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Chemiluminescence

Manufactured by Abclone

Chemiluminescence is a laboratory equipment that produces light through a chemical reaction. It is used to measure the presence and quantity of specific compounds or molecules.

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4 protocols using chemiluminescence

1

Western Blot Protein Analysis Protocol

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Cells were lysed in lysis buffer A [20 mM HEPES (pH 7.5), 150 mM NaCl, 1 mM EDTA, 2 mM EGTA, 1% Triton X-100, 10% glycerol, and protease cocktail I/II; Sigma], and cellular debris was removed by centrifugation at 10,000× g for 10 min. Proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transferred onto nitrocellulose membranes, blocked with 5% skim milk in 0.01 M TBS (pH 7.5) containing 0.5% Tween 20, and blotted with the appropriate primary antibodies. The antigen–antibody complexes were detected by chemiluminescence (Abclone, Seoul, Korea). All of the uncropped images of western blot used in Figures can be found it Figure S9.
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2

Western Blot Protein Detection

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The cells were lysed in lysis buffer A (20 mM N-2-hydroxyethyl piperazine-Nʹ-2-ethanesulfonic acid [pH 7.5], 150 mM NaCl, 1 mM EDTA, 2 mM ethylene glycol tetraacetic acid, 1% Triton X-100, 10% glycerol, and protease cocktail I/II; Sigma). Cell debris was removed by centrifugation at 10,000 × g for 10 min. The proteins were separated using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes. The membranes were then blocked with 5% skimmed milk in 0.01 M TBS (pH 7.5) containing 0.5% Tween 20 and blotted with the appropriate primary antibodies. The antigen–antibody complexes were detected using chemiluminescence (Abclone, Korea).
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3

Western Blot Analysis of Protein Lysates

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Cells were lysed in lysis buffer A (20 mM N-2-hydroxyethylpiperazine-N0-2-ethanesulfonic acid [pH 7.5], 150 mM NaCl, 1 mM EDTA, 2 mM ethylene glycol tetraacetic acid, 1% Triton X-100, 10% glycerol, and protease cocktail I/II; Sigma), and cellular debris was removed by centrifugation at 10,000 × g for 10 minutes. Proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transferred onto nitrocellulose membranes, blocked with 5% skim milk in 0.01 M TBS (pH 7.5), containing 0.5% Tween 20, and blotted with the appropriate primary antibodies. The antigen-antibody complexes were detected by chemiluminescence (Abclone, Korea).
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4

Protein Extraction and Western Blot

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Cells were lysed in lysis buffer A (20 mM HEPES [pH 7.5], 150 mM NaCl, 1 mM EDTA, 2 mM EGTA, 1% Triton X-100, 10% glycerol, and protease cocktail [Sigma]), and the lysate was cleared by centrifugation at 10, 000 × g for 10 minutes. Proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transferred onto nitrocellulose membranes, blocked with 5% skim milk in 0.01 M TBS (pH 7.5) containing 0.5% Tween 20, and blotted with the appropriate primary antibodies. The antibodiesantigen complexes were detected by chemiluminescence (Abclone).
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