Chemiluminescent imaging system

Manufactured by Bio-Techne

The Chemiluminescent Imaging System is a laboratory equipment designed for the detection and analysis of chemiluminescent signals. It provides a sensitive and quantitative method for visualizing and capturing images of chemiluminescent samples, such as those used in Western blotting, ELISA, and other biochemical assays.

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Lab products found in correlation

Bca kit, by Thermo Fisher Scientific (3 mentions) Gapdh, by Cell Signaling Technology (2 mentions) Complete protease inhibitor, by Roche (2 mentions) Connexin 43, by Cell Signaling Technology (1 mentions) Complete edta free protease inhibitor, by Roche (1 mentions) Cell lysis buffer, by Cell Signaling Technology (1 mentions) Mini trans blot electrophoretic transfer cell system, by Bio-Rad (1 mentions) Protein assay kit, by Bio-Rad (1 mentions) Grp78, by Cell Signaling Technology (1 mentions) Caspase 3, by Cell Signaling Technology (1 mentions) Anti flag primary antibody, by Proteintech (1 mentions) Nuclear protein extraction kit, by Solarbio (1 mentions) Anti gapdh primary antibody, by Proteintech (1 mentions)

6 protocols using chemiluminescent imaging system

Western Blotting and Co-Immunoprecipitation Protocols

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For Western blotting, fat tissue and liver tissue were homogenized on ice in 1% CHAPS extraction buffer containing complete protease inhibitors (Roche Bioscience, #04693159001) and 0.1 mM Na₃VO₄ for inhibiting phosphatase. The homogenates were rotated for 30 min at 4°C to ensure extraction of membrane proteins. After centrifugation at 15,000×g for 120 min, supernatants were collected and protein concentration was measured with the BCA protein assay reagent (Pierce). Equal amounts of protein lysates were resolved on 4-12% Bis-Tris NuPAGE gels, followed by standard Western blotting with the antibodies specified above. Chemiluminescent signals were scanned and integrated density values were calculated with a chemiluminescent imaging system (Alpha Innotech).
For Co-IP, 3T3L1 cells were first grown in DMEM for 24 h in 60-mm plates to ~ 80% confluence and then transfected with the indicated expression constructs. After being cultured for 48 h, cells were lysed and equal amounts of lysates (500 μg in 1 ml) were used for immunoprecipitation with Myc or Flag-conjugated beads overnight. The extensively-washed immunoprecipitates were resolved on a 4-12% NuPage Bis-Tris gel, followed by standard Western blotting with the antibodies specified above. Chemiluminescent signals were scanned and integrated density values were calculated with a chemiluminescent imaging system (Alpha Innotech).

Xiang R., Fan L.L., Huang H., Chen Y.Q., He W., Guo S., Li J.J., Jin J.Y., Du R., Yan R, & Xia K. (2018). Increased RTN3 leads to obesity and hypertriglyceridemia by interacting with HSPA5. Circulation, 138(17), 1828-1838.

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Western Blot Analysis of AC16 Cell Proteins

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For Western blot analysis, the cultured AC16 cells were homogenized on ice in 1% CHAPS extraction buffer (150 mM KCl, 50 mM HEPES, pH 7.4, 0.1% CHAPS) containing complete™ EDTA-free Protease Inhibitor (Roche Bioscience) and 0.1 mM Na₃VO₄ to inhibit phosphatases. The homogenates were rotated for 30 min at 4°C to ensure the extraction of membrane proteins. After centrifugation at 15,000 × g for 120 min, the supernatant was collected, and protein concentrations were measured with BCA protein assay reagent (Pierce). Equal amounts of lysate proteins were resolved on 4–12% Bis-Tris NuPAGE gels, followed by standard Western blotting with the antibodies specified below. Chemiluminescent signals were scanned, and integrated density values were calculated with a chemiluminescent imaging system (Alpha Innotech). The antibodies of HIS, DSG2, Connexin 43, and GAPDH were purchased from Cell Signaling Technology (USA).

Liu L., Chen C., Li Y, & Yu R. (2019). Whole-Exome Sequencing Identified a De Novo Mutation of Junction Plakoglobin (p.R577C) in a Chinese Patient with Arrhythmogenic Right Ventricular Cardiomyopathy. BioMed Research International, 2019, 9103860.

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Western Blotting of Brain Proteins

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For western blotting, snap-frozen brain sections were homogenized on ice in 1% CHAPS extraction buffer containing complete protease inhibitors (Roche Bioscience) and 0.1 mM Na₃VO₄ for inhibiting phosphatase. The homogenates were rotated for 30 min at 4 °C to ensure extraction of membrane proteins. After centrifugation at 15,000 × g for 120 min, supernatants were collected and protein concentration was measured with the BCA protein assay reagent (Pierce). Equal amounts of lysate proteins were resolved on 4–12% bis–tris NuPage gels, followed by standard Western blotting with the antibodies specified above. Chemiluminescent signals were scanned and integrated density values were calculated with a chemiluminescent imaging system (Alpha Innotech, San Leandro, CA).

Shi Q., Ge Y., He W., Hu X, & Yan R. (2017). RTN1 and RTN3 protein are differentially associated with senile plaques in Alzheimer’s brains. Scientific Reports, 7, 6145.

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Quantifying Adrenergic Receptor Subtypes in Ovine MCA

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As noted, ovine MCA were cleaned of adventitia and the endothelium was denuded in a phosphate-free balanced salt solution (BSS) of the following composition (mM): 126 NaCl; 5 KCl; 10 HEPES; 1 MgCl₂; 2 CaCl₂; 10 glucose; pH 7.4 (adjusted with NaOH). The arteries were homogenized with a tissue grinder in ice-cold cell lysis buffer (Cell Signaling Technology, Danvers, MA), as described previously [12] (link). Protein concentrations were measured using a protein assay kit (Bio-Rad Laboratories, Hercules, CA) and bovine serum albumin (BSA) was used as a reference protein standard. Mini Trans-Blot Electrophoretic Transfer Cell system (Bio-Rad Laboratories) was used to transfer proteins from the gel to a nitrocellulose membrane at 100 V for 3 h. We then performed an overnight incubation of subtype specific primary antibodies (1∶500 dilution) for α1A-, α1B-, and α1D-AR (Santa Cruz Biotechnology, Santa Cruz, CA). We used α-actin as an internal control for equal protein loading, as well as the blocking peptide for each subtype specific antibody as a negative control (Santa Cruz Biotechnology). The membrane was then incubated in chemiluminescence luminol reagent (Pierce, Rockford, IL) for 1 min, and the protein band was detected using Alpha Innotech Chemiluminescent imaging system (San Leandro, CA).

Goyal R., Goyal D., Chu N., Van Wickle J, & Longo L.D. (2014). Cerebral Artery Alpha-1 AR Subtypes: High Altitude Long-Term Acclimatization Responses. PLoS ONE, 9(11), e112784.

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Western Blot Analysis of Cellular Stress

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Real‐time PCR referred to our previous study (Liu & Luo, 2018). For western blotting, one milliliter of cultured medium was removed from each well and centrifuged at 16,000 × g for 10 min at 4°C, and cell protein was extracted using RIPA lysis buffer and the concentration was measured using a BCA kit (Thermo Fisher Scientific). Bis‐Tris NuPAGE gels (4%–12%) were used to separate the protein by electrophoresis. Chemiluminescent signals were scanned using a chemiluminescent imaging system (Alpha Innotech). The antibodies against HIS, CHOP, GRP78, Caspase 3, and GAPDH were purchased from Cell Signaling Technology.

Liu L., Qin J., Guo T., Chen P., Ouyang R., Peng H, & Luo H. (2020). Identification and functional characterization of a novel surfactant protein A2 mutation (p.N207Y) in a Chinese family with idiopathic pulmonary fibrosis. Molecular Genetics & Genomic Medicine, 8(9), e1393.

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Protein Extraction and Western Blot

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Nuclear and cytosolic proteins from 293T cells were extracted using Nuclear Protein Extraction Kit (Solarbio). SDS-PAGE was performed using a 12.5% PAGE Gel Rapid Preparation Kit (Yeasen). Lysates were mixed with SDS-gel sample buffer and heated at 90°C for 10 min. Then, the protein samples were loaded onto the PAGE gels. After electrophoresis, the bands were electrophoretically transferred onto a nitrocellulose membrane. After blocking with 1% bovine serum albumin (BSA) in Tris-buffered saline, the membranes were incubated with anti-FLAG primary antibody (Proteintech, 20543-1-AP, 1:5,000), anti-GAPDH primary antibody (Proteintech, 10494-1-AP, 1:5,000), and anti-Histone-H3 polyclonal antibody (Proteintech, 17168-1-AP, 1:1,000). Chemiluminescent signals were scanned, and integrated density values were calculated with a chemiluminescent imaging system (Alpha Innotech).

Jin J.Y., Wu P.F., Luo F.M., Guo B.B., Zeng L., Fan L.L., Tang J.Y, & Xiang R. (2022). GLIS Family Zinc Finger 1 was First Linked With Preaxial Polydactyly I in Humans by Stepwise Genetic Analysis. Frontiers in Cell and Developmental Biology, 9, 781388.

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