injection ear samples were digested with the Liberase II kit (Roche) and the secreted amount of VEGFC in the interstitial fluid of ear was determined using the same ELISA Kit described above. All investigators performing Western Blot or ELISA assays were blinded for the sample origin.

Szőke D., Kovács G., Kemecsei É., Bálint L., Szoták-Ajtay K., Aradi P., Styevkóné Dinnyés A., Mui B.L., Tam Y.K., Madden T.D., Karikó K., Kataru R.P., Hope M.J., Weissman D., Mehrara B.J., Pardi N, & Jakus Z. (2021). Nucleoside-modified VEGFC mRNA induces organ-specific lymphatic growth and reverses experimental lymphedema. Nature Communications, 12, 3460.

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Western Blot Analysis of β-Galactosidase

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Cell lysates from β-gal assays were normalized based on OD600 with LB plus PopCulture Reagent. Lysates were mixed with 6× Laemmli loading dye, boiled for 10 min at 95°C and electrophoresed on 10%–20% Tris–glycine gels (Thermo Fisher) in 1× NuPAGE MES Running Buffer (Thermo Fisher). Proteins were transferred to PVDF membranes (Bio-Rad) using a semidry transfer system (Bio-Rad Trans-blot Semidry and Turbo Transfer System) according to the manufacturer’s instructions. Membranes were probed with 1:10,000 primary antibody anti-ProQ overnight at 4°C and then a horseradish peroxidase (HRP)-conjugated secondary antibody (anti-rabbit IgG; 1:10,000). Chemiluminescent signal was detected using ECL Plus Western blot detection reagents (Bio-Rad) and a c600 imaging system (Azure) according to the manufacturer’s instructions.

Stein E.M., Wang S., Dailey K.G., Gravel C.M., Wang S., Olejniczak M, & Berry K.E. (2023). Biochemical and genetic dissection of the RNA-binding surface of the FinO domain of Escherichia coli ProQ. RNA, 29(11), 1772-1791.

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Western Blot Analysis of Protein Samples

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In our study, all of the cell samples were harvested using 1X Sample buffer (100 mM DTT, 2% SDS, 10% glycerol, 0.1% bromophenol blue and 50 mM Tris-HCl pH = 8) and resolved by SDS-PAGE. The samples were further transferred onto a nitrocellulose membrane and blocked with 5% nonfat dried milk diluted in 1X PBS for 1 h. The membrane was then incubated with primary antibody overnight at 4 °C, followed by incubation with secondary antibody for 1 h at room temperature. Finally, the protein bands were visualized using SuperSignal West Femto Maximum Sensitivity Substrate (Thermo Fisher Scientific) on the C600 Imaging System (Azure Biosystems). The results in different groups were quantified using ImageJ 1. x (National Institutes of Health).

Liu P., Luo G., Dodson M., Schmidlin C.J., Wei Y., Kerimoglu B., Ooi A., Chapman E., Garcia J.G, & Zhang D.D. (2020). The NRF2-LOC344887 signaling axis suppresses pulmonary fibrosis. Redox Biology, 38, 101766.

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Western Blot Protein Detection Protocol

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Cell lysates from β-gal assays were normalized based on OD600 with LB plus PopCulture Reagent. Lysates were mixed with 6× Laemmli loading dye, boiled for 10 min at 95°C and electrophoresed on 10–20% Tris–glycine gels (Thermo Fisher) in 1× NuPAGE MES Running Buffer (Thermo Fisher). Proteins were transferred to PVDF membranes (BioRad) using a semi-dry transfer system (BioRad Trans-blot Semi-Dry and Turbo Transfer System) according to manufacturer’s instructions. Membranes were probed with 1:10000 primary antibody anti-ProQ overnight at 4°C and then a horseradish peroxidase (HRP)-conjugated secondary antibody (anti-rabbit IgG; 1:10000). Chemiluminescent signal was detected using ECL Plus western blot detection reagents (Bio-Rad) and a c600 imaging system (Azure) according to manufacturer’s instructions

Stein E.M., Wang S., Dailey K., Gravel C.M., Wang S., Olejniczak M, & Berry K.E. (2023). Biochemical and genetic dissection of the RNA-binding surface of the FinO domain of Escherichia coli ProQ. bioRxiv.

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Quantifying UCP1 Expression via Western Blot

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To quantify UCP1 expression, total protein was extracted via standard methods in RIPA buffer (Thermo Scientific, Waltham, MA) with protease (Sigma, St. Louis, MO) and phosphatase (Roche, Basel, Switzerland) inhibitors added. Protein concentration was determined via BCA assay (Pierce, Rockford, IL). Western blot followed standard SDS-PAGE procedures using Mini-PROTEAN Tetra Cell (Bio-Rad, Hercules, CA) equipment. After transfer, gel was stained with 0.1% Coomassie G-250 (Thermo Scientific, Waltham, MA) and imaged to visualize total protein loading. Primary antibodies for rabbit anti-UCP1 (Thermo Fisher Scientific #PA1–24894) and mouse anti-GAPDH antibody (Ambion #AM4300, Carlsbad, CA) were used 1:1k and 1:2k, respectively, in TBST+5% nonfat dry milk. HRP-conjugated secondary antibodies for anti-rabbit and anti-mouse (Thermo Fisher Scientific #65–6120 and #31430, Rockford, IL) were used 1:30,000 in TBST+5% nonfat dry milk, bands visualized by ECL (Advantsa, Menlo Park, CA) and signals captured on a c600 imaging system (Azure Biosystems, Dublin, CA). Bands were quantitated using ImageJ density values, and UCP1 expression determined via total protein normalization (Aldridge et al. 2008 (link); Gilda and Gomes 2013 (link)).

Robbins A., Tom C.A., Cosman M.N., Moursi C., Shipp L., Spencer T.M., Brash T, & Devlin M.J. (2018). Low temperature decreases bone mass in mice: implications for humans. American journal of physical anthropology, 167(3), 557-568.

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