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Topic: Luciferase

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	ARS \| Publication request: Construction and Testing of An Intron-Containing Luciferase Reporter Gene from Renilla ...
		However, the original luciferase gene was also active within the bacteria (Agrobacteria) normally used to move genes into plants, creating an undesirable background of light in tissues that were infected with Agrobacteria during the process of genetic engineering.
		We have modified the sea pansy luciferase gene by the introduction of DNA sequence containing an intron.
		The new luciferase gene is a significant improvement for assays using luciferase expression to measure gene activity within plant cells.
	www.ars.usda.gov /research/publications/publications.htm?SEQ_NO_115=151342 (453 words)

	Luciferase
		Luciferase is any enzyme that can be used in nature for bioluminescence, or the production of light generated from a living creature.
		The rate of reaction of luciferin with oxygen is quite slow until luciferase stimulates or catalyzes it, sometimes with the help of calcium ions; this action is similar to the energy used to stimulate muscle contraction.
		Luciferase can be produced in the lab via genetic engineering, and is used for tracking and visualization of different biological processes.
	www.iscid.org /encyclopedia/Luciferase (247 words)

	luciferase concentration?-Protein and Proteomics
		What you would need is some kind of control to relate the values of luciferase in your samples to it- usually it would be beta-gal or renilla-luc expressed under the control of a constitutive strong promoter such as RSV or CMV.
		You should co-transfect this control with your luciferase plasmid, so that you can use the control to correct for things such as the differences in cell number or the transfection efficiency from well-to-well.
		In the case of the luciferase assays, let's say you're studying a promoter of interest cloned into pGL3 and you want to study the influence of different hormones on its activity, for instance.
	www.protocol-online.org /archive/posts/5543.html (0 words)

	Bioluminescence \| World of Microbiology and Immunology
		Luciferases isolated from fireflies and other beetles are commonly used in research.
		After adding a known amount of luciferin and luciferase to a blood or tissue sample, the cofactor concentrations may be determined from the intensity of the light emitted.
		Luciferase is often used as a "reporter gene" to study how individual genes are activated to produce protein or repressed to stop producing protein.
	www.bookrags.com /research/bioluminescence-wmi (724 words)

	Luciferase - Biocrawler (Site not responding. Last check: )
		Luciferase is a generic name for enzymes commonly used in nature for bioluminescence.
		Luciferase can be produced in the lab through genetic techniques, and has a wide variety of uses.
		Luciferase can be used in blood banks to determine if red blood cells are starting to break down.
	www.biocrawler.com /encyclopedia/Luciferase (353 words)

	LUCIFERASE : Encyclopedia Entry
		The rates of this reaction between luciferin and oxygen are extremely slow until they are catalyzed by luciferase, often mediated by the presence of calcium ions (an analog of muscle contraction).
		Luciferase can be produced in the lab through genetic engineering for a number of purposes.
		Luciferase is a very heat sensitive protein that is used in studies on protein denaturation, testing the protective capacities of heat shock proteins.
	www.bibleocean.com /OmniDefinition/Luciferase (459 words)

	Promega Dual-Luciferase Method for genetic reporter assays using the Veritas multiwell plate microplate luminometer
		Transcriptional regulation, coupled to the expression of a luciferase reporter gene, is regularly used to study a wide range of biological events in cultured cells.
		Luciferase is an ideal reporter because of the absence of endogenous luciferase activity in mammalian cells, and the functional enzyme is created immediately upon translation
		Use reconstituted Luciferase Assay II Reagent (LAR II) on the same day it is prepared, or aliquot into working volume and store at -20°C for 1 month or 70°C for up to one year.
	www.turnerbiosystems.com /doc/appnotes/S_0084.html (1104 words)

	The Scientist : Bring Out The Sunglasses: Promega's Dual-Luciferase Reporter Assay System
		For example, the firefly luciferase may be coupled to a regulated promoter to study the structural or physiological basis of regulated gene expression.
		Firefly luciferase is a 61 kDa single-subunit enzyme that catalyzes the ATP-dependent oxidation of beetle luciferin.
		The Renilla luciferase is a 36 kDa monomeric enzyme that catalyzes the oxidation of coelenterazine.
	www.the-scientist.com /article/display/18157 (617 words)

	Luciferase Measurements Using the Clarity Luminescence Microplate Reader \| Application Notes
		Luciferase enzyme and its subsequent luminescent reaction is often the gene reporter of choice for many experimental conditions.
		Firefly luciferase is a monomeric 61 kD enzyme that catalyses a two-step oxidation of luciferin, which yields light at 560 nm.
		During the read, 100 µl of luciferase substrate was added to each well and after a 2 second delay the luminescent signal was measured kinetically for a period of 10 seconds.
	www.biotek.com /resources/tech_res_detail.php?id=141 (1754 words)

	Bioluminescence Summary
		In the presence of ATP and the luciferase enzyme, a complex containing all three is formed.
		It is generated by an enzyme-catalyzed chemoluminescence reaction, wherein a luciferin (a kind of pigment) is oxidised by a luciferase (a kind of enzyme).
		Luciferase systems are widely used in the field of genetic engineering as reporter genes (see green fluorescent protein, and picture left).
	www.bookrags.com /Bioluminescence (2941 words)

	PNAS -- Huang et al. 102 (5): 1649 Figure IG4 (Site not responding. Last check: )
		Activity of luciferase was determined by normalizing the measured light units of firefly luciferase with the measured Renilla luciferase activity.
		Luciferase analysis and immunoblotting were performed as in A.
		Luciferase analysis and immunoblotting were performed as in A.(D) NIH 3T3 cells were transfected with luciferase reporter 3xIRS-Luc and FOXO1.
	intl.pnas.org /cgi/content-nw/full/102/5/1649/FIG4 (201 words)

	The 1.5-A Resolution Crystal Structure of Bacterial Luciferase in Low Salt Conditions -- Fisher et al. 271 (36): 21956 ...
		Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light.
		The x-ray structure of bacterial luciferase has been refined to a conventional R-factor of 18.2% for all recorded synchrotron data between 30.0 and 1.50-Å resolution.
		A comparison of the structural similarities between luciferase and a nonfluorescent flavoprotein, which is expressed in the lux operon of one genus of bioluminescent bacteria, suggests that the two proteins originated from a common ancestor.
	www.jbc.org /cgi/content/abstract/271/36/21956 (0 words)

	Luciferase
		A diverse group of organisms use luciferase-mediated bioluminescence to startle predators or to attract prey or mates.
		The luciferase from the North American firefly releases green light during the oxidation of its chemical substrate, luciferin.
		Luciferase is particularly useful as a reporter in living cells and organisms.
	template.bio.warwick.ac.uk /staff/amillar/lucifer.html (0 words)

	[No title]
		Bacterial luciferase is a flavin monooxygenase that catalyses the oxidation of long-chain aldehydes and releases energy in the form of visible light, and which uses flavin as a substrate rather than a cofactor [1].
		There are structural similarities between bacterial luciferase and nonfluorescent flavoproteins (LuxF, FP390), alkanesulphonate monooxygenase (SsuD), and coenzyme F420-dependent terahydromethanopterin reductase, which make up clearly related families with somewhat different folds [2, 3, 4].
		Thoden J.B. Holden H.M. Fisher A.J. Sinclair J.F. Wesenberg G. Baldwin T.O. Rayment I. Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR011251 (0 words)

	Isolation and Expression of a cDNA Encoding Renilla reniformis Luciferase -- Lorenz et al. 88 (10): 4438 -- Proceedings ...
		Isolation and Expression of a cDNA Encoding Renilla reniformis Luciferase -- Lorenz et al.
		Isolation and Expression of a cDNA Encoding Renilla reniformis Luciferase
		The recombinant luciferase expressed in Escherichia coli is identical to native luciferase as determined by SDS/PAGE, immunoblot analysis, and bioluminescence emission characteristics.
	www.pnas.org /cgi/content/short/88/10/4438 (0 words)

	Cloning of Firefly Luciferase cDNA and the Expression of Active Luciferase in Escherichia coli -- Wet et al. 82 (23): ...
		Cloning of Firefly Luciferase cDNA and the Expression of Active Luciferase in Escherichia coli -- Wet et al.
		Cloning of Firefly Luciferase cDNA and the Expression of Active Luciferase in Escherichia coli
		The library was screened with anti-P. pyralis luciferase (Photinus luciferin:oxygen 4-oxidoreductase, EC 1.13.12.7) antibody, and several cDNA clones expressing luciferase antigens were isolated.
	www.pnas.org /cgi/content/abstract/82/23/7870 (0 words)

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