Enhanced chemiluminescence

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Enhanced chemiluminescence is a laboratory technique used to detect and quantify specific proteins in biological samples. It involves the use of chemiluminescent substrates that emit light when exposed to the target protein, allowing for sensitive and accurate detection.

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Lab products found in correlation

Hrp conjugated secondary antibody, by Southern Biotech (2 mentions) Nitrocellulose membrane, by Bio-Rad (2 mentions) Laemmli buffer, by Merck Group (2 mentions) Gapdh, by Thermo Fisher Scientific (1 mentions) E1j4e, by Cell Signaling Technology (1 mentions) Jla20, by Developmental Studies Hybridoma Bank (1 mentions)

4 protocols using enhanced chemiluminescence

Western Blot Analysis of Drosophila Proteins

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For western blot analysis, Drosophila heads were homogenized in 15 μl of 2x Laemmli buffer (Sigma-Aldrich). Samples were boiled for ten minutes and subjected to SDS-PAGE. Protein were transferred onto nitrocellulose membranes (Bio-Rad), blocked in 2% milk in PBS with 0.05% Tween 20 (PBSTw), and incubated overnight at 4°C with primary antibodies. Membranes were washed three times with PBSTw and incubated for three hours with appropriate HRP-conjugated secondary antibody (SouthernBiotech) at room temperature. Following multiple washes with PBSTw, proteins were visualized by enhanced chemiluminescence (Alpha Innotech). Protein transfer and loading were monitored by Ponceau S staining and by reprobing blots with an antibody directed to GAPDH. All immunoblots were repeated at least three times. Primary antibodies to the following proteins were used at the indicated concentrations: α-synuclein (1:6,000,000, H3C, Developmental Studies Hybridoma Bank), GAPDH (1:40,000, Invitrogen), cofilin (1:1,000,000, Anna Marie Sokac).

Sarkar S., Olsen A.L., Sygnecka K., Lohr K.M, & Feany M.B. (2021). α-synuclein impairs autophagosome maturation through abnormal actin stabilization. PLoS Genetics, 17(2), e1009359.

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Western Blot Analysis of MM Cells

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MM cells were lysed as previously described [6 (link)]. Protein from each sample was subjected to SDS-PAGE. Proteins were subsequently transferred to nitrocellulose membranes and blocked with 5% milk in a Tris-buffered saline solution containing 0.1% Tween-20 for 1 h. The blots were probed overnight with primary antibodies, washed, and then probed with species-specific secondary antibodies coupled to HRP. Immunoreactive material was detected by enhanced chemiluminescence (Alpha Innotech, San Jose, CA).

Kelly K.R., Espitia C.M., Zhao W., Wendlandt E., Tricot G., Zhan F., Carew J.S, & Nawrocki S.T. (2015). Junctional adhesion molecule-A is overexpressed in advanced multiple myeloma and determines response to oncolytic reovirus. Oncotarget, 6(38), 41275-41289.

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Western Blot Analysis of AML Cells

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AML cells were incubated with MLN4924, ara-C, or the combination of both drugs for 24 h as indicated. Cells were then lysed for 1 h on ice in Triton X-100 lysis buffer (1% triton X-100, 150 mM NaCl, 25 mM Tris pH 7.5) with protease inhibitors. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes. Blots were probed with the indicated antibodies and bands were detected by enhanced chemiluminescence (Alpha Innotech, San Leandro, CA) as previously described (21 (link)). β-tubulin documented equal loading.

Nawrocki S.T., Kelly K.R., Smith P.G., Keaton M., Carraway H., Sekeres M.A., Maciejewski J.P, & Carew J.S. (2014). The NEDD8-activating enzyme inhibitor MLN4924 disrupts nucleotide metabolism and augments the efficacy of cytarabine. Clinical cancer research : an official journal of the American Association for Cancer Research, 21(2), 439-447.

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Drosophila Western Blot Analysis

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For western blot analysis Drosophila heads were homogenized in 15 μl of 2× Laemmli buffer (Sigma-Aldrich). Samples were boiled for ten minutes and subjected to SDS-PAGE. Protein were transferred onto nitrocellulose membranes (Bio-Rad), blocked in 2% milk in PBS with 0.05% Tween 20 (PBSTw) and incubated overnight at 4°C with primary antibodies. Membranes were washed three times with PBSTw and incubated for three hours with appropriate HRP-conjugated secondary antibody (SouthernBiotech) at room temperature. Following multiple washes with PBSTw, proteins were visualized by enhanced chemiluminescence (Alpha Innotech). Protein transfer and loading were monitored by Ponceau S staining. Blots were reprobed with an antibody directed to actin to illustrate equivalent protein loading in figures. All immunoblots were repeated at least three times. Primary antibodies to the following proteins were used at the indicated concentrations: actin (1:1000, JLA20, Developmental Studies Hybridoma Bank), GFP (1:1000, JL-8, Clontech), GABARAP/Atg8a (1:2000, E1J4E, Cell Signaling), Ref2P/p62 (1:3000, 178440, Abcam).

Nithianandam V., Sarkar S, & Feany M.B. (2024). Pathways controlling neurotoxicity and proteostasis in mitochondrial complex I deficiency. Human Molecular Genetics, 33(10), 860-871.

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