Luciferases encompass a wide range of enzymes used for biolumi-nescence, the emission of light produced by a living organism. Lucif-erases are highly prized bioindicators for life science research and drug discovery, owing to their remarkable sensitivity, lack of toxicity and wide dynamic range of quantitation 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 . Since the last review on the biochemistry of beetle bi-oluminescence , considerable progress in understand-ing of the structure/function of firefly luciferases and bio-luminescence color determination in other beetle lu-ciferases has been achieved. In this review, I will give an overview of currently known insect bioluminescent sys Luciferases are enzymes that emit light in the presence of oxygen and a substrate (luciferin) and which have been used for real-time, low-light imaging of gene expression in cell cultures, individual cells, whole organisms, and transgenic organisms This review aims to cover the major existing applications for bioluminescence in the context of the diversity of luciferases and their substrates, luciferins. Particularly, the properties and applications of D -luciferin, coelenterazine, bacterial, Cypridina and dinoflagellate luciferins and their analogues along with their corresponding.
Imaging of light emission from the expression of luciferases in living cells and organisms: a review Lee F. Greer III , Department of Biochemistry, School of Medicine and Department of Natural Sciences—Biology Section; Loma Linda University, Loma Linda, CA, US The chemical reasons for these different colours are hotly debated yet remain unresolved. This Review summarizes the structural, biochemical and spectrochemical data on beetle bioluminescence..
Plasmids. The sources of the luciferases used in this study were plasmids pB-RmL(), pB-RolT226N (), and pBl-PxRe().To make the luciferases suitable for high-level mammalian expression and to minimize inappropriate activation, we optimized the codons and deleted transcription factor binding sites within the cDNA without changing the deduced amino acid sequences (Y. Nakajima, K. Sugata, and Y. Different bioluminescent systems are dependent on specific types of bioluminescent substrates. For instance, firefly and click beetle luciferases are dependent on d-luciferin. Gaussia, and Renilla luciferases are dependent on coelenterazine. These different systems and their associated substrate offer different advantages within biotechnology. Generally, luciferases, which catalyze a reaction with a substrate luciferin and generate light as a product (bioluminescence), are dim, but highly quantitative reporters and suitable to measure how much and when a gene or protein is expressed In this review, we consider luciferases of various luminous organisms that use coelenterazine or Cypridina luciferin as a substrate, as well as modifications of these proteins that improve their physicochemical and bioluminescent properties and therefore their applicability in bioluminescence imaging in vivo The genomic era, highlighted by large scale, genome-wide association studies (GWAS) for both common and rare diseases, have identified hundreds of disease-associated variants. However, most of these variants are not disease causing, but instead only provide information about a potential proximal fun
phylogenetically distant organisms may use homologous luciferases (e.g., parallel evolution observed in some cnidarians, tunicates and echinoderms that are sharing a homologous luciferase-based system). The evolution of luciferases then appears puzzling. The present review takes stock of th Development of a cytotoxicity assay based on transient expression of different luciferases in cytosol. Gaussia luciferase (Gluc; 185 aa, 19.9 kDa) is one of the smallest luciferase known and is. catalysis rates of luciferases vary dramatically among coe-lenterazine-dependent systems. Below we highlight several practically important luciferases that utilize coelenterazine or its analogues. • Renilla luciferase: a medium-sized (36 kDa) cytosolic protein from a coral that produces a steady luminescent signal The evolution of luciferases then appears puzzling. The present review takes stock of the diversity of known bioluminescent proteins, their evolution and potential evolutionary origins. A total of 134 luciferase and photoprotein sequences have been investigated (from 75 species and 11 phyla), and our analyses identified 12 distinct types. In this review, we consider the main directions, results, and achievements in research involving these luciferases. The functioning of bioluminescent systems in most of the known marine organisms is based on the oxidation reaction of the same substrate—coelenterazine (CTZ), catalyzed by luciferase
This mini-review summarizes the recent advances in development of mutant luciferases with improved stability and activity characteristics. It discusses the common limitations of wild-type luciferases in different applications and presents the efficient approaches that can be used to address these problems Facebook now says medical studies published in peer-reviewed journals are FAKE NEWS; An Urgent Message from Professor Sucharit Bhakdi (Video) STUDY: Pfizer vaccine causes catastrophic damage to every system of your body; Big Pharma's Dirty Dozen; BOMBSHELL! Leak Exposes Global Abuse Of Cyber-Spying Weapon To Target Politicians, Activists. Detailed reviews on chemistry and diversity of luciferins (Kaskova et al. 2016), luciferases (Kotlobay et al. 2019), and ecology of bioluminescence (Haddock et al. 2010; Widder 2010), as well as a comprehensive overview of all known bioluminescent systems (Shimomura and Yampolsky 2019), are available. In this article, we provide an. Luciferases in this family have more recently been found and compared for several Metridia species (Takenaka et al., 2012; Takenaka et al., 2013), and have been shown to usually consist of two paralogous pairs of sequences per species. Indeed our Metridia-related luciferases fall out into these two clades Find methods information, sources, references or conduct a literature review on FIREFLY LUCIFERASES. Topic combinations. Learn more. This page combines publications related to two different topics
Abstract Luciferases are enzymes that emit light in the presence of oxygen and a substrate (luciferin) and which have been used for real‐time, Review Article. Free Access. Imaging of light emission from the expression of luciferases in living cells and organisms: a review Unlike the monomeric luciferases discussed above, bacterial luciferase (Lux) is a heterodimer of two genes, luxA and luxB, that must join together to form a functional unit. It is also only one of two systems, along with the fungal system discussed below, that additionally has a known genetic pathway for luciferin synthesis two luciferases that process the same substrate and emit light at different wavelengths. This system is i) ratiometric, with both reporters measured by the same method and at the same time, ii) has a high was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is mad
Luciferases in this family have more recently been found and compared for several Metridia species (Takenaka et al., 2012; Takenaka et al., 2013), and have been shown to usually consist of two paralogous pairs of sequences per species. Indeed our Metridia-related luciferases fall out into these two clades To determine the time of the first appearance (TFA) of the luminescence signal of the Renilla and firefly luciferases, the activities of luciferases in in vitro translation reactions were monitored over 11 min and relative light units were plotted against the time points. The mean background luminescence was determined and the upper limit for the background luminescence was calculated as the. This review first introduces the development of bioluminescent reporters, and next, their applications in sensing biological changes in vitro and in vivo as biosensors. Lastly, we discuss chemiluminescent sensors that produce photons in the absence of luciferases Academia.edu is a platform for academics to share research papers
In this short review, we discuss some of the recent advances on fusion proteins of eucaryotic luciferases and their applications. Special emphasis is placed on a streptavidin-luciferase fusion protein produced by insect cells using the baculovirus expression system. PMID: 10796991 [Indexed for MEDLINE] Publication Types: Comparative Study; Review Luciferases for BLI Applications. Luciferases applied in in vivo BLI include those derived from beetles, bacteria, and various marine species (Table 1), with the firefly luciferase (FLuc) being the most widely used.FLuc requires d-luciferin (a heterocyclic carboxylic acid), ATP, and molecular oxygen for light production.At a pH between 7.5 and 8.5, FLuc catalyzes the reaction between d. Beetle luciferases produce different bioluminescence colors from green to red using the same d-luciferin substrate. Despite many studies of the mechanisms and structural determinants of bioluminescence colors with firefly luciferases, the identity of the emitters and the specific active site interactions responsible for bioluminescence color modulation remain elusive. To address these. The luciferases from different organisms have evolved differently so have different structures and substrates. Enzymes that oxidize certain LUMINESCENT AGENTS to emit light (PHYSICAL LUMINESCENCE). Review. 2019. Review. 2019. Development and Applications of Bioluminescent and Chemiluminescent Reporters and Biosensors
Luciferases and luciferins from other bioluminescent organisms. Although this review has focused on the bioluminescence of beetles and how they evolved from ancestral enzymes that can adenylate fatty acids, nature has devised many solutions to achieve bioluminescence from a handful of luciferins using structurally distinct luciferases characterized in detail, two of which, the luciferases from firefly (Photinus pyralis) and Renilla(Renilla reniformis, a sea pansy), represent a large part of the Promega luminescence portfolio. As a reporter technology, bioluminescence finds its greatest potential by helping to characterize the enormous complexity of living systems Greer LF, Szalay AA: Imaging of light emission from the expression of luciferases in living cells and organisms: a review. Luminescence. 2002, 17: 43-74. 10.1002/bio.676. CAS Article PubMed Google Scholar 12 Luciferases from bacteria (left) and dinoflagellates (right). Annual Review of Cell and Developmental Biology 14, 197-230. T. O. Baldwin (1996) Firefly luciferase: the structure is known, but the mystery remains. Structure 4, 223-228. D. K. Welsh and S. A. Kay (2005) Bioluminescence imaging in living organisms. Current Opinion in.
Critical Review Fireﬂy Bioluminescence: A Mechanistic Approach of Luciferase Catalyzed Reactions Simone M. Marques and Joaquim C. G. Esteves da Silva Centro de Investigac¸a˜o em Quı´mica (CIQ-UP), Department of Chemistry, Faculty of Sciences, University of Porto, Porto, Portugal Summary Luciferase is a general term for enzymes catalyzing. Fingerprint Dive into the research topics of 'A low-volume rapid luciferase immunoprecipitation system (LIPS) assay utilising a novel antigen to detect autoantibodies to zinc transporter 8 (ZnT8A) in type 1 diabetes provides an alternative to conventional radioimmunoassay' Renilla luciferases. Promega Corporation · 2800 Woods Hollow Road · Madison, WI 53711-5399 USA · Toll Free in USA 800-356-9526 · 608-274-4330 · Fax 608-277-2516 5 www.promega.com TM040 · Revised 6/1 Few organisms are capable of glowing in the dark. Perhaps the best known example is the firefly, a beetle that can emit flashes of yellow-green light when the small molecule d-luciferin is oxidized by the enzyme firefly luciferase. Here we show that a homologous enzyme in fruit flies is also capable of bioluminescence, but only when treated with a rigid synthetic analog of d-luciferin Luciferase assays can be used to investigate a variety of cellular processes using bioluminescent light output as a sensitive measure of biological activity. We offer a full range of luciferase assay products and tools for your research. Reporter options include NanoLuc®, firefly and Renilla luciferases, which have different protein sizes.
Open access peer-reviewed chapter. Thermostabilization of Firefly Luciferases Using Genetic Engineering. By Natalia Ugarova and Mikhail Koksharov. Submitted: March 18th 2011 Reviewed: August 18th 2011 Published: January 18th 2012. DOI: 10.5772/3047 Research output: Contribution to conference › Conference Abstract › peer-review TY - CONF T1 - A low-volume rapid luciferase immunoprecipitation system (LIPS) assay utilising a novel antigen to detect autoantibodies to zinc transporter 8 (ZnT8A) in type 1 diabetes provides an alternative to conventional radioimmunoassa Bioluminescence imaging (BLI) is a powerful tool for cell tracking, monitoring of gene delivery and expression in small laboratory animals. An alternative luciferase (Luc) substrate cyclic luciferin (Cycluc) was recently advanced for BLI applications as providing a stronger, more stable signal at significantly lower doses than the classical substrate D-luciferin (D-Luc) increasing sensitivity. This Review summarizes the structural, biochemical and spectrochemical data on beetle bioluminescence reported over the past three decades. We identify the factors that govern what colour is emitted by wild-type and mutant luciferases. This topic is controversial, but, in general, we note that green emission requires cationic residues in a.
Luciferase assay systems enable the real-time monitoring of gene expression in living cells. We have developed a dual-color luciferase assay system in which the expression of multiple genes can be tracked simultaneously using green- and red-emitting beetle luciferases. We have applied the system to monitoring independent gene expressions in two types of cocultured fibroblasts in real time -review summarizes the recent advances in development of mutant luciferases with improved stability and activity characteristics. It discusses the common limitations of wild-type luciferases in different applications and presents the efficient approaches that can be used to address these problems luciferases lual luciferase pcdna3 coelenterazine Prior art date 2000-11-23 Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Active Application number US14/714,166 Other versions US20150247131A1 (en. Luciferase is a generic term for the class of oxidative enzymes used in bioluminescence. Firefly luciferase as a laboratory reagent usually refers to P. pyralis luciferase although recombinant luciferases from several other species of fireflies are also commercially available Phrixothrix railroad-worms emit yellow-green light through 11 pairs of lateral lanterns along the body and red light through two cephalic lanterns. The cDNAs for the lateral lanterns luciferase of Phrixothrix vivianii, which emit green light (λmax= 542 nm), and for the head lanterns of P. hirtus, which emit the most red-shifted bioluminescence (λmax= 628 nm) among luminescent beetles, were.
This Review summarizes the structural, biochemical and spectrochemical data on beetle bioluminescence reported over the past three decades. We identify the factors that govern what colour is emitted by wild-type and mutant luciferases The SuperLight™ Dual-Luciferase Reporter Gene Assay allows for the sequential measurement of the activity of two different luciferases, firefly (FFL) and Renilla (RL), in a single sample. The firefly luciferase luminescence is measured first by addition of the FFL Reagent. Next, the RL Reagent is added to the same well D-Luciferin is the substrate of luciferases that catalyze the production of light in bioluminescent insects  . D-luciferin is the natural substrate of the enzyme luciferase (Luc), that catalyzes the production of the typical yellowgreen light of fireflies.The present review covers the synthesis of D-luciferin and derivatives or analogues.
Peer Reviewed Papers. Comparison of properties of commercially available crystalline native and recombinant firefly luciferases. S R Ford et al. Journal of bioluminescence and chemiluminescence, 7(3), 185-193 (1992-07-01 Luciferases synonyms, Luciferases pronunciation, Luciferases translation, English dictionary definition of Luciferases. n. An enzyme present in the cells of bioluminescent organisms that catalyzes the oxidation of luciferin and ATP, producing light. (reviewed in Haddock et al., 2010). Bioluminescent organs of two deep-sea arrow worms. ZERO BIAS - scores, article reviews, protocol conditions and more. Home > Search Results > New England Biolabs > pet28a vector. pet28a vector (New England Biolabs) New England Biolabs is a verified supplier luciferases were amplified by PCR (primer sequences 5′-ACCGGTCAAGCTTGGTACC-3′ and 5′-GCATCTTACTTGGCATGACAGTAAG-3′) from pGLuc. Review Substrates for Microsomal Dealkylases, Acetyltransferases, Luciferases and Other Enzymes—Section 10.6 and Photoactivatable Reagents, Including Photoreactive Crosslinkers and Caged Probes—Section 5.3 in the Molecular Probes® Handbook for more information on these products. For Research Use luciferases share sequence homology with each other (5). Luciferases occur in bacteria, fungi, dinoﬂagellates, radiolarians and about 17 metazoan phyla and 700 genera, mostly marine (5, 12, 13). These include Anne-lida (segmented worms), Chordata (some elasmobran-chiomorphs or sharks, many teleosts or bony ﬁshes)
Luciferase Immunoprecipitation System (LIPS) assay is a rapid, simple, and sensitive test to detect antibody response to respiratory syncytial viru REVIEW ARTICLE Enzymatic promiscuity and the evolution of bioluminescence beetle luciferases use the same substrate, but they do not all emit light of the same color . While most ﬁreﬂy species emit yellow-green light, some click bee-tles emit orange light . Since oxyluciferin is th Luciferases that remained in the cytoplasm such as firefly and Renilla were compared to that from Gaussia which is an extracellular luciferase. Additionally, two extracellular domains were tested, one predicted to target the media (CDcel) and the other predicted to target the periplasmic space (PelB)
the lateral transfer of luciferases. In fact, as the sequences of more luciferases become known, cross-phylum homologies have yet to be uncovered. Among some coelenterates, the luminescent Ca2+-binding photoproteins appear to be derived from a common calmodulin-like ancestor (Inouye et al. 1985), but the origins of other marine luciferases and. Review past issues of TekTalk, BioTek's complimentary life science instrumentation e-newsletter. Since their introduction, discovery of luciferases from a variety of organisms, primarily marine sources, have been introduced and offer distinct properties such as secretion into cell culture medium and increased stability. However, many of the. The luciferase reporter assay is commonly used as a tool to study gene expression at the transcriptional level. It is widely used because it is convenient, relatively inexpensive, and gives quantitative measurements instantaneously. It has broad applications across various fields of cell and molecular biology - wherever you want to measure or track expression of a cloned gene Abstract Bioluminescence has evolved independently many times; thus the responsible genes are unrelated in bacteria, unicellular algae, coelenterates, beetles, fishes, and others. Chemically, all involve exergonic reactions of molecular oxygen with different substrates (luciferins) and enzymes (luciferases), resulting in photons of visible light (≈50 kcal). In addition to the structure of.
Lucifer means light-bringer, and luciferases are a loose family of enzymes that are used by many organisms to produce light - a phenomenon known as bioluminescence.. They are a loose family in the sense that different light-producing enzymes use different substrates and have different structures. The generic term for the luciferase substrate is luciferin; which refers to a variety of. The activity regenerating luciferin from the luminescent product oxyluciferin was found in the protein fraction of a lantern extract from Photinus pyralis. The protein, luciferin-regenerating enzyme (LRE), was purified to homogeneity by ammonium sulfate precipitation followed by successive column chromatography on Ultrogel AcA34, S-Sepharose FF, Q-Sepharose FF, TSKgel super Q 5pw and TSKgel. In the present study, the researchers first reviewed characteristics of the amino-acid sequences of conventional luciferases obtained from copepods and reanalyzed their functionality. It is believed that more frequently occurring amino acids are the consequence survived by natural selection over a long period of evolution and thus would. This review is intended to provide an overview of recent basic developments and applications in BL studies, and showcases the bioanalytical utilities. We hope that this review can be luciferases. cDNAs encoding luciferases can be genetically engineered to create bioluminescent probes with improve Review Seeing (and Using) the Light: Recent Developments in Bioluminescence Technology Anna C. Love 1and Jennifer A. Prescher,2 3 * 1Department of Chemistry, University of California, Irvine, Irvine, CA 92697, USA 2Department of Molecular Biology & Biochemistry, University of California, Irvine, Irvine, CA 92697, USA 3Department of Pharmaceutical Sciences, University of California, Irvine.
A preprint is a complete scientific manuscript that an author uploads on a public server for free viewing. Initially it is posted without peer review, but may acquire feedback or reviews as a preprint, and may eventually be published in a peer-reviewed journal. The posting of preprints on public servers allows almost immediate dissemination and. 3.1. 2A Peptide Cleavage for Equimolar Expression of eGFP and Luciferases. It has been demonstrated that 2A peptides can be used for stoichiometric coexpression of proteins. 5, 7 For quantitative comparison of different luciferases for BLI, bicistronic plasmids were constructed in which CBGr99, CBRed, and Fluc was linked to the eGFP sequence via a P2A sequence [Fig. 1a] luciferases from both families use the same substrate, which is a heterocyclic water soluble acid (benzothiazoyl-thiazole) generally called luciferin. Luciferin is oxidised in an ATP-dependent manner leading to oxyluciferin, AMP, CO 2,and. infection. in-review,.
The present study demonstrates cation-driven optical properties of artificial luciferases (ALucs) from copepod luciferases, as an optical readout for bioanalysis. An assignment of the supersecondary structure code (SSC) of ALucs revealed that ALucs carry a helix-loop-helix structure, which appears at the same sites of the EF-hands of typical Ca. Stable Plant Transformation. In a stable plant transformation, the foreign DNA is fully integrated into the host genome and expressed in later generations of the plant. This type of plant transformation is used for longer-term research of genes or production of a trait/compound on a large scale. For instance, a stable transformation project can. The secreted luciferases derived from Gaussia princeps, Metridia longa and Cypridina noctiluca do not require cell lysis to measure activity and are significantly brighter than firefly and Renilla. These features make these luciferases ideal for repeated assays, sensitive measurements in miniaturized assays and single cell applications
Luciferasen sind strukturell unterschiedliche Enzyme, durch deren katalytische Aktivität Luciferine mit Sauerstoff zu energiereichen, instabilen Dioxetanen oder Dioxetanonen reagieren ().Beim Zerfall dieser Substanzen kommt es zur Biolumineszenz.Unterschieden werden unter anderem Firefly-Luciferasen (aus dem Leuchtkäfer), bei denen Luciferol, ATP und Sauerstoff zu Kohlendioxid, AMP und Licht. Novel Luciferases In recent years other luciferases have been used for reporter gene assays, such as Gaussia, Cypridina or NanoLuc® luciferases. These so-called novel luciferases are up to 1000 times brighter than Firefly or Renilla luciferases, and usually have other advantages, for example, improved stability, smaller size. INTRODUCTION. Bioluminescence, the result of a process that occurs in living organisms in which an electronically excited substance produced in a chemical reaction decays to the ground level 1, is a widespread phenomenon in Nature.The scientific research on this subject led to the discovery of the enzyme-substrate system, the former called luciferase and the latter luciferin (from the Latin.
. Luminescence. 2002; 17: 43-74. Crossref Medline Google Scholar; 16 Weissleder R, Simonova M, Bogdanova A, Bredow S, Enochs WS, Bogdanov A Jr. MR imaging and scintigraphy of gene expression through melanin induction. Radiology. 1997; 204: 425. Nano-lanterns, like other luciferases, exhibit broad emission spectra, complicating their resolution by color alone. Further resolution can be achieved using luciferases that respond to distinct luciferin scaffolds, but longer imaging times are required as the substrates (which was not certified by peer review) is the author/funder. All. Red-emitting Firefly luciferase (λmax 617 nm) and Green-emitting Firefly luciferases frrom the Italian firefly Luciola Italica - Thermostable mutant, 1000-fold brighter than it's native counterpart. Also available in secretable form. Green-emitting firely luciferase (λmax 550 nm) from Luciola Italica
The present invention encompasses modified luciferases, methods for making modified luciferases, and assays utilizing modified luciferases. Modified luciferases of the invention show increased activity over wildtype luciferases and also show increased stability of signal. The present invention also encompasses multiplex assays utilizing multiple luciferases reporters with different emission. Abu Dhabi: A team of researchers from the New York University Abu Dhabi's (NYUAD) is studying the natural production of light, called bioluminescence, with the aim of helping others in the field.
In the new study The Elusive Relationship Between Structure and Colour Emission in Beetle Luciferases, which is featured on the cover of the journal Nature Reviews Chemistry, Naumov and colleagues provide the most comprehensive critical overview of the field of the bioluminescence of beetles, including fireflies, to date. November 25, 202 Review. Reporter Gene Imaging. Hyewon Youn 1, 2, 3 and June-Key Chung 1, 3 Chloramphenicol acetyltransferase , β-galactosidase , luciferases , and fluorescent proteins [7, 8] have been conventionally used to monitor cellular processes in assays of reporter activity. However, these optical reporters cannot be used directly in living animals. Evidence Review. A medical librarian with a perioperative background conducted a systematic search of the databases Ovid MEDLINE ®, Ovid Embase ®, EBSCO CINAHL ®, and the Cochrane Database of Systematic Reviews.The search was limited to literature published in English from January 2014 through August 2019
Background: AMV564 is a novel bivalent, bispecific (2x2) CD33/CD3 targeted immunotherapy that binds both CD33 and the invariant CD3ε on T-cell receptors with strong avidity, thus creating an immune synapse between CD33-expressing cells and T cells, initiating T-cell directed lysis of CD33 expressing cells, and inducing expansion, differentiation and proliferation of T cells BPS Bioscience Inc., headquartered in the heart of one of the world's largest clusters of life science research institutes and companies, San Diego, California is the leading provider of highest quality HDACs, histone demethylases and methyltransferases, ubiquitin pathway proteins, phosphodiesterases, kinases, phosphatases, and other recombinant enzymes
Research output: Contribution to journal › Article › peer-review TY - JOUR T1 - Constitutively active Rheb mutants [T23M] and [E40K] drive increased production and secretion of recombinant protein in Chinese hamster ovary cell Next, 0.2 μg TNRC6C-AS1 3′UTR/LPAR5 3′UTR luciferase, 0.04 μg plasmid pRLSV40, 0.6 μg of miR-513c-5p or pGreenPuro control vector were transfected into SW579 and TPC-1 cells and incubated for 58 h. Dual‐luciferase reporter assay Kit (Promega WI, USA) was used to measure the activities of firefly and renilla luciferases Luciferases—Advances in Research and Application: 2012 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about Luciferases in a concise format. research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited.