Month: November 2022

On December 31, 2020, Wu, Nan; Kobayashi, Naohiro; Tsuda, Kengo; Unzai, Satoru; Saotome, Tomonori; Kuroda, Yutaka; Yamazaki, Toshio published an article.HPLC of Formula: 55779-48-1 The title of the article was Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. And the article contained the following:

Abstract: Gaussia luciferase (GLuc) is a small luciferase (18.2 kDa; 168 residues) and is thus attracting much attention as a reporter protein, but the lack of structural information is hampering further application. Here, we report the first solution structure of a fully active, recombinant GLuc determined by heteronuclear multidimensional NMR. We obtained a natively folded GLuc by bacterial expression and efficient refolding using a Solubility Enhancement Petide (SEP) tag. Almost perfect assignments of GLuc′s 1H, 13C and 15N backbone signals were obtained. GLuc structure was determined using CYANA, which automatically identified over 2500 NOEs of which > 570 were long-range. GLuc is an all-alpha-helix protein made of nine helixes. The region spanning residues 10-18, 36-81, 96-145 and containing eight out of the nine helixes was determined with a Cα-atom RMSD of 1.39 Å ± 0.39 Å. The structure of GLuc is novel and unique. Two homologous sequential repeats form two anti-parallel bundles made by 4 helixes and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helixes. Further, we found a hydrophobic cavity where several residues responsible for bioluminescence were identified in previous mutational studies, and we thus hypothesize that this is a catalytic cavity, where the hydrophobic coelenterazine binds and the bioluminescence reaction takes place. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).HPLC of Formula: 55779-48-1

The Article related to amino acid sequence, animals, copepoda: enzymology, disulfides: chemistry, imidazoles: metabolism, luciferases: chemistry, luciferases: metabolism, nuclear magnetic resonance, biomolecular: methods, protein conformation, protein domains, protein folding, pyrazines: metabolism and other aspects.HPLC of Formula: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On January 8, 2022, Inouye, Satoshi; Nakamura, Mitsuhiro; Hosoya, Takamitsu published an article.COA of Formula: C26H21N3O3 The title of the article was Enzymatic conversion of dehydrocoelenterazine to coelenterazine using FMN-bound flavin reductase of NAD(P)H:FMN oxidoreductase. And the article contained the following:

Coelenterazine (CTZ) is known as luciferin (a substrate) for the luminescence reaction with luciferase (an enzyme) in marine organisms and is unstable in aqueous solutions The dehydrogenated form of CTZ (dehydrocoelenterazine, dCTZ) is stable and thought to be a storage form of CTZ and a recycling intermediate from the condensation reaction of coelenteramine and 4-hydroxyphenylpyruvic acid to CTZ. In this study, the enzymic conversion of dCTZ to CTZ was successfully achieved using NAD(P)H:FMN oxidoreductase from the bioluminescent bacterium Vibrio fischeri ATCC 7744 (FRase) in the presence of NADH (the FRase-NADH reaction). CTZ reduced from dCTZ in the FRase-NADH reaction was identified by HPLC and LC/ESI-TOF-MS analyses. Thus, dCTZ can be enzymically converted to CTZ in vitro. Furthermore, the concentration of dCTZ could be determined by the luminescence activity using the CTZ-utilizing luciferases (Gaussia luciferase or Renilla luciferase) coupled with the FRase-NADH reaction. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).COA of Formula: C26H21N3O3

The Article related to aliivibrio fischeri: enzymology, aliivibrio fischeri: genetics, animals, bacterial proteins: genetics, bacterial proteins: metabolism, biocatalysis, biotransformation, chromatography, high pressure liquid, flavin mononucleotide: metabolism, gene expression, imidazoles: metabolism, kinetics, luciferases: genetics and other aspects.COA of Formula: C26H21N3O3

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On March 31, 2021, Dijkema, Fenne Marjolein; Nordentoft, Matilde Knapkoeien; Didriksen, Anders Kroell; Corneliussen, Anders Svaerke; Willemoes, Martin; Winther, Jakob R. published an article.Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one The title of the article was Flash properties of Gaussia luciferase are the result of covalent inhibition after a limited number of cycles. And the article contained the following:

Luciferases are widely used as reporters for gene expression and for sensitive detection systems. The luciferase (GLuc) from the marine copepod Gaussia princeps, has gained popularity, primarily because it is secreted and displays a very high light intensity. While firefly luciferase is characterized by kinetic behavior which is consistent with conventional steady-state Michaelis-Menten kinetics, GLuc displays what has been termed “flash” kinetics, which signify a burst in light emission followed by a rapid decay. As the mechanistic background for this behavior was unclear, we decided to decipher this in more detail. We show that decay in light signal is not due to depletion of substrate, but rather is caused by the irreversible inactivation of the enzyme. Inactivation takes place after between 10 and 200 reaction cycles, depending on substrate concentration and can be described by the sum of two exponentials with associated rate constants The dominant of these increases linearly with substrate concentration while the minor is substrate-concentration independent. In terms of rate of initial luminescence reaction, this increases with the substrate concentration to the power of 1.5 and shows no signs of saturation up to 10 μM coelenterazine. Finally, we find that the inactivated form of the enzyme has a larger apparent size in both size exclusion chromatog. and SDS-PAGE anal. and shows a fluorescence peak at 410 nm when excited at 333 nm. These findings indicate that the “flash” kinetics in Gaussia luciferase are caused by an irreversible covalent binding to a substrate derivative during catalysis. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to animals, copepoda: enzymology, copepoda: genetics, escherichia coli: genetics, imidazoles: chemistry, imidazoles: metabolism, kinetics, luciferases: chemistry, luciferases: genetics, luciferases: metabolism, pyrazines: chemistry, pyrazines: metabolism, recombinant proteins: chemistry, recombinant proteins: genetics and other aspects.Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Nishihara, Ryo; Abe, Masahiro; Suzuki, Koji; Kim, Sung-Bae published an article in 2021, the title of the article was Luciferase-Specific Coelenterazine Analogues for Optical Cross Talk-Free Bioassays.Category: pyrazines And the article contains the following content:

Spectral overlaps in fluorescence (FL) and bioluminescence (BL) commonly cause optical cross talks. The present protocol introduces five different lineages of coelenterazine (CTZ) analogs, which have selectivity to a specific luciferase, and thus cross talk-free. For example, some CTZ analogs with ethynyl or styryl groups display dramatically biased BL to specific luciferases and pH by modifying the functional groups at the C-2 and C-6 positions of the imidazopyridinne backbone of CTZ. The optical cross talk-free feature is exemplified with the multiplex system, which simultaneously illuminated antiestrogenic and rapamycin activities without optical cross talks. This unique protocol contributes to specific and high-throughput BL imaging of multiple optical readouts in mammalian cells without optical contamination. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Category: pyrazines

The Article related to alkynes: chemistry, animals, chlorocebus aethiops, cos cells, estrogen receptor modulators: pharmacology, imidazoles: chemistry, immunosuppressive agents: pharmacology, luciferases: drug effects, luciferases: metabolism, luminescent agents: chemistry, luminescent measurements: methods, optical imaging: methods, pyrazines: chemistry and other aspects.Category: pyrazines

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Gomez-Ramirez, Manuel; More, Alexander I.; Friedman, Nina G.; Hochgeschwender, Ute; Moore, Christopher I. published an article in 2020, the title of the article was The BioLuminescent-OptoGenetic in vivo response to coelenterazine is proportional, sensitive, and specific in neocortex.Reference of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one And the article contains the following content:

BioLuminescent (BL) light production can modulate neural activity and behavior through co-expressed OptoGenetic (OG) elements, an approach termed “BL-OG.” Yet, the relationship between BL-OG effects and bioluminescent photon emission has not been characterized in vivo. Further, the degree to which BL-OG effects strictly depend on optogenetic mechanisms driven by bioluminescent photons is unknown. Crucial to every neuromodulation method is whether the activator shows a dynamic concentration range driving robust, selective, and nontoxic effects. We systematically tested the effects of four key components of the BL-OG mechanism (luciferin, oxidized luciferin, luciferin vehicle, and bioluminescence), and compared these against effects induced by the Luminopsin-3 (LMO3) BL-OG mol., a fusion of slow burn Gaussia luciferase (sbGLuc) and Volvox ChannelRhodopsin-1 (VChR1). We performed combined bioluminescence imaging and electrophysiol. recordings while injecting specific doses of Coelenterazine (substrate for sbGluc), Coelenteramide (CTM, the oxidized product of CTZ), or CTZ vehicle. CTZ robustly drove activity in mice expressing LMO3, with photon production proportional to firing rate. In contrast, low and moderate doses of CTZ, CTM, or vehicle did not modulate activity in mice that did not express LMO3. We also failed to find bioluminescence effects on neural activity in mice expressing an optogenetically nonsensitive LMO3 variant. We observed weak responses to the highest dose of CTZ in control mice, but these effects were significantly smaller than those observed in the LMO3 group. These results show that in neocortex in vivo, there is a large CTZ range wherein BL-OG effects are specific to its active chemogenetic mechanism. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Reference of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to coelenterazine neocortex bioluminescent optogenetic response, bl-og, bioluminescence, chemogenetic, coelenterazine, injection, noninvasive, optogenetic, bioluminescence, cerebral neocortex and other aspects.Reference of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Krasitskaya, Vasilisa V.; Bashmakova, Eugenia E.; Frank, Ludmila A. published an article in 2020, the title of the article was Coelenterazine-dependent luciferases as a powerful analytical tool for research and biomedical applications.Electric Literature of 55779-48-1 And the article contains the following content:

A review. 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. Despite the diversity in structures and the functioning mechanisms, these enzymes can be united into a common group called CTZ-dependent luciferases. Among these, there are two sharply different types of the system organization-Ca2+-regulated photoproteins and luciferases themselves that function in accordance with the classical enzyme-substrate kinetics. Along with deep and comprehensive fundamental research on these systems, approaches and methods of their practical use as highly sensitive reporters in analytics have been developed. The research aiming at the creation of artificial luciferases and synthetic CTZ analogs with new unique properties has led to the development of new exptl. anal. methods based on them. The com. availability of many ready-to-use assay systems based on CTZ-dependent luciferases is also important when choosing them by first-time-users. The development of anal. methods based on these bioluminescent systems is currently booming. The bioluminescent systems under consideration were successfully applied in various biol. research areas, which confirms them to be a powerful anal. tool. In this , we consider the main directions, results, and achievements in research involving these luciferases. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Electric Literature of 55779-48-1

The Article related to review coelenterazine luciferase bioluminescent system, ca2+-regulated photoprotein, analytical systems, bioluminescence, coelenterazine, luciferase, Pharmaceuticals: Reviews and other aspects.Electric Literature of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On July 31, 2019, Weihs, Felix; Dacres, Helen published an article.Electric Literature of 55779-48-1 The title of the article was Red-shifted bioluminescence Resonance Energy Transfer: Improved tools and materials for analytical in vivo approaches. And the article contained the following:

A review. Bioluminescence Resonance Energy Transfer (BRET) has been proven as a highly sensitive optical transduction system for bio-imaging and a variety of anal. approaches. Its use for quant. imaging of physiol. changes in vivo or in vitro of blood samples has been hindered due to signal attenuation of the blue/green light-emitting bioluminescence agents. The field of luciferase-luciferin pairs as well as energy accepting mols. such as fluorescent proteins, organic dyes and quantum dots is rapidly growing. In the present article, progress in the development of red-shifted BRET components that are less affected by light-attenuation and scattering are analyzed. Recently developed NanoLuc variants, Firefly luciferases and luciferin analogs greatly expand options for efficient red-shifted BRET systems. These luciferases in combination with new large Stokes-shifted fluorophores allow quant. imaging in deep-tissues of living subjects. In addition, we point towards yet untested BRET strategies to assist those developing new anal. techniques and BRET tools. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Electric Literature of 55779-48-1

The Article related to review blood bret system red shifted emission spectrum, Biochemical Methods: Reviews and other aspects.Electric Literature of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Ennis, Michael D. published an article in 2012, the title of the article was Oxalyl bromide.Name: 3,5-Dibromo-1-methylpyrazin-2(1H)-one And the article contains the following content:

Synthesis, properties, availability, handling and applications of oxalyl bromide as a reactive acid halide and in heterocycle synthesis was reviewed. The experimental process involved the reaction of 3,5-Dibromo-1-methylpyrazin-2(1H)-one(cas: 87486-34-8).Name: 3,5-Dibromo-1-methylpyrazin-2(1H)-one

The Article related to review oxalyl bromide bromination heterocycle preparation safety, Aliphatic Compounds: Reviews and other aspects.Name: 3,5-Dibromo-1-methylpyrazin-2(1H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On August 20, 2020, Love, Anna C.; Prescher, Jennifer A. published an article.SDS of cas: 55779-48-1 The title of the article was Seeing (and Using) the Light: Recent Developments in Bioluminescence Technology. And the article contained the following:

A review. Bioluminescence has long been used to image biol. processes in vivo. This technol. features luciferase enzymes and luciferin small mols. that produce visible light. Bioluminescent photons can be detected in tissues and live organisms, enabling sensitive and noninvasive readouts on physiol. function. Traditional applications have focused on tracking cells and gene expression patterns, but new probes are pushing the frontiers of what can be visualized. The past few years have also seen the merger of bioluminescence with optogenetic platforms. Luciferase-luciferin reactions can drive light-activatable proteins, ultimately triggering signal transduction and other downstream events. This review highlights these and other recent advances in bioluminescence technol., with an emphasis on tool development. We showcase how new luciferins and engineered luciferases are expanding the scope of optical imaging. We also highlight how bioluminescent systems are being leveraged not just for sensing-but also controlling-biol. processes. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).SDS of cas: 55779-48-1

The Article related to review luciferase luciferin bioluminescence optical imaging, bioluminescence, imaging, luciferase, luciferin, optogenetics, Biochemical Methods: Reviews and other aspects.SDS of cas: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Kim, Sung-Bae; Fujii, Rika published an article in 2021, the title of the article was A New Lineage of Artificial Luciferases for Mammalian Cell Imaging.Quality Control of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one And the article contains the following content:

A review. The present protocol introduces a new lineage of artificial luciferases (ALucs) with unique optical properties for mammalian cell imaging. The primary candidate sequence was first created with a sequence logo generator, resulting in a total of 11 sibling sequences by extracting consensus amino acids from the alignment of 25 copepod luciferase sequences available in natural luciferase pools in public databases. Phylogenetic anal. shows that the newly fabricated ALucs form an independent branch, genetically isolated from the natural luciferases and from a prior series of ALucs produced by our laboratory using a smaller basis set. The protocol also exemplifies that the new lineage of ALucs was strongly luminescent in living mammalian cells with specific substrate selectivity to native coelenterazine. The success of this approach guides on how to engineer and functionalize marine luciferases for bioluminescence imaging and assays. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Quality Control of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to review artificial luciferase mammalian cell imaging lineage, artificial luciferase, bioluminescence, coelenterazine, copepod luciferase, frequency analysis, Biochemical Methods: Reviews and other aspects.Quality Control of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem