coelenterazine  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc coelenterazine
    Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using <t>coelenterazine</t> as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of
    Coelenterazine, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/coelenterazine/product/Gold Biotechnology Inc
    Average 94 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    coelenterazine - by Bioz Stars, 2022-09
    94/100 stars

    Images

    1) Product Images from "A Luminescence-Based System for Identification of Genetically Encodable Inhibitors of Protein Aggregation"

    Article Title: A Luminescence-Based System for Identification of Genetically Encodable Inhibitors of Protein Aggregation

    Journal: ACS Omega

    doi: 10.1021/acsomega.0c00779

    Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using coelenterazine as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of
    Figure Legend Snippet: Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using coelenterazine as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of

    Techniques Used: Solubility, Plasmid Preparation, Expressing, Standard Deviation

    2) Product Images from "A PROTEIN SWITCH SENSING SYSTEM FOR THE QUANTIFICATION OF SULFATE"

    Article Title: A PROTEIN SWITCH SENSING SYSTEM FOR THE QUANTIFICATION OF SULFATE

    Journal: Analytical biochemistry

    doi: 10.1016/j.ab.2011.10.023

    (a) The 3-D crystal structure of aequorin. Coelenterazine is non-covalently bound in the hydrophobic pocket. Protein data bank structure 1EJ3. (b) The 3-D crystal structure of the sulfate-binding protein with sulfate bound in the hinge region. Protein data bank structure 1SBP. Images visualized in Accelrys Discovery Studio Visualizer 2.5.
    Figure Legend Snippet: (a) The 3-D crystal structure of aequorin. Coelenterazine is non-covalently bound in the hydrophobic pocket. Protein data bank structure 1EJ3. (b) The 3-D crystal structure of the sulfate-binding protein with sulfate bound in the hinge region. Protein data bank structure 1SBP. Images visualized in Accelrys Discovery Studio Visualizer 2.5.

    Techniques Used: Binding Assay

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    Gold Biotechnology Inc coelenterazine
    Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using <t>coelenterazine</t> as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of
    Coelenterazine, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/coelenterazine/product/Gold Biotechnology Inc
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    coelenterazine - by Bioz Stars, 2022-09
    94/100 stars
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    Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using coelenterazine as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of

    Journal: ACS Omega

    Article Title: A Luminescence-Based System for Identification of Genetically Encodable Inhibitors of Protein Aggregation

    doi: 10.1021/acsomega.0c00779

    Figure Lengend Snippet: Monitoring the influence of small molecules on protein solubility using the single-plasmid split-Nluc assay. (a) The structure of silibinin, a known inhibitor of amylin aggregation, is shown. (b) Luminescence from bacterial cells expressing amylin-N65/66C in the presence or absence of silibinin using coelenterazine as the substrate. (c) The structure of cystamine, a known inhibitor of Htt aggregation, is shown. (d) Luminescence from bacterial cells expressing Htt97QN65/66C in the presence or absence of cystamine using coelenterazine as the substrate. Error bars represent the standard deviation of three biological replicates assayed in triplicate. ** indicates a p -value of

    Article Snippet: The cells were then mixed with either 200 μL of Nano-Glo Live Cell Assay reagent (Promega, N2011) prepared according to the manufacture’s protocol or 200 μL of 1× Nluc assay buffer containing either furimazine (Promega, N1110, 2% v/v) or coelenterazine (GoldBio, CZ2.5, 25 μM final concentration) as indicated.

    Techniques: Solubility, Plasmid Preparation, Expressing, Standard Deviation

    (a) The 3-D crystal structure of aequorin. Coelenterazine is non-covalently bound in the hydrophobic pocket. Protein data bank structure 1EJ3. (b) The 3-D crystal structure of the sulfate-binding protein with sulfate bound in the hinge region. Protein data bank structure 1SBP. Images visualized in Accelrys Discovery Studio Visualizer 2.5.

    Journal: Analytical biochemistry

    Article Title: A PROTEIN SWITCH SENSING SYSTEM FOR THE QUANTIFICATION OF SULFATE

    doi: 10.1016/j.ab.2011.10.023

    Figure Lengend Snippet: (a) The 3-D crystal structure of aequorin. Coelenterazine is non-covalently bound in the hydrophobic pocket. Protein data bank structure 1EJ3. (b) The 3-D crystal structure of the sulfate-binding protein with sulfate bound in the hinge region. Protein data bank structure 1SBP. Images visualized in Accelrys Discovery Studio Visualizer 2.5.

    Article Snippet: Coelenterazine was purchased from Gold Biotechnology, Inc. (St. Louis, MO).

    Techniques: Binding Assay

    BLI of gluc -expressing M. smegmatis . Mice were endotracheally inoculated with 3.32×10 6 CFU of M. smegmatis pMV306hsp+Gluc [two representative mice (M1 and M2) out of three are shown,) or with 1.58×10 7 CFU of M. smegmatis pMV306hsp as a control (one out of two mice is shown). 10 µg of coelenterazine intranasal was administered 24 h post-inoculation and mice were imaged at time points 0, 5, 10, 15, 30, 60, 120 and 180 min. ( a ) Images were obtained using an IVIS Spectrum and are displayed as pseudocolour images of peak bioluminescence (given as photons s −1 cm −2 sr −1 ), with variations in colour representing light intensity at a given location. Integration time was 5 min. ( b ) Bioluminescence (given as photons s −1 ) was quantified using the Living image software. (C) 10 µg of coelenterazine was given intraperitoneally to the same mice 5 h post-intranasal coelenterazine. Mice were imaged 0, 5, 10, 15, 20, 25 and 30 min post-intraperitoneal coelenterazine with integration times of 3 min.

    Journal: PLoS ONE

    Article Title: Optimisation of Bioluminescent Reporters for Use with Mycobacteria

    doi: 10.1371/journal.pone.0010777

    Figure Lengend Snippet: BLI of gluc -expressing M. smegmatis . Mice were endotracheally inoculated with 3.32×10 6 CFU of M. smegmatis pMV306hsp+Gluc [two representative mice (M1 and M2) out of three are shown,) or with 1.58×10 7 CFU of M. smegmatis pMV306hsp as a control (one out of two mice is shown). 10 µg of coelenterazine intranasal was administered 24 h post-inoculation and mice were imaged at time points 0, 5, 10, 15, 30, 60, 120 and 180 min. ( a ) Images were obtained using an IVIS Spectrum and are displayed as pseudocolour images of peak bioluminescence (given as photons s −1 cm −2 sr −1 ), with variations in colour representing light intensity at a given location. Integration time was 5 min. ( b ) Bioluminescence (given as photons s −1 ) was quantified using the Living image software. (C) 10 µg of coelenterazine was given intraperitoneally to the same mice 5 h post-intranasal coelenterazine. Mice were imaged 0, 5, 10, 15, 20, 25 and 30 min post-intraperitoneal coelenterazine with integration times of 3 min.

    Article Snippet: Luciferases substrates Coelenterazine (Gold BioTechnology®, Inc., St. Louis, Mo., USA), the substrate for Gluc, was reconstituted in acid methanol to a concentration of 10 mM (4.238 mg ml−1 ).

    Techniques: Expressing, Mouse Assay, Software

    Bioluminescence correlates with substrate concentration at low concentrations. Luminescence (given as relative light units [RLUs]) of M. smegmatis pMVhsp+FFluc ( a ) and M. smegmatis pMVhsp+Gluc ( b ) was measured with integration times of 5 s and 0.1 s respectively. The substrate concentrations assayed ranged from 20 to 4710 µM luciferin for FFluc, and from 0.05 to 400 µM coelenterazine for Gluc. Means and standard deviations (smaller than symbols) of six replicates are shown.

    Journal: PLoS ONE

    Article Title: Optimisation of Bioluminescent Reporters for Use with Mycobacteria

    doi: 10.1371/journal.pone.0010777

    Figure Lengend Snippet: Bioluminescence correlates with substrate concentration at low concentrations. Luminescence (given as relative light units [RLUs]) of M. smegmatis pMVhsp+FFluc ( a ) and M. smegmatis pMVhsp+Gluc ( b ) was measured with integration times of 5 s and 0.1 s respectively. The substrate concentrations assayed ranged from 20 to 4710 µM luciferin for FFluc, and from 0.05 to 400 µM coelenterazine for Gluc. Means and standard deviations (smaller than symbols) of six replicates are shown.

    Article Snippet: Luciferases substrates Coelenterazine (Gold BioTechnology®, Inc., St. Louis, Mo., USA), the substrate for Gluc, was reconstituted in acid methanol to a concentration of 10 mM (4.238 mg ml−1 ).

    Techniques: Concentration Assay

    Bioluminescence correlates with cell density during exponential growth in vitro . Cultures of M. smegmatis pMVhsp+FFluc ( a ), pMVhsp+Gluc ( b ) and pMVhsp+Lux ( c ) were inoculated to an optical density (OD) at 600 nm of 0.1 and the OD and the luminescence [given as relative light units (RLUs)] measured over 28 h. The luminescence was measured with integration times of 5, 0.1, and 10 s respectively, and substrate concentrations of 470 µM luciferin for FFluc and 40 µM coelenterazine for Gluc. The values represented correspond to the means of two independent cultures measured in triplicate. The error bars indicate standard deviations. A near linear relationship was found between bioluminescence [given as RLUs] and colony counts (given as colony forming units [CFU]) for mid-log cultures of M. smegmatis pMVhsp+FFluc ( d ), pMVhsp+Gluc ( e ) and pMVhsp+Lux ( f ) using a plate luminometer.

    Journal: PLoS ONE

    Article Title: Optimisation of Bioluminescent Reporters for Use with Mycobacteria

    doi: 10.1371/journal.pone.0010777

    Figure Lengend Snippet: Bioluminescence correlates with cell density during exponential growth in vitro . Cultures of M. smegmatis pMVhsp+FFluc ( a ), pMVhsp+Gluc ( b ) and pMVhsp+Lux ( c ) were inoculated to an optical density (OD) at 600 nm of 0.1 and the OD and the luminescence [given as relative light units (RLUs)] measured over 28 h. The luminescence was measured with integration times of 5, 0.1, and 10 s respectively, and substrate concentrations of 470 µM luciferin for FFluc and 40 µM coelenterazine for Gluc. The values represented correspond to the means of two independent cultures measured in triplicate. The error bars indicate standard deviations. A near linear relationship was found between bioluminescence [given as RLUs] and colony counts (given as colony forming units [CFU]) for mid-log cultures of M. smegmatis pMVhsp+FFluc ( d ), pMVhsp+Gluc ( e ) and pMVhsp+Lux ( f ) using a plate luminometer.

    Article Snippet: Luciferases substrates Coelenterazine (Gold BioTechnology®, Inc., St. Louis, Mo., USA), the substrate for Gluc, was reconstituted in acid methanol to a concentration of 10 mM (4.238 mg ml−1 ).

    Techniques: In Vitro

    Light production from FFluc and Lux is stable, whereas the signal from Gluc rapidly dissipates. Luminescence (given as relative light units [RLUs]) was measured every 10 s for gluc -expressing M. smegmatis and every 30 s for ffluc - or lux -expressing M. smegmatis , over a 30 min period. The integration times used were 0.1 s, 5 s and 10 s for Gluc, FFluc and Lux respectively. At time point 0 min, 470 µM luciferin or 40 µM coelenterazine were added to FFluc- and Gluc-producing M. smegmatis respectively. Two independent cultures were used for FFluc and Lux, and three for Gluc. Each culture was measured in duplicate and the means and standard deviations (smaller than symbols) are plotted.

    Journal: PLoS ONE

    Article Title: Optimisation of Bioluminescent Reporters for Use with Mycobacteria

    doi: 10.1371/journal.pone.0010777

    Figure Lengend Snippet: Light production from FFluc and Lux is stable, whereas the signal from Gluc rapidly dissipates. Luminescence (given as relative light units [RLUs]) was measured every 10 s for gluc -expressing M. smegmatis and every 30 s for ffluc - or lux -expressing M. smegmatis , over a 30 min period. The integration times used were 0.1 s, 5 s and 10 s for Gluc, FFluc and Lux respectively. At time point 0 min, 470 µM luciferin or 40 µM coelenterazine were added to FFluc- and Gluc-producing M. smegmatis respectively. Two independent cultures were used for FFluc and Lux, and three for Gluc. Each culture was measured in duplicate and the means and standard deviations (smaller than symbols) are plotted.

    Article Snippet: Luciferases substrates Coelenterazine (Gold BioTechnology®, Inc., St. Louis, Mo., USA), the substrate for Gluc, was reconstituted in acid methanol to a concentration of 10 mM (4.238 mg ml−1 ).

    Techniques: Expressing