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Chemidoc mp imaging station

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The ChemiDoc MP imaging station is a versatile laboratory instrument designed for capturing and analyzing images of various biomolecular samples, such as gels, blots, and plates. It provides high-quality imaging and quantitative analysis capabilities for a wide range of applications in molecular biology, biochemistry, and cell biology research.

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Lab products found in correlation

Anti zswim8, by Thermo Fisher Scientific (2 mentions) Hrp conjugated antirabbit secondary, by Jackson ImmunoResearch (2 mentions) Femto clean ecl solution, by Thermo Fisher Scientific (2 mentions) Anti gapdh, by Cell Signaling Technology (2 mentions) Page gels, by Merck Group (2 mentions) Anti flag m2 antibody, by Merck Group (2 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (2 mentions) Western lightning, by PerkinElmer (2 mentions) Phsl ser563, by Santa Cruz Biotechnology (2 mentions) P perilipin, by Merck Group (2 mentions) Phsl ser660, by Cell Signaling Technology (2 mentions) Fluorophore conjugated secondary antibody, by Thermo Fisher Scientific (2 mentions) Erk1 2, by Santa Cruz Biotechnology (2 mentions) P erk1 2, by Santa Cruz Biotechnology (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Gapdh, by Bio-Rad (1 mentions) T per, by Thermo Fisher Scientific (1 mentions) M per, by Thermo Fisher Scientific (1 mentions) Gapdh, by Abcam (1 mentions) β actin, by Bio-Rad (1 mentions)

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ChemiDoc MP station ChemiDoc Imaging Station ChemiDoc MP imaging ChemiDoc station ChemiDoc MP Imaging Chemidoc Imaging station ChemiDoc

10 protocols using chemidoc mp imaging station

1

Immunoblot analysis of intestinal proteins

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Protein was extracted from intestinal mucosa dissected from mouse intestine (20–50 µg protein per lane) or total lysates from cells (106/well, 6-well plates) from in vitro experiments. Tissue or cell lysates were extracted in T-Per or M-Per (Thermo Fisher Scientific), respectively, supplemented with protease and phosphatase inhibitors (Roche, St. Louis, MO). Protein was quantified by immunoblot analysis employing antibodies to: GFP (cat. #13970, 1:1000), Axin2 (cat. #32197, 1:1000), c-Myc (cat. #32072, 1:1000) from Abcam; GAPDH (cat. #2118, 1:5000), β-catenin (cat. #8480, 1:1000), human APC (cat. #2504, 1:1000), TCF4 (cat. #2569, 1:1000), β-actin (cat. #4967, 1:3000), phosphorylated VASP-ser239 (cat. #3114, 1:1000) from Cell Signaling Technology (Danvers, MA); mouse APC (cat. #896, 1:1000) from Santa Cruz Biotechnology (Dallas, TX); GUCA2A (cat. # HPA018215, 1:100) from Sigma or guanylin antisera (#2538, 1:100);56 (link) and GUCY2C (1:500).34 (link) Immunoblot images were captured on the BioRad ChemiDoc MP imaging station and bands were quantified by densitometry normalized to that of GAPDH or β-actin using ImageJ. Average relative intensity reflects at least two independent experiments each with at least three biological replicates.
Blomain E.S., Rappaport J.A., Pattison A.M., Bashir B., Caparosa E., Stem J., Snook A.E, & Waldman S.A. (2020). APC-β-catenin-TCF signaling silences the intestinal guanylin-GUCY2C tumor suppressor axis. Cancer Biology & Therapy, 21(5), 441-451.
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2

Purification and Characterization of CbpA Variants

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CbpAs used in this study were CbpA2, CbpA3 and variants thereof, CbpA5, and CbpA6. CbpAs2,3,5,6 were expressed and purified as previously published (16 ) (see Supplemental Text for details). Protein purity was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE) analysis (Fig. S10A–E), visualized with Coomassie blue staining using a ChemiDoc MP Imaging Station (Bio-Rad). Concentrations of CbpAs and variants thereof were determined using absorbance readings at 280 nm, employing extinction coefficients and molecular weights calculated with Expasy (Table S4). The concentration of CbpA396–283 was estimated with a Bradford assay (Amresco), using bovine serum albumin as a calibration standard.
Huard D.J., Johnson A.M., Fan Z., Kenney L.G., Xu M., Drori R., Gumbart J.C., Dai S., Lieberman R.L, & Glass J.B. (2023). Molecular basis for inhibition of methane clathrate growth by a deep subsurface bacterial protein. PNAS Nexus, 2(8), pgad268.
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3

Native PAGE Analysis of RNA Complexes

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Native PAGE conditions were prepared by casting 10×10 cm 10% PAGE gels using 30% acrylamide/bis-acrylamide (29:1) solution (Sigma-Aldrich A3574), 10% ammonium persulfate, tetramethylethylenediamine, and the Native PAGE buffer. The final concentration of the native PAGE buffer in 10% PAGE gel was 40 mM K-HEPES (pH 7.5), 100 mM KCl and 5 mM MgCl2. After polymerization, the samples were run at 40 V for 2 h in a water-cooled PAGE chamber to keep the buffer temperature at ~25°2. For staining, gels were incubated in the native PAGE buffer containing 10 μM DFHO for 15 min. DFHO-stained gels were analyzed on a ChemiDoc MP imaging station (Bio-Rad) at 470/30 nm excitation and 530/28 nm emission (green channel) and 530/28 nm excitation and 605/50 nm emission (red channel). Each presented image is an overlay of both scans. Next, counterstaining with SYBR Gold (ThermoFisher S11494) 1:10,000 diluted in the native PAGE buffer was performed for 15 min followed by gel imaging to detect all RNA species in each lane. SYBR Gold-stained bands were imaged using UV excitation (302 nm) and 590/110 nm emission on the ChemiDoc MP imaging station.
Kim H, & Jaffrey S.R. (2019). A fluorogenic RNA-based sensor activated by metabolite-induced RNA dimerization. Cell chemical biology, 26(12), 1725-1731.e6.
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4

ZSWIM8 Western Blot Analysis

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Brains from E18.5 mice were homogenized in lysis buffer (40 mM HEPES at pH 7.4, 2 mM EDTA, 2 mM EGTA, 150 mM NaCl, 1% Triton X-100) supplemented with 1× complete protease inhibitor cocktail and 1× complete phosphatase inhibitor cocktail (Roche) using a Precellys Evolution homogenizer (Bertin Technologies). Approximately 100 μg of lysate was resolved on 8% SDS-PAGE, blotted onto nitrocellulose membranes, and probed with anti-ZSWIM8 (1:400; Thermo PA5-59492) or anti-GAPDH (1:1000; Cell Signaling 2118) followed by HRP-conjugated antirabbit secondary (1:10,000; Jackson ImmunoResearch 111-035-144). Chemiluminescence detection was performed using Femto Clean ECL solution (Thermo Fisher) with a Chemidoc MP imaging station (Bio-Rad).
Jones B.T., Han J., Zhang H., Hammer R.E., Evers B.M., Rakheja D., Acharya A, & Mendell J.T. (2023). Target-directed microRNA degradation regulates developmental microRNA expression and embryonic growth in mammals. Genes & Development, 37(13-14), 661-674.
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5

Western Blot Analysis of Macrophages and Microglia

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After day 19 (human iPSC-derived macrophages), day 40 (human iPSC-derived microglia), or day 7 (BMDM) of differentiation, cells were washed with ice-cold phosphate-buffered saline and then lysed in 50 mM Tris pH 7.4, 150 mM Nacl, 1% TX-100, 0.5% deoxycholate, and 0.1% SDS) containing protease inhibitor and phosphatase inhibitor cocktails (Roche cOmplete and PhosSTOP) and spun at 13,000 g for 5 min. The supernatant was collected and incubated at 95 °C for 3 min in SDS sample buffer before separation by SDS–PAGE on 4 to 15% gradient Mini-PROTEAN TGX precast polyacrylamide gels and transferred to nitrocellulose membranes (Bio-Rad, Hercules CA). Membranes were next blocked with 5% milk in TBS with 0.1% Tween 20 and incubated with primary antibodies and then HRP-coupled secondary antibodies in 5% milk or bovine serum albumin in TBS with 0.1% Tween 20. Chemiluminescence detection was performed on a Chemidoc MP imaging station (Bio-Rad), and FIJI/ImageJ was used to quantify band intensities (80 (link)). A detailed protocol is available at 10.17504/protocols.io.6qpvr41dzgmk/v1.
Yadavalli N, & Ferguson S.M. (2023). LRRK2 suppresses lysosome degradative activity in macrophages and microglia through MiT-TFE transcription factor inhibition. Proceedings of the National Academy of Sciences of the United States of America, 120(31), e2303789120.
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6

Native PAGE Analysis of Corn Protein

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Native PAGE conditions were prepared by casting 10 × 10 cm 10% PAGE gels (29:1 acrylamide:bisacrylamide; Sigma) using using native PAGE buffer, i.e. the same final buffer composition as used for all the in vitro assays (40 mM HEPES, pH 7.5, 100 mM KCl, 5 mM MgCl2). After polymerization, the samples were run at 40 V for at least 2 h in a water-cooled PAGE chamber to keep the buffer temperature at ~25°C.
For staining, gels were incubated in buffer containing 10 μM DFHO for 15 min. Gels were then imaged to detect DFHO-Corn complexes. DFHO-stained gels were analyzed on a ChemiDoc MP imaging station (BioRad) at 470/30 nm excitation and 530/28 nm emission (green channel) and 530/28 nm excitation and 605/50 nm emission (red channel). Next, counterstaining with 1X SYBR Gold was performed for 15 min followed by gel imaging to detect all RNA species in each lane. SYBR Gold-stained bands were imaged using UV excitation (302 nm) and 590/110 nm emission on the ChemiDoc MP imaging station.
Song W., Filonov G.S., Kim H., Hirsch M., Li X., Moon J.D, & Jaffrey S.R. (2017). Imaging RNA polymerase III transcription using a photostable RNA-fluorophore complex. Nature chemical biology, 13(11), 1187-1194.
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7

Native PAGE Analysis of Corn Protein

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Native PAGE conditions were prepared by casting 10 × 10 cm 10% PAGE gels (29:1 acrylamide:bisacrylamide; Sigma) using using native PAGE buffer, i.e. the same final buffer composition as used for all the in vitro assays (40 mM HEPES, pH 7.5, 100 mM KCl, 5 mM MgCl2). After polymerization, the samples were run at 40 V for at least 2 h in a water-cooled PAGE chamber to keep the buffer temperature at ~25°C.
For staining, gels were incubated in buffer containing 10 μM DFHO for 15 min. Gels were then imaged to detect DFHO-Corn complexes. DFHO-stained gels were analyzed on a ChemiDoc MP imaging station (BioRad) at 470/30 nm excitation and 530/28 nm emission (green channel) and 530/28 nm excitation and 605/50 nm emission (red channel). Next, counterstaining with 1X SYBR Gold was performed for 15 min followed by gel imaging to detect all RNA species in each lane. SYBR Gold-stained bands were imaged using UV excitation (302 nm) and 590/110 nm emission on the ChemiDoc MP imaging station.
Song W., Filonov G.S., Kim H., Hirsch M., Li X., Moon J.D, & Jaffrey S.R. (2017). Imaging RNA polymerase III transcription using a photostable RNA-fluorophore complex. Nature chemical biology, 13(11), 1187-1194.
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8

Western Blot Analysis of Signaling Proteins

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Protein samples were denatured in Laemmli buffer, and loaded onto SDS-PAGE gels and transferred to PVDF membranes (Millipore, Billerica, MD). Membranes were then incubated overnight at 4 °C in wash buffer (10 mM Tris, pH 7.5, 100 mM NaCl, 0.1% Tween-20) containing 1% BSA with the primary antibody. Antibodies were obtained from Cell Signaling Technology [pHSL Ser660 (Cat. 4126), pHSL Ser563 (Cat. 4139), HSL (Cat. #4107), pERK1/2 (Cat. 4370), and ERK 1/2 (Cat. 4695)], Santa Cruz Biotechnology [Actin (Cat. #SC69879)], Vala Biosciences [p-perilipin (Cat. 4854), perilipin (Cat. 4856)], and Sigma [M2 anti-FLAG antibody (Cat. F1804)]. The membrane was then rinsed with wash buffer and incubated for 1 h at room temperature in wash buffer containing 1% BSA with 1:2500 HRP-conjugated secondary antibody (Santa Cruz Biotechnology) or 1:2500 fluorophore-conjugated secondary antibody (Life Technologies). After further washing, membranes were visualized using enhanced chemiluminescence (Western Lightning, Perkin-Elmer) or imaged directly for fluorescent secondary antibodies and recorded on a BioRad ChemiDoc MP imaging station.
Krishnamoorthy L., Cotruvo JA J.r., Chan J., Kaluarachchi H., Muchenditsi A., Pendyala V.S., Jia S., Aron A.T., Ackerman C.M., Vander Wal M.N., Guan T., Smaga L.P., Farhi S.L., New E.J., Lutsenko S, & Chang C.J. (2016). Copper Regulates Cyclic AMP-Dependent Lipolysis. Nature chemical biology, 12(8), 586-592.
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9

ZSWIM8 Protein Expression Analysis

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Brains from E18.5 mice were homogenized in lysis buffer (40 mM HEPES, pH 7.4, 2 mM EDTA, 2 mM EGTA, 150 mM NaCl, 1% Triton X-100) supplemented with 1X complete protease inhibitor cocktail and 1X complete phosphatase inhibitor cocktail (Roche) using a Precellys Evolution homogenizer (Bertin Technologies). Approximately 100 μg of lysate was resolved on 8% SDS-PAGE, blotted onto nitrocellulose membranes, and probed with anti-ZSWIM8 (1:400; Cat #PA5-59492, Thermo) or anti-GAPDH (1:1000; Cat #2118, Cell Signaling) followed by HRP-conjugated anti-rabbit secondary (1:10,000; Cat #111-035-144, Jackson ImmunoResearch). Chemiluminescence detection was performed using Femto Clean ECL Solution (Thermo Fisher) with a Chemidoc MP Imaging Station (BioRad).
Jones B.T., Han J., Zhang H., Hammer R.E., Evers B.M., Rakheja D., Acharya A, & Mendell J.T. (2023). Target-directed microRNA degradation regulates developmental microRNA expression and embryonic growth in mammals. bioRxiv.
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10

Western Blot Analysis of Signaling Proteins

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Protein samples were denatured in Laemmli buffer, and loaded onto SDS-PAGE gels and transferred to PVDF membranes (Millipore, Billerica, MD). Membranes were then incubated overnight at 4 °C in wash buffer (10 mM Tris, pH 7.5, 100 mM NaCl, 0.1% Tween-20) containing 1% BSA with the primary antibody. Antibodies were obtained from Cell Signaling Technology [pHSL Ser660 (Cat. 4126), pHSL Ser563 (Cat. 4139), HSL (Cat. #4107), pERK1/2 (Cat. 4370), and ERK 1/2 (Cat. 4695)], Santa Cruz Biotechnology [Actin (Cat. #SC69879)], Vala Biosciences [p-perilipin (Cat. 4854), perilipin (Cat. 4856)], and Sigma [M2 anti-FLAG antibody (Cat. F1804)]. The membrane was then rinsed with wash buffer and incubated for 1 h at room temperature in wash buffer containing 1% BSA with 1:2500 HRP-conjugated secondary antibody (Santa Cruz Biotechnology) or 1:2500 fluorophore-conjugated secondary antibody (Life Technologies). After further washing, membranes were visualized using enhanced chemiluminescence (Western Lightning, Perkin-Elmer) or imaged directly for fluorescent secondary antibodies and recorded on a BioRad ChemiDoc MP imaging station.
Krishnamoorthy L., Cotruvo JA J.r., Chan J., Kaluarachchi H., Muchenditsi A., Pendyala V.S., Jia S., Aron A.T., Ackerman C.M., Vander Wal M.N., Guan T., Smaga L.P., Farhi S.L., New E.J., Lutsenko S, & Chang C.J. (2016). Copper Regulates Cyclic AMP-Dependent Lipolysis. Nature chemical biology, 12(8), 586-592.
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