Author: Jessica.F

Kanie, Shusei; Komatsu, Mami; Mitani, Yasuo published an article in 2020, the title of the article was Luminescence of Cypridina luciferin in the presence of human plasma alpha 1-acid glycoprotein.Computed Properties of 55779-48-1 And the article contains the following content:

The enzyme Cypridina luciferase (CLase) enables Cypridina luciferin to emit light efficiently through an oxidation reaction. The catalytic mechanism on the substrate of CLase has been studied, but the details remain to be clarified. Here, we examined the luminescence of Cypridina luciferin in the presence of several proteins with drug-binding ability. Luminescence measurements showed that the mixture of human plasma alpha 1-acid glycoprotein (hAGP) and Cypridina luciferin produced light. The total value of the luminescence intensity over 60 s was over 12.6-fold higher than those in the presence of ovalbumin, human serum albumin, or bovine serum albumin. In the presence of heat-treated hAGP, the luminescence intensity of Cypridina luciferin was lower than in the presence of intact hAGP. Chlorpromazine, which binds to hAGP, showed an inhibitory effect on the luminescence of Cypridina luciferin, both in the presence of hAGP and a recombinant CLase. Furthermore, BlastP anal. showed that hAGP had partial amino acid sequence similarity to known CLases in the region including amino acid residues involved in the drug-binding ability of hAGP. These findings indicate enzymol. similarity between hAGP and CLase and provide insights into both the enzymol. understanding of CLase and development of a luminescence detection method for hAGP. 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).Computed Properties of 55779-48-1

The Article related to cypridina luciferin plasma alpha 1 acid glycoprotein luminescence, cypridina luciferase, cypridina luciferin, bioluminescence, cypridinid luciferase, cypridinid luciferin, human plasma alpha 1-aicd glycoprotein and other aspects.Computed Properties of 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On March 8, 2012, Currie, Kevin S.; Wang, Xiaojing; Young, Wendy B. published a patent.Product Details of 87486-34-8 The title of the patent was Preparation of pyridinones and pyrazinones as Btk kinase inhibitors for treating inflammation, immunological disorders, cancer, and other diseases. And the patent contained the following:

Pyridinone and pyrazinone compounds of Formula I (wherein R1 is substituted isoindolinone, thienopyrrolone, or pyrrolothiazolone; R2 is H, Me, or CF3; ring B is ring B is Ph, 5-6 membered heteroaryl, or 8-11 membered heterocyclyl; R3 is H, halo, cyano, etc.; R6 is H, Me, F, etc.; R7 is H, Me F, etc.; R8 is H, Me, CF3, etc.; V is CH or N) including stereoisomers, tautomers, and pharmaceutically acceptable salts thereof, useful for inhibiting Btk kinase, and for treating immune disorders such as inflammation mediated by Btk kinase are claimed. Methods of using compounds of Formula I for in vitro, in situ, and in vivo diagnosis, and treatment of such disorders in mammalian cells, or associated pathol. conditions, are disclosed. Synthetic procedures for preparing I are exemplified. Example compound II, prepared in a multistep synthesis that culminated in the cyclization of III, had an IC50 of 0.0364 in a standard biochem. Btk kinase assay. The experimental process involved the reaction of 3,5-Dibromo-1-methylpyrazin-2(1H)-one(cas: 87486-34-8).Product Details of 87486-34-8

The Article related to preparation pyridinone pyrazinone btk kinase inhibitor therapy diagnosis, immune disorder treatment pyridinone pyrazinone btk kinase inhibitor, inflammation cancer treatment pyridinone pyrazinone btk kinase inhibitor and other aspects.Product Details of 87486-34-8

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On January 31, 2021, Connick, J. Patrick; Reed, James R.; Cawley, George F.; Backes, Wayne L. published an article.Formula: C26H21N3O3 The title of the article was Heteromeric complex formation between human cytochrome P450 CYP1A1 and heme oxygenase-1. And the article contained the following:

P 450 and heme oxygenase-1 (HO-1) receive their necessary electrons by interaction with the NADPH-cytochrome P 450 reductase (POR). As the POR concentration is limiting when compared with P 450 and HO-1, they must effectively compete for POR to function. In addition to these functionally required protein-protein interactions, HO-1 forms homomeric complexes, and several P450s have been shown to form complexes with themselves and with other P450s, raising the question, ‘How are the HO-1 and P 450 systems organized in the endoplasmic reticulum’. Recently, CYP1A2 was shown to associate with HO-1 affecting the function of both proteins. The goal of this study was to determine if CYP1A1 formed complexes with HO-1 in a similar manner. Complex formation among POR, HO-1, and CYP1A1 was measured using bioluminescence resonance energy transfer, with results showing HO-1 and CYP1A1 form a stable complex that was further stabilized in the presence of POR. The POR•CYP1A1 complex was readily disrupted by the addition of HO-1. CYP1A1 also was able to affect the POR•HO-1 complex, although the effect was smaller. This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KPOR•HO-1m without affecting the Vappmax. In like manner, HO-1 inhibited CYP1A1-mediated 7-ethoxyresorufin dealkylation by increasing the KPOR•CYP1A1m. Based on the math. simulation, the results could not be explained by a model where CYP1A1 and HO-1 simply compete for POR, and are consistent with the formation of a stable CYP1A1•HO-1 complex that affected the functional characteristics of both moieties. 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 heteromeric complex human cytochrome p450 cyp1a1 heme oxygenase, bioluminescence resonance energy transfer, cytochrome p450, heme oxygenase-1, membrane proteins, nadph-cytochrome p450 reductase, protein–protein interactions and other aspects.Formula: C26H21N3O3

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On June 12, 2019, Yeh, Hsien-Wei; Ai, Hui-Wang published an article.SDS of cas: 55779-48-1 The title of the article was Development and Applications of Bioluminescent and Chemiluminescent Reporters and Biosensors. And the article contained the following:

A review. Although fluorescent reporters and biosensors have become indispensable tools in biol. and biomedical fields, fluorescence measurements require external excitation light, thereby limiting their use in thick tissues and live animals. Bioluminescent reporters and biosensors may potentially overcome this hurdle because they use enzyme-catalyzed exothermic biochem. reactions to generate excited-state emitters. This review first introduces the development of bioluminescent reporters, and next, their applications in sensing biol. changes in vitro and in vivo as biosensors. Lastly, we discuss chemiluminescent sensors that produce photons in the absence of luciferases. This review aims to explore fundamentals and exptl. insights and to emphasize the yet-to-be-reached potential of next-generation luminescent reporters and biosensors. 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 bioluminescent chemiluminescent reporter biosensor, bret, bioluminescence, bioluminescence resonance energy transfer, chemiluminescence, fluorescence, genetically encoded biosensor, in vivo imaging, luciferase, luciferin and other aspects.SDS of cas: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On May 31, 2021, Hasgur, Suheyla; Desbourdes, Laura; Relation, Theresa; Overholt, Kathleen M.; Stanek, Joseph R.; Guess, Adam J.; Yu, Minjun; Patel, Pratik; Roback, Linda; Dominici, Massimo; Otsuru, Satoru; Horwitz, Edwin M. published an article.SDS of cas: 55779-48-1 The title of the article was Splenic macrophage phagocytosis of intravenously infused mesenchymal stromal cells attenuates tumor localization. And the article contained the following:

Mesenchymal stromal cells (MSCs) possess remarkable tumor tropism, making them ideal vehicles to deliver tumor-targeted therapeutic agents; however, their value in clin. medicine has yet to be realized. A barrier to clin. utilization is that only a small fraction of infused MSCs ultimately localize to the tumor. In an effort to overcome this obstacle, we sought to enhance MSC trafficking by focusing on the factors that govern MSC arrival within the tumor microenvironment. Our findings show that MSC chemoattraction is only present in select tumors, including osteosarcoma, and that the chemotactic potency among similar tumors varies substantially. Using an osteosarcoma xenograft model, we show that human MSCs traffic to the tumor within several hours of infusion. After arrival, MSCs are observed to localize in clusters near blood vessels and MSC-associated bioluminescence signal intensity is increased, suggesting that the seeded cells expand after engraftment. However, our studies reveal that a significant portion of MSCs are eliminated en route by splenic macrophage phagocytosis, effectively limiting the number of cells available for tumor engraftment. To increase MSC survival, we transiently depleted macrophages with liposomal clodronate, which resulted in increased tumor localization without substantial reduction in tumor-associated macrophages. Our data suggest that transient macrophage depletion will significantly increase the number of MSCs in the spleen and thus improve MSC localization within a tumor, theor. increasing the ED of an anti-cancer agent. This strategy may subsequently improve the clin. efficacy of MSCs as vehicles for the tumor-directed delivery of therapeutic agents. 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 mesenchymal stromal cell splenic macrophage phagocytosis tumor localization, cancer cell therapy, lentiviral transduction, mesenchymal stromal cells (mscs), phagocytosis, splenic macrophage, stem cell transplantation, tumor homing and other aspects.SDS of cas: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On September 23, 2022, Kim, Hyemin; Yeow, Jonathan; Najer, Adrian; Kit-Anan, Worrapong; Wang, Richard; Rifaie-Graham, Omar; Thanapongpibul, Chalaisorn; Stevens, Molly M. published an article.HPLC of Formula: 55779-48-1 The title of the article was Microliter Scale Synthesis of Luciferase-Encapsulated Polymersomes as Artificial Organelles for Optogenetic Modulation of Cardiomyocyte Beating. And the article contained the following:

Constructing artificial systems that effectively replace or supplement natural biol. machinery within cells is one of the fundamental challenges underpinning bioengineering. At the sub-cellular scale, artificial organelles (AOs) have significant potential as long-acting biomedical implants, mimicking native organelles by conducting intracellularly compartmentalized enzymic actions. The potency of these AOs can be heightened when judiciously combined with genetic engineering, producing highly tailorable biohybrid cellular systems. Here, the authors present a cost-effective, microliter scale (10 μL) polymersome (PSome) synthesis based on polymerization-induced self-assembly for the in situ encapsulation of Gaussia luciferase (GLuc), as a model luminescent enzyme. These GLuc-loaded PSomes present ideal features of AOs including enhanced enzymic resistance to thermal, proteolytic, and intracellular stresses. To demonstrate their biomodulation potential, the intracellular luminescence of GLuc-loaded PSomes is coupled to optogenetically engineered cardiomyocytes, allowing modulation of cardiac beating frequency through treatment with coelenterazine (CTZ) as the substrate for GLuc. The long-term intracellular stability of the luminescent AOs allows this cardiostimulatory phenomenon to be reinitiated with fresh CTZ even after 7 days in culture. This synergistic combination of organelle-mimicking synthetic materials with genetic engineering is therefore envisioned as a highly universal strategy for the generation of new biohybrid cellular systems displaying unique triggerable properties. 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 luciferase encapsulated polymersome artificial organelle optogenetic modulation cardiomyocyte, artificial organelles, bioluminescences, cardiomyocytes, nanoreactors, optogenetics, polymerization-induced self-assembly, polymersomes and other aspects.HPLC of Formula: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

On August 31, 2019, Al-Ani, Ali W.; Zhang, Lei; Ferreira, Lenny; Turyanska, Lyudmila; Bradshaw, Tracey D.; Thomas, Neil R. published an article.SDS of cas: 55779-48-1 The title of the article was Listeria innocua Dps as a nanoplatform for bioluminescence based photodynamic therapy utilizing Gaussia princeps luciferase and zinc protoporphyrin IX. And the article contained the following:

Listeria innocua DNA binding protein from starved cells (LiDps) belongs to the ferritin family and provides a promising self-assembling spherical 12-mer protein scaffold for the generation of functional nanomaterials. We report the creation of a Gaussia princeps luciferase (Gluc)-LiDps fusion protein, with chem. conjugation of Zinc (II)-protoporphyrin IX (ZnPP) to lysine residues on the fusion protein (giving Gluc-LiDps-ZnPP). The Gluc-LiDps-ZnPP conjugate is shown to generate reactive oxygen species (ROS) via Bioluminescence Resonance Energy Transfer (BRET) between the Gluc (470-490 nm) and ZnPP. In vitro, Gluc-LiDps-ZnPP is efficiently taken up by tumorigenic cells (SKBR3 and MDA-MB-231 breast cancer cells). In the presence of coelenterazine, this construct inhibits the proliferation of SKBR3 due to elevated ROS levels. Following exposure to Gluc-LiDps-ZnPP, migration of surviving SKBR3 cells is significantly suppressed. These results demonstrate the potential of the Gluc-LiDps-ZnPP conjugate as a platform for future development of an anticancer photodynamic therapy agent. 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 luciferase zinc protoporphyrin bioluminescence photodynamic therapy breast cancer, bioluminescence resonance energy transfer, gaussia princeps luciferase, listeria innocua dna binding protein, photodynamic therapy, zinc (ii) protoporphyrin ix and other aspects.SDS of cas: 55779-48-1

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem

Vicente, Manuel; Salgado-Almario, Jussep; Soriano, Joaquim; Burgos, Miguel; Domingo, Beatriz; Llopis, Juan published an article in 2019, the title of the article was Visualization of mitochondrial Ca2+ signals in skeletal muscle of zebrafish embryos with bioluminescent indicators.Application In Synthesis of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one And the article contains the following content:

Mitochondria are believed to play an important role in shaping the intracellular Ca2+ transients during skeletal muscle contraction. There is discussion about whether mitochondrial matrix Ca2+ dynamics always mirror the cytoplasmic changes and whether this happens in vivo in whole organisms. In this study, we characterized cytosolic and mitochondrial Ca2+ signals during spontaneous skeletal muscle contractions in zebrafish embryos expressing bioluminescent GFP-aequorin (GA, cytoplasm) and mitoGFP-aequorin (mitoGA, trapped in the mitochondrial matrix). The Ca2+ transients measured with GA and mitoGA reflected contractions of the trunk observed by transmitted light. The mitochondrial uncoupler FCCP and the inhibitor of the mitochondrial calcium uniporter (MCU), DS16570511, abolished mitochondrial Ca2+ transients whereas they increased the frequency of cytosolic Ca2+ transients and muscle contractions, confirming the subcellular localization of mitoGA. Mitochondrial Ca2+ dynamics were also determined with mitoGA and were found to follow closely cytoplasmic changes, with a slower decay. Cytoplasmic Ca2+ kinetics and propagation along the trunk and tail were characterized with GA and with the genetically encoded fluorescent Ca2+ indicator, Twitch-4. Although fluorescence provided a better spatio-temporal resolution, GA was able to resolve the same kinetic parameters while allowing continuous measurements for hours. 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 danio calcium mitochondria skeletal muscle bioluminescent indicator gfp aequorin, gfp-aequorin, twitch-4, aequorin, bioluminescence, calcium, genetically encoded calcium indicator (geci), microscopy, mitochondria, skeletal muscle, zebrafish embryo 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 June 2, 2021, Azad, Taha; Singaravelu, Ragunath; Taha, Zaid; Jamieson, Taylor R.; Boulton, Stephen; Crupi, Mathieu J. F.; Martin, Nikolas T.; Brown, Emily E. F.; Poutou, Joanna; Ghahremani, Mina; Pelin, Adrian; Nouri, Kazem; Rezaei, Reza; Marshall, Christopher Boyd; Enomoto, Masahiro; Arulanandam, Rozanne; Alluqmani, Nouf; Samson, Reuben; Gingras, Anne-Claude; Cameron, D. William; Greer, Peter A.; Ilkow, Carolina S.; Diallo, Jean-Simon; Bell, John C. published an article.Formula: C26H21N3O3 The title of the article was Nanoluciferase complementation-based bioreporter reveals the importance of N-linked glycosylation of SARS-CoV-2 S for viral entry. And the article contained the following:

The ongoing COVID-19 pandemic has highlighted the immediate need for the development of antiviral therapeutics targeting different stages of the SARS-CoV-2 life cycle. We developed a bioluminescence-based bioreporter to interrogate the interaction between the SARS-CoV-2 viral spike (S) protein and its host entry receptor, angiotensin-converting enzyme 2 (ACE2). The bioreporter assay is based on a nanoluciferase complementation reporter, composed of two subunits, large BiT and small BiT, fused to the S receptor-binding domain (RBD) of the SARS-CoV-2 S protein and ACE2 ectodomain, resp. Using this bioreporter, we uncovered critical host and viral determinants of the interaction, including a role for glycosylation of asparagine residues within the RBD in mediating successful viral entry. We also demonstrate the importance of N-linked glycosylation to the RBD’s antigenicity and immunogenicity. Our study demonstrates the versatility of our bioreporter in mapping key residues mediating viral entry as well as screening inhibitors of the ACE2-RBD interaction. Our findings point toward targeting RBD glycosylation for therapeutic and vaccine strategies against SARS-CoV-2. 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 ace2 spike glycoprotein interaction glycosylation sars cov2 covid19 human, sarscov2 s protein viral entry nanoluciferase bioreporter n glycosylation, 2019-ncov, covid-19, sars-cov-2, bioluminescence, bioreporter, coronavirus, high-throughput screening, viral entry and other aspects.Formula: C26H21N3O3

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem