Enhanced chemiluminescence detection system

Manufactured by PerkinElmer

Sourced in United States

The enhanced chemiluminescence detection system is a laboratory equipment designed to detect and measure chemiluminescent signals. It provides a sensitive and quantitative approach for analyzing various biological samples.

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Lab products found in correlation

Polyvinylidene difluoride membrane, by Merck Group (11 mentions) Pvdf membrane, by Bio-Rad (9 mentions) Protease inhibitor cocktail, by Roche (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Semi dry transfer, by Bio-Rad (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Protein assay kit, by Bio-Rad (2 mentions) Immobilon p membrane, by Merck Group (2 mentions) Sds page gel, by Merck Group (2 mentions) β actin, by Merck Group (2 mentions) Anti β actin, by Merck Group (2 mentions) Fitc conjugated goat anti mouse igg, by Merck Group (1 mentions) Hybond ecl, by GE Healthcare (1 mentions) Anti myc tag mouse monoclonal antibody, by Cell Signaling Technology (1 mentions) Hybond, by Cytiva (1 mentions) Polyvinylidene fluoride (pvdf), by Merck Group (1 mentions) P ampk, by Cell Signaling Technology (1 mentions) Horseradish peroxidase coupled secondary antibody, by Cytiva (1 mentions) Anti β actin antibody, by Merck Group (1 mentions) Rabbit anti collagen 1, by Abcam (1 mentions)

Spelling variants of this product

Enhanced chemiluminescence (148 citations) Enhanced chemiluminescence system (35 citations) Chemiluminescence detection system (16 citations) Enhanced chemiluminescence detection (10 citations) Chemiluminescence system (6 citations) Enhanced Chemiluminescence (ECL) Western Blot detection system (2 citations) Enhanced chemiluminescence Western blot detection system (2 citations) Enhanced chemiluminescence (ECL) detection system (2 citations)

45 protocols using enhanced chemiluminescence detection system

Western Blot and Immunocytochemistry for Protein Detection

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For Western blotting, the samples were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions and transferred onto Hybond-ECL (GE Healthcare). The recombinant proteins were detected using mouse monoclonal anti-Myc tag antibody (Cell Signaling Technology) (1:500) as primary antibody and HRP-conjugated rabbit anti-mouse IgG antibody (Thermo Fisher Scientific) (1:1,000) as secondary antibody. Immunoreactive bands were visualized using an enhanced chemiluminescence detection system (PerkinElmer) as described (Yamashita et al., 2002 (link)).
To detect Cebelin by immunocytochemical analysis, mouse monoclonal anti-Myc tag antibody and FITC-conjugated goat anti-mouse IgG (Sigma-Aldrich) were used as primary and secondary antibodies, respectively. To detect Mannosidase II, EEA1, and GRP78, rabbit anti-Mannosidase II antibody, anti-EEA1 antibody, and anti-GRP78 antibody (Abcam) and TRITC-conjugated goat anti-rabbit antibody (Sigma-Aldrich) were used as primary and secondary antibodies, respectively.

Miwa H, & Itoh N. (2018). Unknown genes, Cebelin and Cebelin-like, predominantly expressed in mouse brain. Heliyon, 4(9), e00773.

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Immunoblotting Protocol for Macrophage Lysis

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Immunoblotting was performed as previously mentioned elsewhere [15 (link)]. Infected or treated macrophages were lysed in RIPA buffer constituting 50 mM Tris-HCl (pH 7.4), 1% NP-40, 0.25% Sodium deoxycholate, 150 mM NaCl, 1 mM EDTA, 1 mM PMSF, 1 μg/ml of each aprotinin, leupeptin, pepstatin, 1 mM Na₃VO₄ and 1 mM NaF. Equal amount of protein from each cell lysate was resolved on a 12% SDS-polyacrylamide gel and transferred to polyvinylidene difluoride membranes (PVDF) (Millipore) by the semi-dry transfer (Bio-Rad) method. Nonspecific binding was blocked with 5% nonfat dry milk powder in TBST [20 mM Tris-HCl (pH 7.4), 137 mM NaCl, and 0.1% Tween 20] for 60 min. The blots were incubated overnight at 4°C with primary antibody followed by incubation with anti-rabbit-HRP or anti-mouse-HRP secondary antibody in 5% BSA for 2 h. After washing in TBST, the immunoblots were developed with enhanced chemiluminescence detection system (Perkin Elmer) as per manufacturer’s instructions. β-ACTIN was used as loading control.

Holla S., Prakhar P., Singh V., Karnam A., Mukherjee T., Mahadik K., Parikh P., Singh A., Rajmani R.S., Ramachandra S.G, & Balaji K.N. (2016). MUSASHI-Mediated Expression of JMJD3, a H3K27me3 Demethylase, Is Involved in Foamy Macrophage Generation during Mycobacterial Infection. PLoS Pathogens, 12(8), e1005814.

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SDS-PAGE and Western Blot Protocol

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The total protein samples from cell lysates after IPTG induction were mixed with SDS buffer (125 mM Tris-HCl, pH 6.8, 5% glycerol, 4% SDS, 0.005% bromophenol blue, and 10% 2-mercaptoethanol). Extracts were subjected to 12% SDS-polyacrylamide gel electrophoresis and transferred onto a polyvinylidene difluoride membrane (Merck Millipore, Darmstadt, Germany). After blocking with 5% nonfat dry milk for 30 min, the membranes were incubated with the indicated antibodies for 1 h at room temperature followed by incubation with secondary antibodies (HRP-conjugated anti-mouse or anti-rabbit IgG at the appropriate dilutions) for 45 min at room temperature. Antibody binding was detected with an enhanced chemiluminescence detection system (PerkinElmer, Waltham, USA).

Tomiyama L., Kamino H., Fukamachi H, & Urano T. (2017). Precise epitope determination of the anti-vimentin monoclonal antibody V9. Molecular Medicine Reports, 16(4), 3917-3921.

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Protein Analysis by Gel Electrophoresis and Western Blotting

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Gel electrophoresis and western blotting were performed as previously described.[ 21 ] Briefly, proteins were subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis and then transferred to nitrocellulose membranes. After blocking in 5% dried skimmed milk in 0.05% Tween-20/Tris-buffered saline (TBS) buffer, the membranes were incubated with primary antibodies followed by peroxidase-conjugated secondary antibodies in 5% dried skimmed milk in 0.05% Tween-20/TBS buffer. Proteins were visualized on X-ray film using an enhanced chemiluminescence detection system (PerkinElmer Co., Waltham, MA, USA).

Yamana Y., Fujihara S., Kobara H., Oura K., Samukawa E., Chiyo T., Okamura M., Yamana H., Tadokoro T., Fujita K., Morishita A., Iwama H, & Masaki T. (2022). MicroRNA profiles following telmisartan treatment in pancreatic ductal adenocarcinoma cells. Journal of cancer research and therapeutics, 18(Supplement).

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Neuronal Protein Extraction and Western Blot

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Total protein was extracted from neurons by using RIPA contained 1% PMSF. A bicinchoninic acid (BCA) method was used to determine protein concentration. Then the protein was separated by SDS-PAGE and transferred to Polyvinylidene Fluoride (PVDF) membranes (Bio-Rad Laboratories, Inc., Hercules, CA, USA). The membranes were incubated with 5% milk for 2 h and then incubated with LC3b, Beclin-1, p62 and ATG5 primary antibody (1:1,000 dilution) overnight at 4°C. After washing three times with TBST, the membranes were incubated secondary antibody labeled with horseradish peroxidase at 37°C for 2 h and exposed to an enhanced chemiluminescence detection system (PerkinElmer, Inc., Waltham, MA, USA) with ECL plus regent (Thermo Fisher Scientific, Inc.). Semi-quantitative analysis of protein bands was performed using an AlphaEaseFC 4.0 software.

He J.L., Dong X.H., Li Z.H., Wang X.Y., Fu Z.A, & Shen N. (2018). Pterostilbene inhibits reactive oxygen species production and apoptosis in primary spinal cord neurons by activating autophagy via the mechanistic target of rapamycin signaling pathway. Molecular Medicine Reports, 17(3), 4406-4414.

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Chondrocyte Protein Extraction and Western Blot Analysis

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After treatments as described in the experimental design, chondrocytes in 10 cm dishes were washed with cold phosphate-buffered saline (PBS) and incubated with RIPA containing 1 mM phenylmethylsulfonyl fluoride, followed by cell scraping and centrifugation. The nuclear protein was isolated as recommended by the manufacturer (Beyotime, Shanghai, China). After measuring protein concentration with the bicinchoninic acid (BCA) assay, 40 μg total protein containing loading buffer was separated by SDS-PAGE and transferred to PVDF membranes. The membranes were immersed in 5% nonfat milk for 2 h to block non-specific antigen and then incubated with primary antibodies (LC3, 1:1000; ATG5, 1:800; p-p65, 1:500; p65, 1:500; IκBα, 1:500) overnight at 4 °C. After incubation with secondary antibodies (1:2000), an enhanced chemiluminescence detection system (PerkinElmer, USA) with an ECL reagent was used to expose proteins on the membrane. A semi-quantitative analysis of protein bands was performed using AlphaEaseFC 4.0 software.

Jiang L.B., Meng D.H., Lee S.M., Liu S.H., Xu Q.T., Wang Y, & Zhang J. (2016). Dihydroartemisinin inhibits catabolism in rat chondrocytes by activating autophagy via inhibition of the NF-κB pathway. Scientific Reports, 6, 38979.

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Western Blot Analysis of VEGF-C Signaling

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Cells were incubated in serum-free DMEM/F12 for 24 hours before treatment with or without rhVEGF-C (100 ng/mL). Cells were lysed in RIPA buffer [Tris-HCl (50 mM; pH 7.5), NaCl (120 mM), NP-40 (0.5%), Na₃VO₄ (200 mM), EDTA (100 mM), sodium deoxycholate (0.5%), SDS (1%)] for 10 minutes on ice. An equal quantity of protein from the cell lysates was resuspended in gel sample buffer, resolved by 10% SDS-PAGE, and transferred to polyvinylidene difluoride membrane membranes (Millipore Corp., Milford, MA). After blocking, membranes were incubated with specific primary antibodies and corresponding secondary antibodies. Immunoreaction signals were visualized by an enhanced chemiluminescence detection system (PerkinElmer Health Sciences, Waltham MA).

Chang Y.W., Su C.M., Su Y.H., Ho Y.S., Lai H.H., Chen H.A., Kuo M.L., Hung W.C., Chen Y.W., Wu C.H., Chen P.S, & Su J.L. (2014). Novel peptides suppress VEGFR-3 activity and antagonize VEGFR-3-mediated oncogenic effects. Oncotarget, 5(11), 3823-3835.

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Immunoblotting Analysis of Cell Signaling

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Immunoblotting was performed as done before [19 (link)]. Primary antibodies against ACC (#3662, 1:1000), phospho-acetyl-CoA carboxylase (pACC) (#3661, 1:500), AMPK (#2532, 1:1000), pAMPK (#2535, 1:500), GLI1 (#2534, 1:500) from Cell Signaling Technologies (Beverly, MA, USA), cyclin D1 (CCND1) (sc-8396, 1:200) and PTCH1 (sc-6149, 1:200) from Santa Cruz (Dallas, TX, USA) and GLI2 (600-401-845, 1:1000) from Rockland Immunochemicals (Limerick, PA, USA) were used. Β-actin (Cell Signaling Technologies, #4967, 1:1000) was used as loading control. An enhanced chemiluminescence detection system (Perkin Elmer, Waltham, MA, USA) was used to visualize immune-reactive proteins using Fujifilm LAS-3000 mini camera (Fujifilm, Germany). Protein expression was quantified using ImageJ 1.50.

Gonnissen A., Isebaert S., McKee C.M., Muschel R.J, & Haustermans K. (2017). The Effect of Metformin and GANT61 Combinations on the Radiosensitivity of Prostate Cancer Cells. International Journal of Molecular Sciences, 18(2), 399.

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Rat Hypothalamus Protein Analysis

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Rat hypothalamus samples were homogenized in an ice-cold lysis buffer containing 150 mmol/l NaCl, 50 mmol/l Tris-HCl (pH 8.0), 0.1% SDS, 1% Nonidet P-40, a PhosSTOP Phosphatase Inhibitor Cocktail (Rosche, Osaka, Iapan) and protease inhibitor cocktail (Boehringer Mannheim, Lewes, UK). These samples were resolved by 10% SDS-polyacrylamide gel electrophoresis and transferred to polyvinylidene fluoride membranes (Immobilon, Bedford, MA). The membranes were incubated with anti-β actin antibody (Sigma, Tokyo, Japan, #A5316), anti-phospho-acetyl CoA carboxylase (ACC) (Ser79) antibody (Upstate Cell Signaling, Lake Placid, NY, #07–303), anti-AMPK, anti-phospho AMPK (Thr172) and anti-ACC antibodies, (Cell Signaling Technology, Beverly, MA, #4150, #2531, and #3662 respectively), washed, and incubated with horseradish peroxidase-coupled secondary antibodies (Amersham, Buckinghamshire, UK). The blots were visualized using an enhanced chemiluminescence detection system (Perkin Elmer Life Science, Boston, MA).

Kume S., Kondo M., Maeda S., Nishio Y., Yanagimachi T., Fujita Y., Haneda M., Kondo K., Sekine A., Araki S.I., Araki H., Chin-Kanasaki M., Ugi S., Koya D., Kitahara S., Maeda K., Kashiwagi A., Uzu T, & Maegawa H. (2016). Hypothalamic AMP-Activated Protein Kinase Regulates Biphasic Insulin Secretion from Pancreatic β Cells during Fasting and in Type 2 Diabetes. EBioMedicine, 13, 168-180.

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Quantification of Cardiac Extracellular Matrix

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The left ventricles were homogenized in an ice-cold RIPA lysis buffer (Thermo Scientific, Waltham, MA) with a protease inhibitor cocktail (Roche Applied Science, Mannheim, Germany). These samples were loaded in 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to polyvinylidene difluoride membranes (Millipore). The membranes were then incubated with rabbit anti-collagen 1 (1 : 5000, Abcam, Cambridge, MA, USA), rabbit anti-TGF-β1 (1 : 1000, Abcam), or rabbit anti-tubulin (1 : 5000, Millipore) antibodies overnight. After that, membranes were washed and incubated with goat anti-rabbit HRP-coupled secondary antibodies (1: 10,000). The results were visualized by an enhanced chemiluminescence detection system (PerkinElmer, Boston, MA, USA).

Liu W., Gong W., He M., Liu Y., Yang Y., Wang M., Wu M., Guo S., Yu Y., Wang X., Sun F., Li Y., Zhou L., Qin S, & Zhang Z. (2018). Spironolactone Protects against Diabetic Cardiomyopathy in Streptozotocin-Induced Diabetic Rats. Journal of Diabetes Research, 2018, 9232065.

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