Month: November 2022

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

Referemce:
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

Vicente, Manuel; Salgado-Almario, Jussep; Collins, Michelle M.; Martinez-Sielva, Antonio; Minoshima, Masafumi; Kikuchi, Kazuya; Domingo, Beatriz; Llopis, Juan published an article in 2021, the title of the article was Cardioluminescence in Transgenic Zebrafish Larvae: A Calcium Imaging Tool to Study Drug Effects and Pathological Modeling.Synthetic Route of 55779-48-1 And the article contains the following content:

Zebrafish embryos and larvae have emerged as an excellent model in cardiovascular research and are amenable to live imaging with genetically encoded biosensors to study cardiac cell behaviors, including calcium dynamics. To monitor calcium ion levels in three to five days post-fertilization larvae, we have used bioluminescence. We generated a transgenic line expressing GFP-aequorin in the heart, Tg(myl7:GA), and optimized a reconstitution protocol to boost aequorin luminescence. The analog diacetylh-coelenterazine enhanced light output and signal-to-noise ratio. With this cardioluminescence model, we imaged the time-averaged calcium levels and beat-to-beat calcium oscillations continuously for hours. As a proof-of-concept of the transgenic line, changes in ventricular calcium levels were observed by Bay K8644, an L-type calcium channel activator and with the blocker nifedipine. The β-adrenergic blocker propranolol decreased calcium levels, heart rate, stroke volume, and cardiac output, suggesting that larvae have a basal adrenergic tone. Zebrafish larvae treated with terfenadine for 24 h have been proposed as a model of heart failure. Tg(myl7:GA) larvae treated with terfenadine showed bradycardia, 2:1 atrioventricular block, decreased time-averaged ventricular calcium levels but increased calcium transient amplitude, and reduced cardiac output. As alterations of calcium signalling are involved in the pathogenesis of heart failure and arrhythmia, the GFP-aequorin transgenic line provides a powerful platform for understanding calcium dynamics. 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 zebrafish calcium aequorin coelenterazine heart failure imaging, aequorin, calcium, coelenterazine, heart, heart failure, imaging, zebrafish, Nonmammalian Biochemistry: Classical Genetics and Phylogeny and other aspects.Synthetic Route of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Larionova, Marina D.; Markova, Svetlana V.; Tikunova, Nina V.; Vysotski, Eugene S. published an article in 2020, the title of the article was The smallest isoform of Metridia longa luciferase as a fusion partner for hybrid proteins.Electric Literature of 55779-48-1 And the article contains the following content:

Bioluminescent proteins are widely used as reporter mols. in various in vitro and in vivo assays. The smallest isoform of Metridia luciferase (MLuc7) is a highly active, naturally secreted enzyme which, along with other luciferase isoforms, is responsible for the bright bioluminescence of marine copepod Metridia longa. In this study, we report the construction of two variants of a hybrid protein consisting of MLuc7 and 14D5a single-chain antibody to the surface glycoprotein E of tick-borne encephalitis virus as a model fusion partner. We demonstrate that, whereas fusion of a single-chain antibody to either N- or C-terminus of MLuc7 does not affect its bioluminescence properties, the binding site on the single-chain antibody influences its binding capacity. The affinity of 14D5a-MLuc7 hybrid protein (KD = 36.2 nM) where the C-terminus of the single-chain antibody was fused to the N-terminus of MLuc7, appeared to be 2.5-fold higher than that of the reverse, MLuc7-14D5a (KD = 87.6 nM). The detection limit of 14D5a-MLuc7 hybrid protein was estimated to be 45 pg of the recombinant glycoprotein E. Although the smallest isoform of M. longa luciferase was tested as a fusion partner only with a single-chain antibody, it is reasonable to suppose that MLuc7 can also be successfully used as a partner for genetic fusion with other proteins. 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 metridia longa luciferase fusion hybrid protein, bioluminescence, coelenterazine, copepod luciferase, immunoassay, single-chain antibody, tick-borne encephalitis virus, Nonmammalian Biochemistry: Classical Genetics and Phylogeny and other aspects.Electric Literature of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On January 2, 2014, Do, Steven; Hu, Huiyong; Kolesnikov, Aleksandr; Tsui, Vickie H.; Wang, Xiaojing published a patent.SDS of cas: 87486-34-8 The title of the patent was 5-Azaindazole compounds as Pim kinase inhibitors and their preparation. And the patent contained the following:

5-Azaindazole compounds of formula I, including stereoisomers, geometric isomers, tautomers, and pharmaceutically acceptable salts thereof, are useful for inhibiting Pim kinase, and for treating disorders such as cancer mediated by Pim kinase. Compounds of formula I wherein R1 is (un)substituted 5- to 6-membered heteroaryl; R2 is (un)substituted Ph and (un)substituted 6-membered heteroaryl; and stereoisomers, geometric isomers, tautomers, and pharmaceutically acceptable salts thereof, are claimed. Example compound II was prepared by a multistep procedure (procedure given). The invention compounds were evaluated for their Pim kinase inhibitory activity (data given). The experimental process involved the reaction of 3,5-Dibromo-1-methylpyrazin-2(1H)-one(cas: 87486-34-8).SDS of cas: 87486-34-8

The Article related to azaindazole preparation pim kinase inhibitors, Heterocyclic Compounds (More Than One Hetero Atom): Pyrazoles and other aspects.SDS of cas: 87486-34-8

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On December 31, 2020, Rodriguez-Rodriguez, Ismael; Kalafut, Joanna; Czerwonka, Arkadiusz; Rivero-Muller, Adolfo 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 A novel bioassay for quantification of surface Cannabinoid receptor 1 expression. And the article contained the following:

The cannabinoid receptor type 1 (CB1) plays critical roles in multiple physiol. processes such as pain perception, brain development and body temperature regulation. Mutations on this gene (CNR1), results in altered functionality and/or biosynthesis such as reduced membrane expression, changes in mRNA stability or changes in downstream signaling that act as triggers for diseases such as obesity, Parkinson, Huntington, among others; thus, it is considered as a potential pharmacol. target. To date, multiple quantification methods have been employed to determine how these mutations affect receptor expression and localization; however, they present serious disadvantages that may arise quantifying errors. Here, we describe a sensitive bioassay to quantify receptor surface expression; in this bioassay the Gaussia Luciferase (GLuc) was fused to the extracellular portion of the CB1. The GLuc activity was assessed by coelenterazine addition to the medium followed by immediate readout. Based on GLuc activity assay, we show that the GLuc signals corelate with CB1 localization, besides, we showed the assay functionality and reliability by comparing its results with those generated by previously reported mutations on the CNR1 gene and by using flow cytometry to determine the cell surface receptor expression. Detection of membrane-bound CB1, and potentially other GPCRs, is able to quickly screen for receptor levels and help to understand the effect of clin. relevant mutations or polymorphisms. 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 cnr1 surface receptor luciferase mutation bioassay, Biochemical Methods: Other (Not Covered At Other Subsections) 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

On November 19, 2009, Crew, Andrew P.; Jin, Meizhong; Kadalbajoo, Mridula; Kleinberg, Andrew; Mulvihill, Mark J.; Wang, Jing published a patent.Name: 3-(8-Chloroimidazo[1,5-a]pyrazin-3-yl)cyclobutanone The title of the patent was Substituted imidazopyrazines and imidazotriazines as ACK1 inhibitors and their preparation. And the patent contained the following:

The invention relates to fused pyridine-based bicyclic compounds having the structure of formula I, pharmaceutically acceptable salts thereof, preparation, compositions, and disease treatment therewith. Compounds of formula I wherein A is CH and N; Q1 is X1Y1Z1, 1-phenylbenzimidazol-5-yl and carbazolyl; X1 is (un)substituted 5- to 10-membered cyclic ring; Y is CO, O, S, SO, SO2, etc.; Z1 is (un)substituted 5- to 10-membered cyclic ring and C1-6 alkoxy; R1 is SH and derivatives, (un)substituted C1-6 alkyl, (un)substituted 5,6-bicyclic aryl and (un)substituted 3- to 6-membered ring; and pharmaceutically acceptable salt thereof, are claimed. Example compound II was prepared by a general procedure (procedure given). All the invention compounds were evaluated for their ACK1 inhibitory activity. From the assay, it was determined that compound II exhibited IC50 value of 0.1759 μM. The experimental process involved the reaction of 3-(8-Chloroimidazo[1,5-a]pyrazin-3-yl)cyclobutanone(cas: 936901-72-3).Name: 3-(8-Chloroimidazo[1,5-a]pyrazin-3-yl)cyclobutanone

The Article related to imidazopyrazine imidazotriazine preparation ack1 inhibitor, Heterocyclic Compounds (More Than One Hetero Atom): Triazines and other aspects.Name: 3-(8-Chloroimidazo[1,5-a]pyrazin-3-yl)cyclobutanone

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On November 30, 2020, Krasitskaya, V. V.; Bashmakova, E. E.; Kudryavtsev, A. N.; Vorobjeva, M. A.; Shatunova, E. A.; Frank, L. A. published an article.Category: pyrazines The title of the article was The Hybrid Protein ZZ-OL as an Analytical Tool for Biotechnology Research. And the article contained the following:

Abstract: The gene of the hybrid protein that encodes the double synthetic fragment proZZ of the Ig-binding domain of protein A of Staphylococcus aureus and apo-obelin joined by a short linker has been cloned. The corresponding hybrid protein has been obtained by expression in Escherichia coli cells. The protein activated with a substrate (coelenterazine) possesses the bioluminescent Ca2+-dependent activity of the photoprotein close to that of recombinant wild-type obelin, and the Ig-binding ability of protein A. It has been shown that the hybrid can be used as a highly sensitive label to detect antibodies and estimate their affinity and interaction with recombinant proteins, as well as in investigations of other kinds. 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 staphylococcus escherichia hybrid protein zz ol biotechnol research, Biochemical Methods: Other (Not Covered At Other Subsections) and other aspects.Category: pyrazines

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem