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Synergy ht multimode microplate fluorescence reader

Manufactured by Agilent Technologies
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The Synergy HT multimode microplate fluorescence reader is a laboratory instrument designed to measure fluorescence signals in microplates. It is capable of detecting and quantifying fluorescent molecules in a variety of sample types.

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Lab products found in correlation

Fitc d, by Merck Group (1 mentions) Anti stromelysin1 antibody cat no sc 6839, by Santa Cruz Biotechnology (1 mentions) 5 fam qxl 520 fluorescence resonance energy transfer peptide, by AnaSpec (1 mentions)

Spelling variants of this product

Microplate reader (6925 citations) Synergy HT (3550 citations) Synergy microplate reader (229 citations) Multimode microplate reader (191 citations) Fluorescence microplate reader (178 citations) Synergy HT reader (90 citations) Multimode reader (74 citations) Synergy HT fluorescence microplate reader (9 citations) HT Multimode Reader (2 citations)

5 protocols using synergy ht multimode microplate fluorescence reader

1

Assessing Intestinal Permeability with FITC-D

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Intestinal leakage of FITC-D (MW 3–5 KDa; Sigma-Aldrich Co., St. Louis, MO, USA) and the measurement of its serum concentration were done in experiment 2 as a marker of paracellular transport and mucosal barrier dysfunction (19 (link)–22 (link)). At 24 h, post-SH challenge (day 8 of age), poults in all groups were given an oral gavage dose of FITC-D (4.16 mg/kg). Following 2.5 h, they were killed by CO2 asphyxiation. Blood samples were collected from the femoral vein kept at room temperature for 3 h and centrifuged (500 × g for 15 min) to separate the serum from the red blood cells. FITC-D levels of diluted serum samples (1:5 PBS) were measured at excitation wavelength of 485 nm and an emission wavelength of 528 nm with a Synergy HT, Multi-mode microplate fluorescence reader (BioTek Instruments, Inc., Vermont, USA). Fluorescence measured was then compared to a standard curve with known FITC-D concentrations. Gut leakage for each bird was reported as microgram of FITC-D/mL of serum (20 (link)).
Morales-Barrera E., Calhoun N., Lobato-Tapia J.L., Lucca V., Prado-Rebolledo O., Hernandez-Velasco X., Merino-Guzman R., Petrone-García V.M., Latorre J.D., Mahaffey B.D., Teague K.D., Graham L.E., Wolfenden A.D., Baxter M.F., Hargis B.M, & Tellez G. (2016). Risks Involved in the Use of Enrofloxacin for Salmonella Enteritidis or Salmonella Heidelberg in Commercial Poultry. Frontiers in Veterinary Science, 3, 72.
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2

Fluorometric Assay for Stromelysin-1

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The enzymatic activity of stromelysin1 was determined using a fluorescence resonance energy transfer peptide and immunocapture assay as previously described (Artham et al., 2019 (link)). Briefly, 50 μg total protein of patient serum/plasma samples were incubated at 4°C for 2 hours with rabbit polyclonal anti-stromelysin1 antibody (Cat no. sc-6839; Santa Cruz Biotechnology, Dallas, TX). A/G agarose beads were then added and allowed to incubate overnight at 4°C. The beads were then washed and samples were transferred to a black 96well plate and 100 μL of 2 mmol/L 5-FAM/QXL 520 fluorescence resonance energy transfer peptide (cat no. 60580–01; AnaSpec, San Jose, CA) in assay buffer was added per well. Plates were incubated for 15 hours at 37°C, and the relative fluorescence units were read and monitored at excitation/emission wavelengths of 485 of 528 nm in a Synergy HT multimode microplate fluorescence reader (BioTek, Winooski, VT) running Gen5 data analysis software.
Alharthi A., Verma A., Sabbineni H., Adil M.S, & Somanath P.R. (2020). Distinct effects of pharmacological inhibition of stromelysin1 on endothelial-to-mesenchymal transition and myofibroblast differentiation. Journal of cellular physiology, 236(7), 5147-5161.
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3

MMP-3 Activity Quantification via FRET Assay

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The enzymatic activity of MMP-3 was determined using a fluorescence resonance energy transfer (FRET) peptide and immunocapture assay as previously described elsewhere with minor modifications [16 (link)]. Briefly, 50 µg total protein of homogenized brain tissue were incubated at 4°C for 2 h with rabbit polyclonal anti-MMP-3 antibody (Cat.No. sc-6839-R; Santa Cruz Biotechnology, Dallas, TX, USA). A/G agarose beads were then added and allowed to incubate overnight at 4°C. The beads were then washed and samples are transferred to black 96 well plate and 100 ul of 2mM 5-FAM/QXL™520 FRET peptide (Cat. No. 60580-01; AnaSpec, San Jose, CA, USA) in assay buffer were added per well. Plates were incubated for 8 h at 37°C and the relative fluorescence units (RFUs) were read and monitored at excitation/emission wavelengths of 485/528 nm in a Synergy HT Multi-mode microplate fluorescence reader (BioTek, Winooski, VT, USA) running Gen5™ data analysis software.
Hafez S., Abdelsaid M., Fagan S.C, & Ergul A. (2017). PEROXYNITRITE-INDUCED TYROSINE NITRATION CONTRIBUTES TO MATRIX METALLOPROTEASE-3 ACTIVATION: RELEVANCE TO HYPERGLYCEMIC ISCHEMIC BRAIN INJURY AND TISSUE PLASMINOGEN ACTIVATOR. Neurochemical research, 43(2), 259-266.
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4

Stromelysin-1 Enzymatic Activity Assay

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The enzymatic activity of stromelysin1 was determined using a fluorescence resonance energy transfer (FRET) peptide and immunocapture assay as previously described elsewhere [31 (link)] with minor modifications. Briefly, 50 μg total protein of endothelial cells or lung lysates were incubated at 4°C for 2 hours with rabbit polyclonal anti-MMP3 antibody (cat no. sc-6839-R; Santa Cruz Biotechnology, Dallas, TX). A/G agarose beads were then added and allowed to incubate overnight at 4°C. The beads were then washed, and samples were transferred to black 96well plate and 100 μL of 2 μmol/L 5-FAM/QXL 520 FRET peptide (cat no. 60580-01; AnaSpec, San Jose, CA) in assay buffer was added per well. Plates were incubated for 15 hours at 37°C; then relative fluorescence units were read and monitored at excitation/emission wavelengths of 485 of 528 nm in a Synergy HT multimode microplate fluorescence reader (BioTek, Winooski, VT) running Gen5 data analysis software.
Artham S., Gao F., Verma A., Alwhaibi A., Sabbineni H., Hafez S., Ergul A, & Somanath P.R. (2019). Endothelial stromelysin1 regulation by the forkhead box-O transcription factors is crucial in the exudative phase of acute lung injury. Pharmacological research, 141, 249-263.
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5

MMP-3 Enzymatic Activity Assay

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The enzymatic activity of MMP-3 was determined using a fluorescence resonance energy transfer (FRET) peptide and immunocapture assay as previously described elsewhere with minor modifications.17 (link) Briefly, 50 µg total protein of macrovascular or brain homogenates were incubated at 4°C for 2 h with rabbit polyclonal anti-MMP-3 antibody (Cat.No. sc-6839-R; Santa Cruz Biotechnology, Dallas, TX, USA). A/G agarose beads were then added and allowed to incubate overnight at 4°C. The beads were then washed and samples were transferred to black 96 well plate and 100 ul of 2mM 5-FAM/QXL™520 FRET peptide (Cat. No. 60580-01; AnaSpec, San Jose, CA, USA) in assay buffer were added per well. Plates were incubated for 8 h at 37°C, then relative fluorescence units (RFUs) were read and monitored at excitation/emission wavelengths of 485/528 nm in a Synergy HT Multi-mode microplate fluorescence reader (BioTek, Winooski, VT, USA) running Gen5™ data analysis software.
Hafez S., Abdelsaid M., El-Shafey S., Johnson M.H., Fagan S.C, & Ergul A. (2016). Matrix Metalloprotease 3 Exacerbates Hemorrhagic Transformation and Worsens Functional Outcomes in Hyperglycemic Stroke. Stroke; a journal of cerebral circulation, 47(3), 843-851.
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