Glomax explorer

Manufactured by Promega

Sourced in United States, Italy, Germany, Sweden

The GloMax Explorer is a multi-mode microplate reader designed for a variety of laboratory applications. It offers luminescence, fluorescence, and absorbance detection capabilities in a compact and user-friendly format.

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Lab products found in correlation

Lipofectamine 2000, by Thermo Fisher Scientific (5 mentions) Celltiter glo reagent, by Promega (5 mentions) Celltiter blue, by Promega (5 mentions) Bright glo, by Promega (4 mentions) Peroxidase anti hamster igg h l, by LGC (4 mentions) Kpl abts peroxidase substrate solution mix, by LGC (4 mentions) Celltiter glo luminescent cell viability assay, by Promega (4 mentions) Luciferase assay system, by Promega (3 mentions) Dual luciferase reporter assay system, by Promega (3 mentions) Methyl thiazolyl tetrazolium (mtt), by Merck Group (3 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (3 mentions) Enzchek caspase 3 assay kit 1, by Thermo Fisher Scientific (2 mentions) 96 well assay plate, by Corning (2 mentions) Opti mem, by Thermo Fisher Scientific (2 mentions) Britelite reagent, by PerkinElmer (2 mentions) X tremegene 9 dna transfection reagent, by Merck Group (2 mentions) Ripa lysis buffer, by Rockland Immunochemicals (2 mentions) Dual glo luciferase assay system, by Promega (2 mentions) Nunc maxisorp, by Thermo Fisher Scientific (2 mentions) Sars cov 2 2019 ncov spike receptor binding domain polyhistidine tagged recombinant protein, by Sino Biological (2 mentions)

Spelling variants of this product

GloMax (528 citations) GloMax® Explorer Multimode Microplate Reader (75 citations) GloMax Explorer System (45 citations) GloMax Explorer microplate reader (34 citations) GloMax Explorer plate reader (24 citations) GloMax Explorer luminometer (16 citations) GloMax Discover and Explorer Detection System equipment (5 citations) GloMax® Explorer System model GM3500 (2 citations) GloMax® Explorer System GM3500 (2 citations) GloMax Explorer Luminometer/Fluorometer Instrument (2 citations)

148 protocols using glomax explorer

Quantification of Plasma Biomarkers

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D-dimer levels in sodium citrate plasma samples were measured via an enzyme-linked immunosorbent assay (ELISA) (Ray Biotech, Peachtree Corners, GA) per the manufacturer’s protocol. Samples were diluted 600,000-fold and plated in duplicate. IL-4 levels in plasma samples were measured using a Monkey IL-4 ELISA kit (abcam, Boston, MA) per the manufacturer’s protocol. Plasma samples were diluted 1:2 and assayed in duplicate along with two replicates of undiluted sample. In modification to the manufacturer’s protocol, the standard/sample incubation time was increased to 2.5 hours. Plates were analyzed using the GloMax Explorer plate reader (Promega, Madison, WI) and GraphPad Prism (GraphPad Software version 9, LaJolla, California). Heatmap was generated using Microsoft Excel. Data was normalized by dividing raw data values from Day 4, (D-dimer only) 6, 14 and 21 by the baseline value for each animal.
Kynurenine and tryptophan levels in plasma were measured using commercially available enzyme-linked immunosorbent assays (Rocky Mountain Diagnostics, Colorado Springs, CO) per the manufacturer’s protocol. The GloMax Explorer plate reader (Promega, Madison, WI) along with GraphPad Prism v9 were used to analyze the plates.

Melton A., Doyle-Meyers L.A., Blair R.V., Midkiff C., Melton H.J., Russell-Lodrigue K., Aye P.P., Schiro F., Fahlberg M., Szeltner D., Spencer S., Beddingfield B.J., Goff K., Golden N., Penney T., Picou B., Hensley K., Chandler K.E., Plante J.A., Plante K.S., Weaver S.C., Roy C.J., Hoxie J.A., Gao H., Montefiori D.C., Mankowski J.L., Bohm R.P., Rappaport J, & Maness N.J. (2021). The pigtail macaque (Macaca nemestrina) model of COVID-19 reproduces diverse clinical outcomes and reveals new and complex signatures of disease. PLoS Pathogens, 17(12), e1010162.

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Viral infection and inhibition assay

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Cells were plated at a density of 2.5 × 10⁴ cells per well in a 96-well plate, the day before infection. Cells were infected with CHIKV-Nluc, rVSVΔG-LASV-NlucP, or Coxsackie B5 at an MOI of 0.05. Two hours post-infection, cells were treated with 10 mM ammonium chloride (NH₄Cl) to inhibit subsequent rounds of replication. Eight hours after infection, cells infected with CHIKV or rVSVΔG-LASV were lysed with NanoGlo substrate, and lysates were quantified in a GloMax Explorer (Promega) according to the manufacturer’s instructions. Cells infected with Coxsackie B5 were harvested 24 h post-infection and cell viability was assessed using Cell Titer Glo and quantified in a GloMax Explorer (Promega) according to the manufacturer’s instructions.

Reyes Ballista J.M., Miazgowicz K.L., Acciani M.D., Jimenez A.R., Belloli R.S., Havranek K.E, & Brindley M.A. (2023). Chikungunya virus entry and infectivity is primarily facilitated through cell line dependent attachment factors in mammalian and mosquito cells. Frontiers in Cell and Developmental Biology, 11, 1085913.

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HEK293 Cell Luciferase Reporter Assay

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HEK293 cells were seeded in 24-well plates at 70–80% confluency. In total, 200 ng/well of firefly luciferase-encoding reporter plasmids, 500 ng/well of dLwCas13a-NF and gRNA (gene-specific or nontargeting) were transfected using Lipofectamine 2000. Ten ng/well of Renilla luciferase was used as transfection control. Firefly and Renilla luciferase activities were measured using Dual-Luciferase Reporter Assay System (Promega) using GloMax Explorer (Promega) 24 h post transfection in case of samples involving VEGFA and MTCH2, and 48 h post transfection in case of AGO1.
For in vitro induction of SCR, the AGO1-Luciferase reporter construct was linearized using NotI restriction enzyme. Following this, the purified linearized plasmid was subjected to in vitro transcription using T7 RNA polymerase for 3 h at 37 °C. The RNA was purified, and the quality and concentration were determined using BioPhotometer (Eppendorf). The luciferase reporter RNA (500 ng) was in vitro translated using Rabbit Reticulocyte Lysate (Promega) in the presence of 4 µg cell extract (prepared as described under “Luminescence-based ribosomal pausing assay”) and RNase inhibitor for 90 min. Luminescence was measured using the Luciferase Assay System (Promega) in the GloMax Explorer (Promega).

Manjunath L.E., Singh A., Devi Kumar S., Vasu K., Kar D., Sellamuthu K, & Eswarappa S.M. (2024). Transcript-specific induction of stop codon readthrough using a CRISPR-dCas13 system. EMBO Reports, 25(4), 2118-2143.

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Biofilm Formation and Quantification in C. difficile

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To generate biofilms, we diluted overnight cultures of C. difficile 1:100 into fresh BHISG, deposited 1 ml per well in 24-well polystyrene tissue culture–treated plates (Falcon, USA), and incubated the plates at 37°C in anaerobic environment for 24 hours. Biofilm biomass was measured using a crystal violet as described elsewhere (79 (link)). Briefly, spent media were removed by inversion, and wells were washed twice with phosphate-buffered saline (PBS), dried, stained with crystal violet for 2 min, and washed twice again with PBS. Crystal violet was solubilized with a 75% ethanol solution, and the OD₆₀₀ was measured with a plate reader (Promega GloMax Explorer, Promega, France).

Oberkampf M., Hamiot A., Altamirano-Silva P., Bellés-Sancho P., Tremblay Y.D., DiBenedetto N., Seifert R., Soutourina O., Bry L., Dupuy B, & Peltier J. (2022). c-di-AMP signaling is required for bile salt resistance, osmotolerance, and long-term host colonization by Clostridioides difficile. Science signaling, 15(750), eabn8171.

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SARS-CoV-2 Pseudovirus Neutralization Assay

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SARS-CoV-2 pseudovirus neutralization assay was performed as previously described [14 (link)]. Briefly, hACE2-expressing cells, hACE2-293T, were seeded onto 96-well plates 18 h before infection. mAbs were serially diluted and co-incubated with the same volume of pseudotype particles at 37 °C for 1 h. MEM was added as the negative control. The mixtures were added to the monolayers of hACE2-293T. Next, the plates were incubated at 37 °C in 5% CO₂. Forty-eight hours later, the cells were lysed and analyzed using Promega GloMax Explorer (Promega, Madison, USA). Inhibition rates of mAbs at different dilutions were calculated and compared to those of the negative control. Anti-SARS-CoV-2-RBD mouse serum samples were used as the positive control, and mouse anti-PBS serum samples were used as the negative control. For each experiment, the positive convalescent serum from a patient with COVID-19 was used as a standard experimental control.

Yang Y., Zhou L., Mo C., Hu L., Zhou Z., Fan Y., Liu W., Li X., Zhou R, & Tian X. (2023). Identification of conserved linear epitopes in the SARS-CoV-2 receptor-binding region using monoclonal antibodies. Heliyon, 9(6), e16847.

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Measuring Redox State in Botrytis cinerea

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Redox state of roGFP transformed B. cinerea was measured in liquid culture using a fluorimeter. B. cinerea strains expressing GRX-roGFP and mito-roGFP were grown for 2 weeks on PDA medium at 18°C in the light to induce mass sporulation. A total of 10 mL of PDB medium containing 100 μM CK was inoculated with conidia and incubated for 24 h at 18°C, with 150 rpm shaking. Samples of 1 mL were taken and washed twice in double-distilled water, and 200 μL of the washed germlings were transferred to a 96-well plate (Microplate pureGrade 96-well PS, transparent bottom) for fluorescence measurements using a fluorimeter (Promega GloMax explorer multimode microplate reader, GM3500, USA). Fluorescence was measured at the bottom with 3 × 3 reads/well and an excitation wavelength of 405 ± 5 nm for the oxidized state and 488 ± 5 nm for the reduced state of roGFP2. The emission was detected at 510 ± 5 nm (52 (link)). The gain was set to 100. Relative fluorescence units (RFU) were recorded to calculate the Em₄₀₅/Em₄₈₈ ratio.

Anand G., Gupta R, & Bar M. (2022). Cytokinin Regulates Energy Utilization in Botrytis cinerea. Microbiology Spectrum, 10(4), e00280-22.

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Cell-Cell Spread of VSV-G Infection

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Cell-to-cell spread of VSV-G in Vero cells was determined using Endurazine substrate (Promega, Madison, WI, USA) following manufacturer’s specifications. Vero cells were plated in a black-walled, clear-bottom 96-well plate at a density of 3 × 10⁵ cells/mL with DMEM 5% FBS. Once attached to the plate, cells were starved from lipids by replacing the media with serum-free DMEM. After 20 h, media were substituted with DMEM 5% Lipoprotein Depleted FBS (Cat #880100-1, Kalen Biomedical LLC, Germantown, MD, USA). Cells were infected with 50 µL of VSV-G-nLuciPest at an MOI of 0.04 using serum-free DMEM. One hour after infection, media were removed and replaced with 200µL of phenol red-free DMEM supplemented with 5% Lipoprotein Depleted FBS, 25 mM HEPES, 1:200 Endurazine and treated with LysoPC 16:0 (SKU #855675P, Avanti Polar Lipids, Birmingham, AL, USA) or 18:1 (SKU #845875P, Avanti Polar Lipids, Birmingham, AL, USA) 0.5 µM or 5 µM. The plate was moved into a pre-warmed (37 °C) GloMax Explorer (Promega, Madison, WI, USA), and luminescence was measured every 10 min for a period of 24 h.

Havranek K.E., Reyes Ballista J.M., Hines K.M, & Brindley M.A. (2021). Untargeted Lipidomics of Vesicular Stomatitis Virus-Infected Cells and Viral Particles. Viruses, 14(1), 3.

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Cloning and Evaluating IL-1β 3'UTR

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The UTR sequences of human IL-1β, including the XhoI (forward) and XbaI (reverse) endonuclease sites at both ends, were purchased from Integrated DNA Technologies (IDT, Republic of Singapore). The 3′ UTR fragment was then cloned into the pMIR GLO vector (Promega Corporation, Fitchburg, WI, USA). HeLa cells were plated at a density of 1 × 10⁵ cells/well in a 12-well plate and then transfected with either pMIR GLO control vector or pMIR GLO vector with IL-1β 3′ UTR using Lipofectamine 2000 (Thermo Fisher Scientific). Two days after the transfection, the luciferase activity of the cells was measured using a luminometer and Dual Luciferase Assay Kit (Promega Corporation) according to the manufacturer’s instructions. Cell number and transfection efficiency were normalized with Renilla luciferase assay. Luciferase intensity was determined using the Glomax^® Explorer multimode microplate reader (Promega, WI, USA).

Lee C.Y., Lee S., Jeong S., Lee J., Seo H.H., Shin S., Park J.H., Song B.W., Kim I.K., Choi J.W., Kim S.W., Han G., Lim S, & Hwang K.C. (2021). Suppressing Pyroptosis Augments Post-Transplant Survival of Stem Cells and Cardiac Function Following Ischemic Injury. International Journal of Molecular Sciences, 22(15), 7946.

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Neutralizing Clostridium Difficile Toxins

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When almost reaching confluence, cells were treated with 7.5 ng/mL TcdA, 100 ng/mL TcdB, or a combination of both. The applied toxin concentrations were predetermined as the respective IC50. The neutralisation assay was carried out by pre-incubating TcdA and TcdB with 50 µg/mL monoclonal antibody bezlotoxumab (Merck, Darmstadt, Germany), monoclonal recombinant sIgA, or sIgA isolated from goat whey for 2 h at 37 °C prior to cell treatment. Used concentrations equalled to a 14,000-fold and 930-fold molar excess of bezlotoxumab and a 5300-fold and 350-fold molar excess of sIgA to TcdA and TcdB, respectively. After 24 h, cells were fixed and subjected to sulforhodamine B (SRB) cytotoxicity assays [54 (link)]. In brief, cells were fixed with 10% trichloroacetic acid (TCA) for one hour at 4 °C and then rinsed with tap water four times. After air-drying, cells were stained with 0.057% SRB in 1% acetic acid for 30 min. Subsequently, cells were rinsed with 1% acetic acid four times to remove excess SRB before air-drying again. Cell-bound dye was then solubilised in 10 mM TRIS and extinction was measured at 488 nm using a fluoro spectrometer (Glomax^® Explorer, Promega, Vienna, Austria).

Csukovich G., Kramer N., Pratscher B., Gotic I., Freund P., Hahn R., Himmler G., Brandt S, & Burgener I.A. (2023). Neutralising Effects of Different Antibodies on Clostridioides difficile Toxins TcdA and TcdB in a Translational Approach. International Journal of Molecular Sciences, 24(4), 3867.

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Cisplatin and Biochanin A Cytotoxicity Assay

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Briefly, 3000 cells/well were plated into 96-well, grown for overnight, treated with cisplatin (8 µM) and/or Biochanin A (100 µM) for the indicated time points, followed by incubation with cell counting kit-8 (CCK-8) substrate (Dojindo) for 1 h at 37 °C. The absorbance was examined at 450 nm by the GloMax Explorer (Promega).

Li J., Kou Y., Zhang X., Xiao X., Ou Y., Cao L., Guo M., Qi C., Wang Z., Liu Y., Shuai Q., Wang H, & Yang S. (2022). Biochanin A inhibits lung adenocarcinoma progression by targeting ZEB1. Discover. Oncology, 13, 138.

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