Enhanced chemiluminescence detection system

Manufactured by Santa Cruz Biotechnology

Sourced in United States

The Enhanced chemiluminescence detection system is a laboratory equipment designed to detect and quantify specific proteins or molecules in a sample using chemiluminescence technology. It provides sensitive and accurate detection of target analytes.

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Lab products found in correlation

Colorimetric protein assay kit, by Bio-Rad (9 mentions) Nitrocellulose membrane, by Cytiva (5 mentions) Biomax mr film, by Kodak (4 mentions) Sc 1615, by Santa Cruz Biotechnology (4 mentions) Mouse anti β actin antibody, by Santa Cruz Biotechnology (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Horseradish peroxidase conjugated goat anti mouse igg secondary antibody, by Santa Cruz Biotechnology (3 mentions) Chemidoc imaging system, by Bio-Rad (3 mentions) Cyquant, by Thermo Fisher Scientific (3 mentions) Image lab, by Bio-Rad (3 mentions) Cleaved caspase 3, by Cell Signaling Technology (3 mentions) Notch1, by Cell Signaling Technology (3 mentions) β actin, by Proteintech (3 mentions) N1icd, by Cell Signaling Technology (3 mentions) Sc 30080, by Santa Cruz Biotechnology (2 mentions) Ab76026, by Abcam (2 mentions) Sc 365626, by Santa Cruz Biotechnology (2 mentions) Sc 11407, by Santa Cruz Biotechnology (2 mentions) Rabbit anti trkb antibody, by Santa Cruz Biotechnology (2 mentions) Rabbit anti bdnf, by Santa Cruz Biotechnology (2 mentions)

Spelling variants of this product

Enhanced chemiluminescence (65 citations) Enhanced chemiluminescence system (37 citations) Chemiluminescence detection system (9 citations) Enhanced chemiluminescence western blotting detection system (8 citations) Enhanced chemiluminescence detection (5 citations) Enhanced Chemiluminescence (ECL) detection system (2 citations) Enhanced chemiluminescence western blot detection system (2 citations)

45 protocols using enhanced chemiluminescence detection system

Western Blot Analysis of Cardiac Proteins

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The total proteins were purified from the LA free wall, separated by 10 % SDS-PAGE, and then transferred onto a polyvinylidene difluoride membrane. This was blocked at room temperature for 1 h in Tris-buffered saline with 0.5 % Tween 20 containing 5 % skim milk and probed with primary antibodies overnight at 4 °C.
The following primary antibodies were independently used to detect specific proteins: collagen I (1:500 dilution, Bioworld, USA), collagen III (1:500 dilution, Bioworld, USA), MPO (1:200 dilution, Santa Cruz, USA), matrix metalloproteinase (MMP)-2 (1:500 dilution, ProteinTech, USA), MMP-9 (1:500 dilution, ProteinTech, USA), and tissue inhibitors of metalloproteinase (TIMP)-1 (1:1000 dilution, Abcam, USA). An antibody against β-actin (1:1000 dilution, ProteinTech, USA) was used as an internal control.
Horseradish peroxidase-conjugated anti-goat (1:10000 dilution, Beyotime, China) or anti-mouse (1:10000 dilution, ZSGB Biological Company, China) IgGs were used to bind the primary antibodies. Protein bands on Western blots were visualized using an enhanced chemiluminescence detection system (Santa Cruz, USA). Relative band densities of proteins in Western blots were normalized against β-actin.

Yang Q., Qi X., Dang Y., Li Y., Song X, & Hao X. (2016). Effects of atorvastatin on atrial remodeling in a rabbit model of atrial fibrillation produced by rapid atrial pacing. BMC Cardiovascular Disorders, 16, 142.

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Nrf2-Keap1 Pathway Regulation Analysis

Cited 2 times

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Whole-cell and nuclear extracts were prepared as previously described [35 (link)]. Western blot analysis was performed as described previously [29 (link)]. Briefly, cell extracts (10–40 μg/lane) were separated by 8–10% SDS polyacrylamide gel electrophoresis and electroblotting, and proteins were detected using antibodies against p-Nrf2 (ab76026, Abcam), Nrf2 (ab62352, Abcam), Keap1 (sc-365626, Santa Cruz Biotechnology), HO-1 (ADI-SPA-895-F, Enzo Life Sciences, NY, USA), SOD-1 (sc-11407, Santa Cruz Biotechnology), SOD-2 (sc-30080, Santa Cruz Biotechnology), lamin B1 (ab16048, Abcam), and β-actin (sc-47778, Santa Cruz Biotechnology). After detection with horseradish peroxidase-conjugated secondary antibody (anti-mouse or -rabbit), proteins were visualized using an enhanced chemiluminescence detection system (Santa Cruz Biotechnology) and an EZ-Capture ST imaging system (Atto, Tokyo, Japan). β-actin was used as the loading control. The densitometry data represent the mean ± standard error (SE) from three immunoblots and are shown as the relative density of protein bands normalized to the indicated protein (input Nrf2, input Keap1, actin, or lamin B1).

Kim H.S., Lim J.W, & Kim H. (2022). Korean Red Ginseng Extract Inhibits IL-8 Expression via Nrf2 Activation in Helicobacter pylori-Infected Gastric Epithelial Cells. Nutrients, 14(5), 1044.

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Western Blotting for BDNF and TrkB Quantification

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Western blotting for the determination of BDNF and TrkB was conducted, according to the previous method (Park et al., 2017 (link)). Hippocampal samples were homogenized on ice and lysed in a lysis buffer containing 50 mM Tris-HCl (pH, 7.5), 150 mM NaCl, 0.5% deoxycholic acid, 1% Nonidet P40, 0.1% sodium dodecyl sulfate (SDS), 1 mM phenylmethylsulfonyl fluoride, and 100 mg/mL leupeptin. Protein content was measured using a Bio-Rad colorimetric protein assay kit (Bio-Rad, Hercules, CA, USA). Thirty micrograms of total protein were separated on SDS-polyacrylamide gels and transferred onto a nitrocellulose membrane. The membrane was blocked with dehydrated milk, then incubated with mouse anti-β-actin antibody (1:1,000; Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit anti-BDNF antibody (1:1,000; Santa Cruz Biotechnology), and rabbit anti-TrkB antibody (1:1,000; Santa Cruz Biotechnology). After washing, horseradish peroxidase-conjugated, appropriate secondary antibodies were applied. Incubations were performed at room temperature. The bands were detected using the enhanced chemiluminescence detection system (Santa Cruz Biotechnology), and quantified using an Image-Pro Plus computer-assisted image analysis system (Media Cyberbetics Inc., Silver Spring, MD, USA).

Park S.S., Shin M.S., Park H.S., Kim T.W., Kim C.J, & Lim B.V. (2019). Treadmill exercise ameliorates nicotine withdrawal-induced symptoms. Journal of Exercise Rehabilitation, 15(3), 383-391.

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Western Blot Analysis of Protein Targets

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Cells were collected and lysed in TNES buffer. Equal aliquots of proteins were electrophoresed on SDS‐polyacrylamide gels and electrotransferred onto PVDF membranes. Membranes were blocked with TBS containing 5% nonfat dry milk for at least 1 hour. The blots were then incubated with 1 of the following Abs: anti‐ITGA6, anti‐ASAP3, anti‐musashi homolog 2 (MSI2) (Boster, Wuhan, China), anti‐cysteine‐rich with EGF‐like domains 1 (CRELD1), or anti‐β‐actin (Abcam, Cambridge, UK). Proteins were visualized with peroxidase‐conjugated secondary Abs at 1:2000 for 1 hour, using an enhanced chemiluminescence detection system (Santa Cruz Biotechnology, Santa Cruz, CA, USA).

Guo L., Fu J., Sun S., Zhu M., Zhang L., Niu H., Chen Z., Zhang Y., Guo L, & Wang S. (2019). MicroRNA‐143‐3p inhibits colorectal cancer metastases by targeting ITGA6 and ASAP3. Cancer Science, 110(2), 805-816.

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Evaluating Protein Levels in Pancreatic Tissue

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Western blotting was performed to evaluate the protein expression levels of α-SMA and fibronectin. Pancreatic tissue homogenates (120 μg protein/lane) were separated by 8% to 12% SDS-PAGE and transferred onto nitrocellulose membranes (Amersham Inc., Arlington Heights, IL, USA) by electroblotting. Membranes were then incubated with antibodies against α-SMA (1:5,000, sc-53015; Santa Cruz Biotechnology, Dallas, TX, USA), fibronectin (1:100, sc-8422; Santa Cruz Biotechnology), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:3,000, sc-47724; Santa Cruz Biotechnology) at 4°C overnight. Following incubation, membranes were washed with TBS with Tween-20. The primary antibodies were then detected using horseradish peroxidase (HRP)-conjugated secondary antibodies, and visualized using enhanced chemiluminescence detection system (Santa Cruz Biotechnology) according to the manufacturer’s instruction. GAPDH was used as loading control. Expression levels were standardized to GAPDH expression level. Further, data were processed and quantified using volume analysis and molecular analysis software, respectively.

Lee S., Jeong Y.K., Lim J.W, & Kim H. (2019). Docosahexaenoic Acid Inhibits Expression of Fibrotic Mediators in Mice With Chronic Pancreatitis. Journal of Cancer Prevention, 24(4), 233-239.

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Western Blot Analysis of Protein Expression

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Whole cell lysates were prepared in lysis buffer as described. Equivalent amounts of protein (5μg) were mixed with LDS buffer (Invitrogen) containing 2.5mM DTT, heated at 90°C for 5min, and loaded into 4–12% Bis-Tris NuPAGE gels (Invitrogen). Proteins were electrophoretically separated, transferred to a PVDF membrane (Immobilon Millipore), and probed with one of the following primary antibodies: 1:4000 dilution of mouse anti-tetra-His monoclonal antibody (34679; Qiagen) to detect NS1 or 1:10000 dilution of mouse anti-β-actin monoclonal antibody (A1978; Sigma). Bound antibodies were detected with a 1:2000 dilution of horseradish peroxidase-conjugated goat anti-mouse IgG (H+L) secondary antibody (474-1806; KPL and an enhanced chemiluminescence detection system (Santa Cruz Biotechnology).

Morrison C.R, & Scholle F. (2014). Abrogation of TLR3 inhibition by discrete amino acid changes in the C-terminal half of the West Nile virus NS1 protein. Virology, 0, 96-107.

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Western Blot Analysis of AQP1 Protein

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Total protein sample was extracted from cell lines with RIPA lysis buffer and protein concentration was determined using the BCA protein assay kit (both from Beyotime Institute of Biotechnology). Then, equal amount of protein sample (30 µg) was separated on 10% SDS-PAGE and transferred onto PVDF membranes (EMD Millipore). Blocking of membranes was performed with 5% (w/v) skimmed milk in Tris buffered saline with 0.2% Tween-20 (TBST) for 2 h at room temperature. Then, the membranes were incubated with primary antibodies against AQP1 (1:1,000; cat. no. ab168387; Abcam) and GAPDH (1:5,000; cat. no. ab8245; Abcam) overnight at 4°C. After washed with TBST, membranes were incubated with goat anti-rabbit IgG-horseradish peroxidase secondary antibody (MBS435036; MyBioSource) for 2 h at room temperature and visualized via an enhanced chemiluminescence detection system (Santa Cruz Biotechnology, Inc.).

Kong B., Zhao S., Kang X, & Wang B. (2021). MicroRNA-133a-3p inhibits cell proliferation, migration and invasion in colorectal cancer by targeting AQP1. Oncology Letters, 22(3), 649.

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Quantifying Hippocampal Protein Levels

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Western blot analysis for BDNF, TrkB, and AMPK was done as previously explained method [14 ,22 (link)]. Lysis buffer was applied to lyse hippocampal tissues, and protein content was detected by a colorimetric protein assay kit (Bio-Rad, Hercules, CA, USA). Sodium dodecyl sulfate-polyacrylamide gel was used to separated 30-μg protein, then reaction mixture was transferred to a nitrocellulose membrane, stopped reaction by applying dehydrated milk, and then incubated by primary antibodies. Mouse anti-β actin (1:3,000; Santa Cruz Biotechnology, Santa Cruz, CA, USA), rabbit anti-BDNF (1:1,000; Santa Cruz Biotechnology), rabbit anti-TrkB (1:1,000; Santa Cruz Biotechnology), and rabbit anti-AMPK (1:1,000; Santa Cruz Biotechnology) were selected as the primary antibodies. Horseradish peroxidaseconjugated secondary antibodies were used, and enhanced chemiluminescence detection system (Santa Cruz Biotechnology) measured the expression of bands.

Kim S.H., Hwang L., Jin J.J., Ko I.G., Kim Y.B., Yoon H.S, & Baek S.S. (2021). Resistance Exercise Improves Spatial Learning Ability Through Phosphorylation of 5’-Adenosine Monophosphate-Activated Protein Kinase in Parkinson Disease Mice. International Neurourology Journal, 25(Suppl 2), S55-S62.

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Western Blot Analysis of Liver Proteins

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Western blot analysis for Bax, Bcl-2, and AMPK was done as the same method of Park et al. (2020) (link). After homogenizing liver tissues on ice, the tissues were lysed using lysis buffer. Protein content was calculated using Bio-Rad colorimetric protein assay kit (Bio-Rad, Hercules, CA, USA). After separation of 40-μg protein on sodium dodecyl sulfate-poly-acrylamide gels, it was transferred to the nitrocellulose membrane. Then, the reaction mixture was treated with primary antibodies such as mouse β-actin antibody (1:3,000; Santa Cruz Biotechnology), mouse Bcl-2 antibody (1: 1,000; Santa Cruz Biotechnology), rabbit Bax antibody (1:1,000; Santa Cruz Biotechnology), and rabbit AMPK antibody (1:1,000; Santa Cruz Biotechnology). Horseradish peroxidase-conjugated anti-mouse antibodies for β-actin and Bcl-2 and horseradish peroxidase-conjugated anti-rabbit antibodies for Bax and AMPK were used as the secondary antibodies. The expression for bands was analyzed using enhanced chemiluminescence detection system (Santa Cruz Biotechnology).

Kim S.H., Ko I.G., Jin J.J., Hwang L., Yoon H.S, & Baek S.S. (2022). Treadmill exercise ameliorates ethanol with lipopolysaccharide and carbon tetrachloride-mediated liver injury in mice. Journal of Exercise Rehabilitation, 18(1), 28-33.

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Western Blotting Analysis of Nrf2, KEAP1, and HO-1

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Whole-cell extracts (6–40 μg/per lane) were loaded onto 8–10% SDS polyacrylamide gels and separated by electrophoresis under reducing conditions. The proteins were then transferred by electroblotting and verified by using reversible staining with Ponceau S. The membranes were blocked using 3% non-fat dry milk in TBS-T (Tris-buffered saline and 0.2% Tween 20). The proteins were detected with antibodies for Nrf2 (sc-722, Santa Cruz Biotechnology, Dallas, TX, USA), p-Nrf2 (ab76026, Abcam, Cambridge, UK), KEAP 1 (sc-365626, Santa Cruz Biotechnology), and HO-1 (ADI-SPA-895, Enzo Life Science Inc., Farmingdale, NY, USA). The antibodies were diluted in TBS-T containing 3% dry milk and incubated with the membrane overnight at 4 °C. After washing with TBS-T, primary antibodies were detected with horseradish peroxidase-conjugated secondary antibodies (anti-rabbit, anti-mouse, anti-goat) and visualized by using the enhanced chemiluminescence detection system (Santa Cruz Biotechnology, Dallas, TX, USA) and BioMax MR film (Kodak, Rochester, NY, USA). The protein levels were compared to that of the loading control actin, or histone H1.

Kyung S., Lim J.W, & Kim H. (2019). α-Lipoic Acid Inhibits IL-8 Expression by Activating Nrf2 Signaling in Helicobacter pylori-infected Gastric Epithelial Cells. Nutrients, 11(10), 2524.

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