fluorescence microplate reader gomax-multi (Promega)

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Promega fluorescence microplate reader gomax-multi

The depicted plot shows the absolute <t>fluorescense.of</t> the formed PfG-Protein-BGTP complex monitored at a wavelength between 480 nm and 510 nm versus increasing protein concentrations with a crude extract of the purified expressed PfG- protein (black square) and a purified enzyme preparation (black circle) after native purificaion. A non-recombinant pET-28a vector (open triangle) and a constitutively expressed Gα s human subunit (open square) were employed as a positive and a negative control. Each point represents the mean value of three different experiments.

Fluorescence Microplate Reader Gomax Multi, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fluorescence+multi+function+microplate+reader/pmc04634863-112-12-16?v=Promega
Average 90 stars, based on 1 article reviews

fluorescence microplate reader gomax-multi - by Bioz Stars, 2026-08

90/100 stars

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1) Product Images from "A Putative Non-Canonical Ras-Like GTPase from P . falciparum : Chemical Properties and Characterization of the Protein"

Article Title: A Putative Non-Canonical Ras-Like GTPase from P . falciparum : Chemical Properties and Characterization of the Protein

Journal: PLoS ONE

doi: 10.1371/journal.pone.0140994

The depicted plot shows the absolute fluorescense.of the formed PfG-Protein-BGTP complex monitored at a wavelength between 480 nm and 510 nm versus increasing protein concentrations with a crude extract of the purified expressed PfG- protein (black square) and a purified enzyme preparation (black circle) after native purificaion. A non-recombinant pET-28a vector (open triangle) and a constitutively expressed Gα s human subunit (open square) were employed as a positive and a negative control. Each point represents the mean value of three different experiments.

Figure Legend Snippet: The depicted plot shows the absolute fluorescense.of the formed PfG-Protein-BGTP complex monitored at a wavelength between 480 nm and 510 nm versus increasing protein concentrations with a crude extract of the purified expressed PfG- protein (black square) and a purified enzyme preparation (black circle) after native purificaion. A non-recombinant pET-28a vector (open triangle) and a constitutively expressed Gα s human subunit (open square) were employed as a positive and a negative control. Each point represents the mean value of three different experiments.

Techniques Used: Purification, Recombinant, Plasmid Preparation, Negative Control

Part A Absolute Fluorescense of binding of 50 nmol BODIPY FL GTPγS to the plasmodial, PfG-protein (black line). The increase in fluorescence was monitored until saturation over a time interval of 600 s. Part B At the arrow at t = 200 s, 20 μM unlabeled GTPγS was added and the decrease in fluorescence was monitored. The dissociation of BODIPY FL GTPγS was fit with single exponential functions and the half life value was determined i.e. t 1/2 = 9 s suggesting a low affinity for the binding of BODIPY FL GTP. b Monitoring GTP-binding of the P . falciparum G-protein in a time course experiment: Binding assay with different protein concentrations of PfG from Plasmodium green line 62.5 μg, red line 16,5 μg; the reaction was antagonized with unlabeled GTP after 100 s blue line (62,5 μg purified G-protein), purple line (16,5 μg purified-G-protein), yellow line (8,0 μg G-protein).

Figure Legend Snippet: Part A Absolute Fluorescense of binding of 50 nmol BODIPY FL GTPγS to the plasmodial, PfG-protein (black line). The increase in fluorescence was monitored until saturation over a time interval of 600 s. Part B At the arrow at t = 200 s, 20 μM unlabeled GTPγS was added and the decrease in fluorescence was monitored. The dissociation of BODIPY FL GTPγS was fit with single exponential functions and the half life value was determined i.e. t 1/2 = 9 s suggesting a low affinity for the binding of BODIPY FL GTP. b Monitoring GTP-binding of the P . falciparum G-protein in a time course experiment: Binding assay with different protein concentrations of PfG from Plasmodium green line 62.5 μg, red line 16,5 μg; the reaction was antagonized with unlabeled GTP after 100 s blue line (62,5 μg purified G-protein), purple line (16,5 μg purified-G-protein), yellow line (8,0 μg G-protein).

Techniques Used: Binding Assay, Fluorescence, Purification

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fluorescence microplate reader gomax-multi (Promega)

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1) Product Images from "A Putative Non-Canonical Ras-Like GTPase from P . falciparum : Chemical Properties and Characterization of the Protein"

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