Category: 55779-48-1

On December 31, 2020, Galaway, Francis; Wright, Gavin J. published an article.Related Products of 55779-48-1 The title of the article was Rapid and sensitive large-scale screening of low affinity extracellular receptor protein interactions by using reaction induced inhibition of Gaussia luciferase. And the article contained the following:

Extracellular protein interactions mediated by cell surface receptors are essential for intercellular communication in multicellular organisms. Assays to detect extracellular interactions must account for their often weak binding affinities and also the biochem. challenges in solubilizing membrane-embedded receptors in an active form. Methods based on detecting direct binding of soluble recombinant receptor ectodomains have been successful, but genome-scale screening is limited by the usual requirement of producing sufficient amounts of each protein in two different forms, usually a “bait” and “prey”. Here, we show that oligomeric receptor ectodomains coupled to concatenated units of the light-generating Gaussia luciferase enzyme robustly detected low affinity interactions and reduced the amount of protein required by several orders of magnitude compared to other reporter enzymes. Importantly, we discovered that this flash-type luciferase exhibited a reaction-induced inhibition that permitted the use of a single protein preparation as both bait and prey thereby halving the number of expression plasmids and recombinant proteins required for screening. This approach was tested against a benchmarked set of quantified extracellular interactions and shown to detect extremely weak interactions (KDs ≥ μM). This method will facilitate large-scale receptor interaction screening and contribute to the goal of mapping networks of cellular communication. 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).Related Products of 55779-48-1

The Article related to modified avexis low affinity ectodomain interaction luminescent screening, Biochemical Methods: Spectral and Related Methods and other aspects.Related Products of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Silva, Jose Pedro; Gonzalez-Berdullas, Patricia; Esteves da Silva, Joaquim C. G.; Pinto da Silva, Luis published an article in 2022, the title of the article was Development of a Coelenterazine Derivative with Enhanced Superoxide Anion-Triggered Chemiluminescence in Aqueous Solution.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:

Superoxide anion is a reactive oxygen species (ROS) of biol. interest. More specifically, it plays a role in intra- and intercellular signaling, besides being associated with conditions such as inflammation and cancer. Given this, efforts have been made by the research community to devise new sensing strategies for this ROS species. Among them, the chemiluminescent reaction of marine Coelenterazine has been employed as a sensitive and dynamic probing approach. Nevertheless, chemiluminescent reactions are typically associated with lower emissions in aqueous solutions Herein, here we report the synthesis of a new Coelenterazine derivative with the potential for superoxide anion sensing. Namely, this novel compound is capable of chemiluminescence in a dose-dependent manner when triggered by this ROS species. More importantly, the light-emission intensities provided by this derivative were relevantly enhanced (intensities 2.13 x 101 to 1.11 x 104 times higher) in aqueous solutions at different pH conditions when compared to native Coelenterazine. The half-life of the chemiluminescent signal is also greatly increased for the derivative Thus, a new chemiluminescence mol. with significant potential for superoxide anion sensing was discovered and reported for the first time. 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 chemiluminescence coelenterazine imidazopyrazinone derivative ros indicator, Biochemical Methods: Spectral and Related Methods and other aspects.Reference of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

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Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On August 31, 2021, Crespo, Emmanuel L.; Bjorefeldt, Andreas; Prakash, Mansi; Hochgeschwender, Ute published an article.Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one The title of the article was Bioluminescent optogenetics 2.0: harnessing bioluminescence to activate photosensory proteins in vitro and in vivo. And the article contained the following:

Bioluminescence – light emitted by a luciferase enzyme oxidizing a small mol. substrate, a luciferin – has been used in vitro and in vivo to activate light-gated ion channels and pumps in neurons. While this bioluminescent optogenetics (BL-OG) approach confers a chemogenetic component to optogenetic tools, it is not limited to use in neuroscience. Rather, bioluminescence can be harnessed to activate any photosensory protein, thus enabling the manipulation of a multitude of light-mediated functions in cells. A variety of luciferase-luciferin pairs can be matched with photosensory proteins requiring different wavelengths of light and light intensities. Depending on the specific application, efficient light delivery can be achieved by using luciferase-photoreceptor fusion proteins or by simple co-transfection. Photosensory proteins based on light-dependent dimerization or conformational changes can be driven by bioluminescence to effect cellular processes from protein localization, regulation of intracellular signaling pathways to transcription. The protocol below details the exptl. execution of bioluminescence activation in cells and organisms and describes the results using bioluminescence-driven recombinases and transcription factors. The protocol provides investigators with the basic procedures for carrying out bioluminescent optogenetics in vitro and in vivo. The described approaches can be further extended and individualized to a multitude of different exptl. paradigms. 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).Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

The Article related to bioluminescent optogenetics harnessing bioluminescence photosensory protein, Biochemical Methods: Spectral and Related Methods and other aspects.Safety of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one

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Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Yu, Xiaowen; Scott, Daniel; Dikici, Emre; Joel, Smita; Deo, Sapna; Daunert, Sylvia published an article in 2019, the title of the article was Multiplexing cytokine analysis: towards reducing sample volume needs in clinical diagnostics.Formula: C26H21N3O3 And the article contains the following content:

The trend for improved more precise diagnostics and management of disease heavily relies on the measurement of panels of biomarkers in physiol. samples of patients. Ideally, the ultimate goal would be to detect as many clin. relevant biomarkers as possible in a single drop of blood, achieving quick, sensitive, reproducible, and affordable detection in small volume physiol. samples. Bioluminescent (BL) proteins provide many of the desired characteristics required for such labels, including detection at extremely low concentrations, no interference from physiol. fluids leading to excellent detection limits, and compatibility with many miniaturized systems. However, to date the use of BL proteins has been restricted by their limited multiplexing capabilities. BL proteins typically exhibit a single emission profile and decay kinetics making the simultaneous detection of multiple analytes difficult. Recent progresses in this area include the use of two different engineered luminescent proteins to achieve resolved signals via one-dimensional time resolution This approach, however, to date only lead to a dual analyte detection. Herein, we have demonstrated that using a two-dimensional approach that combines both temporal and spatial resolution, we can expand the multiplexing capabilities of bioluminescent proteins. To that end, the photoprotein aequorin (AEQ) has been employed for the simultaneous detection of three sep. analytes in a single well, differentiated through the use of three discrete time/wavelength windows. Through a combination of site-specific mutations and synthetic coelenterazines “semi-synthetic” AEQ variants have been developed with altered emission profiles and decay kinetics. In this study, two AEQ mutant proteins were genetically conjugated to three pro-inflammatory cytokines (tumor necrosis factor alpha, interleukins 6 and 8) resulting in AEQ-labeled cytokines. These fusion proteins were combined with synthetic coelenterazines resulting in proteins with differing emission maxima and half-lives to allow for the simultaneous detection of all three cytokines in a single sample. The validity of the assay was demonstrated in serum by employing human physiol. samples and comparing our results with com. available individual tests for each of the three cytokines. 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).Formula: C26H21N3O3

The Article related to aequorin cytokine fusion protein coelenterazine blood analysis interleukin tnfalpha, Biochemical Methods: Spectral and Related Methods and other aspects.Formula: C26H21N3O3

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Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On August 28, 2020, Ruffinatti, Federico Alessandro; Lomazzi, Samuela; Nardo, Luca; Santoro, Romualdo; Martemiyanov, Alexander; Dionisi, Marianna; Tapella, Laura; Genazzani, Armando A.; Lim, Dmitry; Distasi, Carla; Caccia, Massimo published an article.Synthetic Route of 55779-48-1 The title of the article was Assessment of a Silicon-Photomultiplier-Based Platform for the Measurement of Intracellular Calcium Dynamics with Targeted Aequorin. And the article contained the following:

Ca2+ is among the most important intracellular second messengers participating in a plethora of biol. processes, and the measurement of Ca2+ fluctuations is significant in the phenomenol. of the underlying processes. Aequorin-based Ca2+ probes represent an invaluable tool for reliable measurement of Ca2+ concentrations and dynamics in different subcellular compartments. However, their use is limited due to the lack on the market of ready-to-use, cost-effective, and portable devices for the detection and readout of the low-intensity bioluminescence signal produced by these probes. Silicon photomultipliers (SiPMs) are rapidly evolving solid-state sensors for low light detection, with single photon sensitivity and photon number resolving capability, featuring low cost, low voltage, and compact format. Thus, they may represent the sensors of choice for the development of such devices and, more in general, of a new generation of multipurpose bioluminescence detectors suitable for cell biol. studies. Ideally, a detector customized for these purposes must combine high dynamic range with high fidelity in reconstructing the light intensity signal temporal profile. The ability to perform aequorin-based intracellular Ca2+ measurements using a multipurpose, low-cost setup exploiting SiPMs as the sensors is demonstrated. SiPMs turn out to assure performances comparable to those exhibited by a custom-designed photomultiplier tube-based aequorinometer. Moreover, the flexibility of SiPM-based devices might pave the way toward routinely and wide scale application of innovative biophys. protocols. 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).Synthetic Route of 55779-48-1

The Article related to silicon photomultiplier calcium dynamics aequorin, aequorin, bioluminescence, calcium signaling, live cell, silicon photomultipliers, Biochemical Methods: Spectral and Related Methods and other aspects.Synthetic Route of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On February 15, 2020, Hosseinnia, Maryam; Khalifeh, Khosrow; Jafarian, Vahab published an article.Synthetic Route of 55779-48-1 The title of the article was Polarity change of a representative helix in coelenterazin-binding cavity of mnemiopsin 2: Functional and structural consequences. And the article contained the following:

To evaluate the effect of a pos. charged residue at the end of the fourth helix on the function and stability of the folded state of mnemiopsin 2, Lys89 was replaced with Ala (K89A mutant). Its structural and functional features were investigated and compared with Wild type (WT) protein using a combination of theor. and exptl. procedures. The tertiary structures of WT and mutant photoproteins were made with MODELLER program, and were used for designing of mutation as well as explaining the results of exptl. measurements. Activity measurements showed that the initial intensity of light emission is reduced, but decay time is not changed upon mutation. K89A mutant exhibited more sensitivity to calcium ion than WT protein did. As compared to the pH 9 of WT, the optimum pH for the mutant increased to 9.25. According to the CD measurements at far UV region, the total amount of helical structure is not changed upon mutation; however, the helicity of chromophores is reduced in K89A mutant, demonstrating that the secondary structural elements in WT protein are more rigid. Heat-induced denaturation data showed that the stability of the WT is greater than mutant photoprotein by 2 kcal/mol. It appears that the higher value of the dipole momentum at the axis of fourth helix in WT photoprotein leads to strengthening of intra-mol. “head-to-tail” vs. “side-by-side” anti-parallel interaction between the third and fourth helixes. It was concluded that dipole-dipole interaction between the helixes are important factors in packaging of the substrate in the core structure of the photoprotein. 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).Synthetic Route of 55779-48-1

The Article related to mnemiopsin 2 coelenterazin bioluminescence thermostability dipole, General Biochemistry: Proteins and Their Constituents and other aspects.Synthetic Route of 55779-48-1

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Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On September 30, 2020, Gunter, Julia; Wenger, Roland H.; Scholz, Carsten C. published an article.Recommanded Product: 55779-48-1 The title of the article was Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor. And the article contained the following:

The three hypoxia-inducible factor (HIF) prolyl-4-hydroxylase domain (PHD) 1-3 enzymes confer oxygen sensitivity to the HIF pathway and are novel therapeutic targets for treatment of renal anemia. Inhibition of the PHDs may further be beneficial in other hypoxia-associated diseases, including ischemia and chronic inflammation. Several pharmacol. PHD inhibitors (PHIs) are available, but our understanding of their selectivity and its chem. basis is limited. We here report that the PHI JNJ-42041935 (JNJ-1935) is structurally similar to the firefly luciferase substrate D-luciferin. Our results demonstrate that JNJ-1935 is a novel inhibitor of firefly luciferase enzymic activity. In contrast, the PHIs FG-4592 (roxadustat) and FG-2216 (ICA, BIQ, IOX3, YM 311) did not affect firefly luciferase. The JNJ-1935 mode of inhibition is competitive with a Ki of 1.36μM. D-luciferin did not inhibit the PHDs, despite its structural similarity to JNJ-1935. This study provides insights into a previously unknown JNJ-1935 off-target effect as well as into the chem. requirements for firefly luciferase and PHD inhibitors and may inform the development of novel compounds targeting these enzymes. 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).Recommanded Product: 55779-48-1

The Article related to jnj1935 luciferase prolyl 4 hydroxylase domain inhibitor d luciferin, 2-oxoglutarate, dioxygenase, epigenetics, erythropoietin, hypoxia, kidney disease, Pharmacology: Drug Interactions and General Pharmacology and other aspects.Recommanded Product: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On December 31, 2021, Kanie, Shusei; Miura, Daisuke; Jimi, Naoto; Hayashi, Taro; Nakamura, Koji; Sakata, Masahiko; Ogoh, Katsunori; Ohmiya, Yoshihiro; Mitani, Yasuo published an article.Synthetic Route of 55779-48-1 The title of the article was Violet bioluminescent Polycirrus sp. (Annelida: Terebelliformia) discovered in shallow coastal waters of Noto Peninsula in Japan. And the article contained the following:

Terebellidae worms have large numbers of tentacles responsible for various biol. functions. Some Terebellidae worms whose tentacles emit light are found around the world, including exceptional violet-light-emitting Polycirrus spp. found in Europe and North America. However, there is no video-recorded observation of the luminous behavior of such unique species in nature, and the genetic information related to their ecol. are lacking. Here, for the first time, we video-recorded the violet-light-emitting behavior of an undescribed Japanese worm in its natural habitat. The worm was designated as Polycirrus sp. ISK based on morphol. observations, and the luminescence spectrum showed a peak at 444 nm, which is an exceptionally short wavelength for bioluminescence in a shallow coastal water environment. An anal. of differentially expressing genes based on sep. RNA-Seq anal. for the tentacles and the rest of body revealed the specific expression of genes that are probably involved in innate immunity in the tentacles exposed to predators. We also found a Renilla luciferase homologous gene, but coelenterazine was not detected in the worm extract by analyses using a liquid chromatog. and a recombinant Renilla luciferase. These results will promote an understanding of the ecol. and luminescence mechanisms of luminous Polycirrus spp. 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).Synthetic Route of 55779-48-1

The Article related to violet bioluminescence terebelliformia shallow coastal water, Nonmammalian Biochemistry: Classical Genetics and Phylogeny and other aspects.Synthetic Route of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On December 31, 2020, Tessler, Michael; Gaffney, Jean P.; Oliveira, Anderson G.; Guarnaccia, Andrew; Dobi, Krista C.; Gujarati, Nehaben A.; Galbraith, Moira; Mirza, Jeremy D.; Sparks, John S.; Pieribone, Vincent A.; Wood, Robert J.; Gruber, David F. published an article.Related Products of 55779-48-1 The title of the article was A putative chordate luciferase from a cosmopolitan tunicate indicates convergent bioluminescence evolution across phyla. And the article contained the following:

Pyrosomes are tunicates in the phylum Chordata, which also contains vertebrates. Their gigantic blooms play important ecol. and biogeochem. roles in oceans. Pyrosoma, meaning “fire-body”, derives from their brilliant bioluminescence. The biochem. of this light production is unknown, but has been hypothesized to be bacterial in origin. We found that mixing coelenterazine-a eukaryote-specific luciferin-with Pyrosoma atlanticum homogenate produced light. To identify the bioluminescent machinery, we sequenced P. atlanticum transcriptomes and found a sequence match to a cnidarian luciferase (RLuc). We expressed this novel luciferase (PyroLuc) and, combined with coelenterazine, it produced light. A similar gene was recently predicted from a bioluminescent brittle star, indicating that RLuc-like luciferases may have evolved convergently from homologous dehalogenases across phyla (Cnidaria, Echinodermata, and Chordata). This report indicates that a widespread gene may be able to functionally converge, resulting in bioluminescence across animal phyla, and describes and characterizes the first putative chordate luciferase. 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).Related Products of 55779-48-1

The Article related to pyrosoma atlanticum vertebrates transcriptomes bioluminescence bacteria, Nonmammalian Biochemistry: Classical Genetics and Phylogeny and other aspects.Related Products of 55779-48-1

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Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On August 31, 2020, Bessho-Uehara, Manabu; Francis, Warren R.; Haddock, Steven H. D. published an article.Related Products of 55779-48-1 The title of the article was Biochemical characterization of diverse deep-sea anthozoan bioluminescence systems. And the article contained the following:

Abstract: Bioluminescence, light produced by living organisms, is a common trait in the ocean. In benthic ecosystems in the deep-sea, octocorals are some of the most abundant luminous animals. Among luminous sessile organisms, the shallow-water sea pansy Renilla has been well studied for its chem. and mol. biol. Aside from Renilla, however, little is known about the bioluminescent mechanisms of other anthozoans, especially deep-sea corals. In this study, we investigated the characteristics of bioluminescence in deep-sea anthozoans. The bioluminescent capabilities of Heteropolypus, Kophobelemnon, Paragorgia, and a hormathiid anemone are newly described. Coelenterazine, a substrate for bioluminescent reactions, was detected in extracts from octocorals. Coelenterazine-dependent luciferase activity was found in all the anthozoans. Moreover, immunoreactivity against Renilla luciferase was detected in protein extracts from the families Isididae, Alcyoniidae, Umbellulidae, Funiculinidae, Kophobelemnidae and Protoptilidae, suggesting that all luminous octocorals may share a common biochem. mechanism, which utilizes coelenterazine and Renilla-type luciferase. Our results support the hypothesis that the last common ancestor of all the octocorals was bioluminescent, and that bioluminescence evolved a min. of six times in Cnidaria. Our study provides fundamental observations of deep-sea corals and exptl. evidence of their coelenterazine-dependent luciferase systems. 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).Related Products of 55779-48-1

The Article related to renilla heteropolypus kophobelemnon paragorgia anthozoan bioluminescence biochemisty, Nonmammalian Biochemistry: Classical Genetics and Phylogeny and other aspects.Related Products of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem