“Luciferase. Can’t make this up.”
Yup, Looks like they can.
This is both series and Hugh.
Can’t wait to see the next bombshell. They are becoming parodies of themselves.
Posted on 10/15/2021, 1:08:50 PM by ransomnote
ransomnote: I see some jeering the existance of the chemical compound known as 'Luciferase' and want to do my part to share information about this well known chemical and some of its scientific uses, particularly now that a Pfizer whistleblower is claiming it's in the Covid 'vaccine'. ON Free Republic: BOMBSHELL: Pfizer whistleblower says vaccine ‘glows,’ contains toxic luciferase, graphene oxide compounds (freerepublic.com)
In addition to the Fireflies article at the top of my post, I added additional information about Luciferase from the FDA, ScienceDirect and Wikipedia to help bring peeps up to speed.
SNIP
To develop the assay, the FDA scientists genetically engineered RSV G proteins from both subgroups. They tagged each G protein with luciferase, an enzyme that interacts with a protein called luciferin to release light.
The luciferase-tagged G proteins (RSV-GA and RSV-GB) acted as “bait” to antibodies against the G proteins in samples of human serum (the clear fluid of blood without red or white cells), causing them to bind to the tagged proteins. The scientists added special protein beads that bind the antibodies with the luciferase-tagged G proteins to the bottom of a plastic test well. Then they added luciferin and measured the amount of light released when it interacted with luciferase, which enabled them to calculate how strong the antibody response was to the G proteins.
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Luciferase - an overview | ScienceDirect Topics
P. Riggs, in Brenner's Encyclopedia of Genetics (Second Edition), 2013
Luciferases are enzymes that produce light when they oxidize their substrate. The gene for the most common luciferase comes from the firefly, but luciferases from other animals such as the sea pansy Renilla reniformis, the copepod Gaussia princeps, and the ostracod Cypridina noctiluca are also used as reporters. When a luciferase is fused to a protein of interest, its expression can be measured very accurately using a luminometer. The firefly luciferase reaction requires its substrate luciferin, plus adenosine triphosphate (ATP), O2, and Mg2+. The Renilla and Gaussia luciferases use coelenterazine as their substrates; Cypridina uses its own luciferin as a substrate. Luciferases are commonly used to report the expression level of proteins to which they are fused.
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| Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the and enzyme, respectively.[1] Both words are derived from the Latin word lucifer, meaning "lightbearer", which in turn is derived from the Latin words for "light" (lux) and "to bring or carry" (ferre).[2] |
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Luciferases are widely used in biotechnology, for microscopy and as reporter genes, for many of the same applications as fluorescent proteins. However, unlike fluorescent proteins, luciferases do not require an external light source, but do require addition of luciferin, the consumable substrate.
Luciferases can be produced in the lab through genetic engineering for a number of purposes. Luciferase genes can be synthesized and inserted into organisms or transfected into cells. As of 2002, mice, silkworms, and potatoes are just a few of the organisms that have already been engineered to produce the protein.[14]
In the luciferase reaction, light is emitted when luciferase acts on the appropriate luciferin substrate. Photon emission can be detected by light sensitive apparatus such as a luminometer or modified optical microscopes. This allows observation of biological processes.[15] Since light excitation is not needed for luciferase bioluminescence, there is minimal autofluorescence and therefore virtually background-free fluorescence.[16] Therefore, as little as 0.02 pg can still be accurately measured using a standard scintillation counter.[17]
In biological research, luciferase is commonly used as a reporter to assess the transcriptional activity in cells that are transfected with a genetic construct containing the luciferase gene under the control of a promoter of interest.[18] Additionally, proluminescent molecules that are converted to luciferin upon activity of a particular enzyme can be used to detect enzyme activity in coupled or two-step luciferase assays. Such substrates have been used to detect caspase activity and cytochrome P450 activity, among others.[15][18]
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