Luminescent image analyzer

Manufactured by GE Healthcare

Sourced in Sweden, United States, United Kingdom

The Luminescent image analyzer is a laboratory equipment designed to detect and analyze luminescent signals. It is used to quantify and visualize luminescent samples, such as those in biochemical and molecular biology applications.

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Lab products found in correlation

Protease inhibitor cocktail, by Merck Group (5 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Pvdf membrane, by Merck Group (3 mentions) Enhanced bca protein assay kit, by Beyotime (2 mentions) β tubulin, by CWBIO (2 mentions) Flag tag (flag), by Merck Group (2 mentions) Anti flag, by Merck Group (2 mentions) Imagequant las 4000, by GE Healthcare (2 mentions) Nanodrop 2000 spectrophotometer, by Thermo Fisher Scientific (2 mentions) Immobilon, by Merck Group (1 mentions) Anti bdnf, by Santa Cruz Biotechnology (1 mentions) Anti gapdh, by Abcam (1 mentions) Anti muc1 c, by Abcam (1 mentions) Anti muc 1, by BD (1 mentions) Bca assay kit, by Thermo Fisher Scientific (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions) Trans blot turbo mini pvdf transfer pack, by Bio-Rad (1 mentions) Ebm 2, by PromoCell (1 mentions) Halt protease and phosphatase inhibitor cocktail, by Thermo Fisher Scientific (1 mentions) Dc protein assay, by Bio-Rad (1 mentions)

Spelling variants of this product

ImageQuant LAS 4000 Luminescent Image Analyzer (27 citations) LAS-1000 plus Luminescent Image Analyzer (13 citations) LAS3000 luminescent image analyzer (10 citations) Luminescent Image Analyzer LSA 4000 (7 citations) ImageQuant LAS 4000 Mini Luminescent Image Analyzer (5 citations) Image Quant LAS 4000 Luminescent Analyzer (3 citations) Luminescent Image Analyzer Amersham Imager 600 (3 citations) Image Analyzer (2 citations) LAS-4000EPUV mini Luminescent Image Analyzer (2 citations) Luminescent Image Analyzer–Image Quant Las 4000 mini (2 citations)

23 protocols using luminescent image analyzer

Polyacrylamide Gel Electrophoresis Protocol

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The 40% polyacrylamide gel was prepared according to the composition in Table 1.Table 1

Composition of the gel.

Table 1

Separating gel (Two pieces of gel)
stock solutions	volume
60% acrylamide/1% bis-acrylamide	10 mL
1 M Tris–HCl (pH 8.8)	5 mL
10% ammonium persulfate	50 μL
TEMED	10 μL

Stacking gel (Two pieces of gel)
stock solutions	volume
H₂O	5.8 mL
30% acrylamide	1.7 mL
1% bis-acrylamide	1.3 mL
1 M Tris–HCl (pH 6.8)	1.3 mL
10% ammonium persulfate	50 μL
TEMED	10 μL

The samples were separated by polyacrylamide gel electrophoresis (PAGE), as described previously [1 (link),3] (link).

The electrophoresis plate was 106 mm wide and 100 mm high (Mini gel slab electrophoresis device; Oriental Instruments, Sagamihara, Kanagawa, Japan).

The electrophoresis voltage was set at 150 V for the stacking gel and 150–250 V for the separating gel.

When the above apparatus was used, the electrophoresis time was 4 h.

The samples were quantified using the Luminescent Image Analyzer (ImageQuant LAS 4000, GE Healthcare), according to the manufacturer's instructions (Transillumination at 312 nm. Exposure conditions were fixed as follows: exposure type, precision; sensitivity, high resolution; exposure time, 5 s).

The samples were quantified using Analysis Toolbox according to the Luminescent Image Analyzer manual.

Kimura M., Umeyama T., Wakita S., Okawa K., Sakaguchi M., Matoska V., Bauer P.O, & Oyama F. (2020). Quantification of chitooligosaccharides by FACE method: Determination of combinatory effects of mouse chitinases. MethodsX, 7, 100881.

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CTS Modulates STAT3/JAK2 Signaling

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EC109 and CAES17 cells were seeded into six-well plates and treated with CTS (0, 1, 2.5, 5, 10 and 20 µmol/L). Then, the cells were harvested and lysed in RIPA buffer (50 mM Tris, pH 7.4, 150 mM NaCl, 1 mM PMSF, 1 mM EDTA, 1% Triton X-100, 0.1% SDS, 1 mM Na₃VO₄, 1 mM NaF and protease inhibitor cocktail; ZSGB-Bio, Beijing, People’s Republic of China). Protein concentration was determined by the Enhanced BCA Protein Assay Kit (Beyotime, Beijing, People’s Republic of China). For Western blot analysis,20 samples were separated on an 8%–10% SDS-PAGE gel, transferred to a polyvinylidene fluoride membrane (Immobilon; Millipore, USA) by semi-wet electrophoresis, then probed with primary antibodies: p-STAT3 (Tyr705), STAT3, p-JAK2 and JAK2. Signals were detected using a Luminescent Image Analyzer (GE Healthcare, Little Chalfont, UK). The experiments were independently performed at least twice, each in triplicate.

Ji Y., Liu Y., Xue N., Du T., Wang L., Huang R., Li L., Yan C, & Chen X. (2019). Cryptotanshinone inhibits esophageal squamous-cell carcinoma in vitro and in vivo through the suppression of STAT3 activation. OncoTargets and therapy, 12, 883-896.

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Quantification of BDNF Levels in Mouse Brain

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The method was modified from Umka et al. [17 (link)]. Briefly, mouse hippocampus and prefrontal cortex were homogenized in ice-cold lysis buffer and a cocktail of protease inhibitors. The homogenate was centrifuged at 13,000 rpm at 4 °C for 10 min and supernatant was collected. The protein concentrations were measured by Nanodrop 2000 spectrophotometer (Thermo Scientific, Waltham, MA, USA). Equal amounts of protein samples (80 µg) were separated by electrophoresis using 14% SDS-PAGE gels. The separated proteins were then transferred onto the nitrocellulose membrane. The membrane was blocked using blocking buffer (5% skim milk in BSA) for one hour at room temperature. Blots were probed with the following primary antibodies: polyclonal anti-BDNF (1:150 SantaCruz Biotechnology, Santa Cruz, CA, USA) and anti-GAPDH (1:20,000 Abcam, Cambridge, UK) overnight at 4 °C. The blot was incubated with secondary conjugated antibodies (anti-rabbit (1:2000) and anti-mouse (1:2000) IgG, HRP-linked antibody, Dako, Carpinteria, CA, USA) at room temperature for one hour. The blot was developed using the enhanced chemiluminescence method by a luminescent image analyzer (GE Healthcare Bio-Sciences, Uppsala, Sweden). The signal was visualized with ECL Western blotting substrate. Protein band densities were quantified with Image-J software and expressed as the density of BDNF/GAPDH.

Boonlert W., Benya-aphikul H., Umka Welbat J, & Rodsiri R. (2017). Ginseng Extract G115 Attenuates Ethanol-Induced Depression in Mice by Increasing Brain BDNF Levels. Nutrients, 9(9), 931.

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MUC1 Protein Expression Analysis

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Cells were lysed in RIPA buffer (50 mM Tris-HCl, 150 mM NaCl, 1% NP-40, and 0.25% Na-deoxycholate) with a protease and phosphatase inhibitor cocktail (Genedepot, Katy, TX, USA). The concentration of total protein was determined using the BCA Assay kit (Thermo Scientific, Rockford, IL, USA). Whole-cell lysates were separated by SDS-PAGE and transferred to PVDF membranes (Bio-Rad, Hercules, CA, USA). The primary antibodies used were anti-MUC1 (BD Bioscience, Franklin Lakes, NJ, USA) and anti-MUC1-C (AbCam, Cambridge, UK). Antibodies were routinely used at 1∶1000 dilution with 5% skim milk/PBS for primary antigen binding, then secondary anti-mouse IgG conjugated with horseradish peroxidase were incubated at 1:5000 dilution with 5% skim milk/PBS. This immunoblot was visualized with a chemiluminescent Western blot detection kit (Ab Frontier, Seoul, Korea) and Luminescent Image Analyzer (GE Healthcare Bio-sciences, Chicago, IL, USA) according to the manufacturer’s instructions.

Kim M.J., Choi J.R., Tae N., Wi T.M., Kim K.M., Kim D.H, & Lee E.S. (2020). Novel Antibodies Targeting MUC1-C Showed Anti-Metastasis and Growth-Inhibitory Effects on Human Breast Cancer Cells. International Journal of Molecular Sciences, 21(9), 3258.

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Immunoblotting Analysis of Endothelial Signaling

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HAECs were starved overnight in endothelial cell basal medium (EBM-2; PromoCell GmbH). After treatment with reagents for 1 h, cells were lysed with RIPA buffer (50 mM Tris-HCl, pH 8, 150 mM NaCl, 1% Nonidet P40, 0.5% sodium deoxycholate, and 0.1% SDS) containing protease and phosphatase inhibitors (100× Halt Protease and Phosphatase Inhibitor Cocktail, Thermo Fisher Scientific Inc., Waltham, MA, USA). Protein concentrations were measured using the Bio-Rad DC protein assay (Bio-Rad, Hercules, CA, USA). Cell lysates (25 μg/lane) were subjected to 10% SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane (Trans-Blot Turbo Mini PVDF Transfer Packs, Bio-Rad). After blocking with 5% skim milk in Tris-buffered saline, the membranes were incubated overnight at 4°C with primary antibodies against PDE3A, PDE3B, Epac-1, PKA RIIβ (1:200 dilution), phospho-PDK1, PDK-1, phospho-Akt, Akt, phospho-MAPK, MAPK, Rap-1A/B (1:250), phospho-PLA₂, or PLA₂ (1:100), followed by incubation with secondary antibodies (1:1000 dilution). The membranes were developed using Super Signal West Pico Chemiluminescent Substrate (Thermo Fisher Scientific Inc.) followed by exposure to a CCD camera (Luminescent image analyzer, GE Healthcare UK Ltd., Buckinghamshire, UK), and analyzed using Image quant LAS4000 software (GE Healthcare UK Ltd.).

Hashimoto A., Tanaka M., Takeda S., Ito H, & Nagano K. (2015). Cilostazol Induces PGI2 Production via Activation of the Downstream Epac-1/Rap1 Signaling Cascade to Increase Intracellular Calcium by PLCε and to Activate p44/42 MAPK in Human Aortic Endothelial Cells. PLoS ONE, 10(7), e0132835.

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Protein Isolation and Western Blot Analysis

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At 3, 6, 12 and 24 h following reperfusion, the brain samples were collected, and protein isolation from cortical tissues, based on total cell extracts or subcellular fractionation (cytosolic), was performed as previously described (19 (link)). A total of 20 mg tissue was homogenized and lyzed in radioimmunoprecipitation assay buffer on ice and the protein concentration of samples was determined using the Bradford protein assay kit (both from Beyotime Institute of Biotechnology, Shanghai, China). Western blotting was performed as previously described (20 (link)), and the following primary antibodies were incubated at 4°C overnight: anti-BID (1:200; cat. no. sc-6358; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), anti-cytochrome c (1:300; cat. no. ab13575) and anti-β-actin (1:2,000; cat. no. ab8226) (both from Abcam, Cambridge, UK). The polyvinylidene fluoride membranes were incubated with horseradish peroxidase-conjugated rabbit anti-goat immunoglobulin (Ig) G (1:1,000; cat. no. ZB-2306) and goat anti-mouse IgG secondary antibodies (1:1,000; cat. no. ZB-2305) (both from ZSGB-BIO, Beijing, China) for 1 h at room temperature. The expression of β-actin in the same membrane served as an internal reference. Blots were detected using a luminescent image analyzer and semi-quantified using Image Quant TL version 7.0 (both from GE Healthcare Biosciences, Pittsburgh, PA, USA).

Gao X., Liu Y., Xie Y., Wang Y, & Qi S. (2017). Remote ischemic postconditioning confers neuroprotective effects via inhibition of the BID-mediated mitochondrial apoptotic pathway. Molecular Medicine Reports, 16(1), 515-522.

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Protein Expression Analysis by SDS-PAGE

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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) immunoblotting was performed as follows: After trypsinization and cell pelleting at 500×g for 5 min, whole-cell lysates were harvested in cell lysis buffer (50 mM Tris-HCl [pH 7.5], 150 mM NaCl, 1 mM EDTA, 1% NP-40) supplemented with protease inhibitor (P8340, Sigma). Lysates were electrophoresed in 4–12% polyacrylamide gels and transferred onto PVDF membrane (IPVH00010, Millipore). The blots were blocked at room temperature for 0.5 h using 5% non-fat milk in PBS containing 0.1% (v/v) Tween 20. The blots were exposed to primary antibodies, β-Tubulin (CW0098, CWBIO), β-actin (AM1021b, Abcepta), Flag (F7425, Sigma), PRMT5 (sc-376937, Santa Cruz), WDR77 (2018S, CST), HA-HRP (M20021, Abmart) in 5% nonfat milk in 1×PBS containing 0.1% Tween 20 for 1.5 h. The blots were then washed in 1×PBS containing 0.1% Tween 20. After 1h exposure to HRP-conjugated secondary antibodies (AS003 or AS014, ABclonal) and subsequent washes were performed as described for the primary antibodies. Membranes were subsequently development with enhanced chemiluminescence (ECL) substrate (BE6706, Easybio) and visualized using the Luminescent Image Analyzer (GE).

Ju X., Yu Y., Ren W., Dong L., Meng X., Deng H., Nan Y, & Ding Q. (2023). The PRMT5/WDR77 complex restricts hepatitis E virus replication. PLOS Pathogens, 19(6), e1011434.

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Investigating Rapamycin and Doxorubicin Effects

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Total cell proteins were extracted from K562 cells treated with rapamycin and/or doxorubicin using lysis buffer (1% Triton X-100, 150 mM NaCl, 2 mM EDTA, 50 mM Tris-HCl) supplemented with phosphatase inhibitor cocktail. After protein concentration was measured by Gen5 1.0 software (BioTek Instruments, Inc.) on a spectrophotometer microplate reader (BioTek Instruments, Inc.), 20–40 µg protein was run on a 10–15% sodium dodecyl sulfate polyacrylamide gel electrophoresis gel and transferred to a polyvinylidinedifluoride membrane. Following blocking non-specific binding sites with 5% nonfat dry milk in tris-buffered saline with 0.05% Tween at 37°C for 60 min, the membranes were incubated with primary antibodies against mTOR, p-mTOR, p70S6K, p-p70S6K, Bcl-2, Bax, Bcl-xL, CDK4, CDK6, Cyclin B1 and CyclinD1at 4°C overnight. Next, the membranes were probed with horseradish peroxidase-conjugated secondary antibody (1:5,000) for 60 min at 37°C. Subsequently, the immunoreactive membranes were developed using Pierce™ ECL Western Blotting Substrate (cat. no. 32109; Thermo Fisher Scientific, Inc. cat. no.32109) on Luminescent Image Analyzer (GE Healthcare Bio-Sciences AB, Uppsala, Sweden). Band density was quantified and normalized to β-actinby Image J software (version 2; National Institutes of Health).

Li J., Liu W., Hao H., Wang Q, & Xue L. (2019). Rapamycin enhanced the antitumor effects of doxorubicin in myelogenous leukemia K562 cells by downregulating the mTOR/p70S6K pathway. Oncology Letters, 18(3), 2694-2703.

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SDS-PAGE Immunoblotting for Protein Analysis

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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) immunoblotting was performed as follows: After trypsinization and cell pelleting at 500 × g for 10 min, whole-cell lysates were harvested in RIPA lysis buffer (50 mM Tris-HCl [pH 8.0], 150mM NaCl, 1% NP-40, 0.5% sodium deoxycholate, and 0.1% SDS) supplemented with protease inhibitor cocktail (Sigma). Lysates were electrophoresed in 12% polyacrylamide gels and transferred onto nitrocellulose membrane. The blots were blocked at room temperature for 0.5 h using 5% nonfat milk in 1× phosphate-buffered saline (PBS) containing 0.1% (v/v) Tween 20. The blots were exposed to primary antibodies anti-β-Actin (abcepta, AM1021B), or anti-FLAG (F7425, Sigma) in 5% nonfat milk in 1× PBS containing 0.1% Tween 20 for 2 h. The blots were then washed in 1× PBS containing 0.1% Tween 20. After 1h exposure to HRP-conjugated secondary antibodies, subsequent washes were performed and membranes were visualized using the Luminescent image analyzer (GE).

Ren W., Lan J., Ju X., Gong M., Long Q., Zhu Z., Yu Y., Wu J., Zhong J., Zhang R., Fan S., Zhong G., Huang A., Wang X, & Ding Q. (2021). Mutation Y453F in the spike protein of SARS-CoV-2 enhances interaction with the mink ACE2 receptor for host adaption. PLoS Pathogens, 17(11), e1010053.

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Protein Expression Analysis by Western Blot

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Protein concentration was detected by Enhanced BCA Protein Assay Kit (Beyotime, Shanghai, China). The proteins in the lysate were then subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE, Solarbio) for separation and transferred to polyvinylidene difluoride (PVDF) membranes (Merck Millipore, Billerica, MA, USA). After transfection, the membrane was blocked in 5% skim milk powder (Becton, Dickinson, and Company, Franklin Lakes, NJ, USA) and slowly incubated for 2 hrs in the shaker at room temperature. The immunoreactive protein bands were visualized by EasySee Western Blot Kit (TransGen Biotech). Primary antibodies were anti-Cdc42, anti-Dvl-2, anti-Insulin, anti-Ngn3, anti-NeuroD1, anti-PDX1, anti-non-p-GSK3β, anti-p-GSK3β, anti-non-p-β-catenin, and anti-β-actin at a dilution of 1:1000. β-Actin was used as an internal control. All Western blot assays were determined by a luminescent image analyzer (GE Healthcare Bio-Sciences AB, Sweden).

Xiao X.H., Huang Q.Y., Qian X.L., Duan J., Jiao X.Q., Wu L.Y., Huang Q.Y., Li J., Lai X.N., Shi Y.B, & Xiong L.X. (2019). Cdc42 Promotes ADSC-Derived IPC Induction, Proliferation, And Insulin Secretion Via Wnt/β-Catenin Signaling. Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy, 12, 2325-2339.

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