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Enhanced chemi luminescence (ecl)

Manufactured by Vector Laboratories
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ECL is a chemiluminescent detection reagent used for Western blot analysis. It provides a sensitive and reliable method for detecting target proteins labeled with horseradish peroxidase (HRP).

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Lab products found in correlation

Wheat germ agglutinin (wga), by Vector Laboratories (2 mentions) Rca 1, by Vector Laboratories (2 mentions) Mal 2, by Vector Laboratories (1 mentions) Streptavidin fitc, by BioLegend (1 mentions) Facscanto 2, by BD (1 mentions) Streptavidin biotin blocking kit, by Vector Laboratories (1 mentions) Dylight 488 conjugated neutravidin, by Thermo Fisher Scientific (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Vector Laboratories (1 mentions) Uea 1, by Vector Laboratories (1 mentions) Concanavalin a (cona), by Vector Laboratories (1 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (1 mentions) Chemidoc mp imaging system, by Bio-Rad (1 mentions)

4 protocols using enhanced chemi luminescence (ecl)

1

Quantifying Sialylation in Murine Cardiac Tissue

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To determine the relative levels of sialylation, the Erythrina cristagalli lectin (ECL, Vector Lab, CA) was used to probe murine left ventricular sections. ECL binds preferentially to terminal unsubstituted galactose β1,4 N-acetylglucosamine (Galβ1,4GlcNAc) [68 (link)]. Biotinylated ECL with an avidin–biotin–fluorophore system was applied on paraformaldehyde-fixed paraffin-embedded WT and ST3Gal4−/− cardiac tissues, as described previously [7 , 8 , 28 (link), 47 (link), 68 (link)]. Specifically, tissue sections were blocked for endogenous biotin (Streptavidin/Biotin blocking kit, Vector Lab, CA) and non-specific binding (Vector Lab, CA) before incubation with 1:200 biotinylated ECL for 2 h at room temperature. Tissue sections were then incubated 2 h at room temperature with 1:1000 Dylight™ 488 conjugated NeutrAvidin (Thermo Scientific, MA) followed by 4,6-diamidino-2-phenylindole (DAPI, Vector Lab, CA) counterstain. No positive staining was observed for the negative controls in which biotinylated lectin, Dylight 488 conjugated neutravidin or both were omitted. Multiple sections from each of two to three hearts per condition were studied, with the data showing staining for a given condition among slices consistent with that shown in Fig. 5.
Deng W., Ednie A.R., Qi J, & Bennett E.S. (2016). Aberrant sialylation causes dilated cardiomyopathy and stress-induced heart failure. Basic research in cardiology, 111(5), 57.
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2

Lectin Staining of Cell Surfaces

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Totally, 2 x 105 cells were stained with 200 µl of 10 µg/ml fluorescein isothiocyanate or biotin-conjugated MAL I, MAL II, SNA, AAL, WGA, and ECL (Vector Laboratories) in lectin staining buffer (PBS, 1% FBS, 0.1 mM CaCl2) for 30 min on ice followed by washing twice with the same buffer. When using biotinylated lectins, additional incubation with streptavidin-FITC (Biolegend) for 20 min on ice was performed. Before the analysis using a FACScanto II flow cytometer (BD Bioscience), cells were washed twice and resuspended in lectin staining buffer.
Parshenkov A, & Hennet T. (2022). Glycosylation-Dependent Induction of Programmed Cell Death in Murine Adenocarcinoma Cells. Frontiers in Immunology, 13, 797759.
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3

Platelet Surface Glycan and Receptor Analysis

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Platelet surface β1–4 galactose exposure using FITC-conjugated R. communis agglutinin I (RCA-I, Vector Labs) and FITC-conjugated E. cristagalli lectin (ECL, Vector Labs), and Mpl expression were determined by flow cytometry.20 (link) To determine Mpl internalization platelets were incubated with 50 ng ml−1 TPO for 10 min at 37 °C or not (rest), then all samples were incubated with a rabbit antibody directed against the extracellular domain of Mpl (provided by Dr. Wei Tong, UPenn) or control rabbit IgG, followed by Alexa Fluor 488-labeled goat anti-rabbit IgG antibody, and analyzed by flow cytometry.
Grozovsky R., Begonja A.J., Liu K., Visner G., Hartwig J.H., Falet H, & Hoffmeister K.M. (2014). The Ashwell-Morell receptor regulates hepatic thrombopoietin production via JAK2-STAT3 signaling. Nature medicine, 21(1), 47-54.
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4

Carbohydrate and Glycosylation Analysis of PcH

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Total PcH carbohydrate content was determined by the phenol sulfuric acid method (Dubois et al., 1956). Biotinylated lectins were used for the analysis of PcH glycosylation pattern, namely PVL, BSL 1, JAC, SBA, Con A, WGA, DBA, UEA 1, PNA, RCA I, ECL, PSA and LCA (Vector Labs, Burlingame, CA, USA). Dots containing 5 μg of PcH were adsorbed onto nitrocellulose strips (Hybond, GE Healthcare, Uppsala, Sweden) and incubated for 1.5 h at 37°C in a humid environment. After washing with PBS-Tween 0.1%, the strips were then blocked overnight at 4°C with 3% (w/v) oxidized BSA in PBS. Then, each strip was incubated 1.5 h at 37°C with a different lectin at limiting concentrations to avoid nonspecific binding. After five washes in PBS-Tween 0.1% binding was detected using a horseradish peroxidase–streptavidin conjugate (Vector Labs) and visualized by chemiluminescence using the Immobilon Western Chemiluminescent HRP Substrate (Sigma-Aldrich) in a ChemiDoc MP Imaging System (Bio-Rad Laboratories, Inc.) and analyzed with ImageJ software (NIH).
Chiumiento I.R., Ituarte S., Sun J., Qiu J.W., Heras H, & Dreon M.S. (2020). Hemocyanin of the caenogastropod Pomacea canaliculata exhibits evolutionary differences among gastropod clades. PLoS ONE, 15(1), e0228325.
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