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3-Aminoquinoline

$52

  • Brand : BIOFRON

  • Catalogue Number : BN-O1172

  • Specification : 98%(HPLC)

  • CAS number : 580-17-6

  • Formula : C9H8N2

  • Molecular Weight : 144.17

  • PUBCHEM ID : 11375

  • Volume : 5mg

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Catalogue Number

BN-O1172

Analysis Method

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

144.17

Appearance

Botanical Source

Structure Type

Category

SMILES

C1=CC=C2C(=C1)C=C(C=N2)N

Synonyms

3-Aminoquinoline/3-Quinolinamine/quinolin-3-amine

IUPAC Name

quinolin-3-amine

Density

1.2±0.1 g/cm3

Solubility

Flash Point

167.8±7.6 °C

Boiling Point

311.4±15.0 °C at 760 mmHg

Melting Point

91-92 °C(lit.)

InChl

InChl Key

SVNCRRZKBNSMIV-UHFFFAOYSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:580-17-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

29057454

Abstract

Background and Purpose
The aim of this study was to compare the abilities of cannabidiolic acid methyl ester (HU‐580) and cannabidiolic acid (CBDA) to enhance 5‐HT1A receptor activation in vitro and produce 5‐HT1A‐mediated reductions in nausea and anxiety in vivo.

Experimental Approach
We investigated the effects of HU‐580 and CBDA on (i) activation by 8‐hydroxy‐2‐(di‐n‐propylamino)tetralin of human 5‐HT1A receptors in CHO cell membranes, using [35S]‐GTPγS binding assays, (ii) gaping by rats in acute and anticipatory nausea models, and (iii) stress‐induced anxiety‐like behaviour, as indicated by exit time from the light compartment of a light-dark box of rats subjected 24 h earlier to six tone‐paired foot shocks.

Key Results
HU‐580 and CBDA increased the Emax of 8‐hydroxy‐2‐(di‐n‐propylamino) tetralin in vitro at 0.01-10 and 0.1-10 nM, respectively, and reduced signs of (i) acute nausea at 0.1 and 1 μg·kg−1 i.p. and at 1 μg·kg−1 i.p., respectively, and (ii) anticipatory nausea at 0.01 and 0.1 μg·kg−1, and at 0.1 μg·kg−1 i.p. respectively. At 0.01 μg·kg−1, HU‐580, but not CBDA, increased the time foot‐shocked rats spent in the light compartment of a light-dark box. The anti‐nausea and anti‐anxiety effects of 0.01 or 0.1 μg·kg−1 HU‐580 were opposed by the 5‐HT1A antagonist, WAY100635 (0.1 mg·kg−1 i.p.).

Conclusions and Implications
HU‐580 is more potent than CBDA at enhancing 5‐HT1A receptor activation, and inhibiting signs of acute and anticipatory nausea, and anxiety. Consequently, HU‐580 is a potential medicine for treating some nausea and anxiety disorders and possibly other disorders ameliorated by enhancement of 5‐HT1A receptor activation.

Title

Cannabidiolic acid methyl ester, a stable synthetic analogue of cannabidiolic acid, can produce 5‐HT1A receptor‐mediated suppression of nausea and anxiety in rats

Author

Roger G Pertwee,corresponding author 1 Erin M Rock, 2 Kelsey Guenther, 2 Cheryl L Limebeer, 2 Lesley A Stevenson, 1 Christeene Haj, 3 Reem Smoum, 3 Linda A Parker, 2 and Raphael Mechoulam 3

Publish date

2018 Jan;

PMID

31438573

Abstract

QuasAr1 is a fluorescent voltage sensor derived from Archaerhodopsin 3 (Arch) of Halorubrum sodomense by directed evolution. Here we report absorption and emission spectroscopic studies of QuasAr1 in Tris buffer at pH 8. Absorption cross-section spectra, fluorescence quantum distributions, fluorescence quantum yields, and fluorescence excitation spectra were determined. The thermal stability of QuasAr1 was studied by long-time attenuation coefficient measurements at room temperature (23 ± 2 °C) and at 2.5 ± 0.5 °C. The apparent melting temperature was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 65 ± 3 °C). In the protein melting process the originally present protonated retinal Schiff base (PRSB) with absorption maximum at 580 nm converted to de-protonated retinal Schiff base (RSB) with absorption maximum at 380 nm. Long-time storage of QuasAr1 at temperatures around 2.5 °C and around 23 °C caused gradual protonated retinal Schiff base isomer changes to other isomer conformations, de-protonation to retinal Schiff base isomers, and apoprotein structure changes showing up in ultraviolet absorption increase. Reaction coordinate schemes are presented for the thermal protonated retinal Schiff base isomerizations and deprotonations in parallel with the dynamic apoprotein restructurings.

KEYWORDS

QuasArs, Archaerhodopsin 3, genetically encoded voltage sensors (GEVIs), absorption spectroscopic characterization, fluorescence spectroscopic characterization, apparent protein melting temperature, thermal stability, thermal isomerization, thermal deprotonation

Title

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1

Author

Alfons Penzkofer,1,* Arita Silapetere,2 and Peter Hegemann2

Publish date

2019 Sep;

PMID

29899087

Abstract

Herpes simplex virus 1 (HSV-1) is a prevalent human pathogen that infects the cornea, causing potentially blinding herpetic disease. A clinical herpes vaccine is still lacking. In the present study, a novel prime/pull vaccine was tested in a human leukocyte antigen (HLA) transgenic rabbit model of ocular herpes (HLA Tg rabbits). Three peptide epitopes were selected, from the HSV-1 membrane glycoprotein C (UL44400-408), the DNA replication binding helicase (UL9196-204), and the tegument protein (UL25572-580), all preferentially recognized by CD8+ T cells from “naturally protected” HSV-1-seropositive healthy asymptomatic (ASYMP) individuals (who never had recurrent corneal herpetic disease). HLA Tg rabbits were immunized with a mixture of these three ASYMP CD8+ T cell peptide epitopes (UL44400-408, UL9196-204, and UL25572-580), which were delivered subcutaneously with CpG2007 adjuvant (prime). Fifteen days later, half of the rabbits received a topical ocular treatment with a recombinant neurotropic adeno-associated virus type 8 (AAV8) vector expressing the T cell-attracting CXCL10 chemokine (pull). The frequency and function of HSV-specific CD8+ T cells induced by the prime/pull vaccine were assessed in the peripheral blood, cornea, and trigeminal ganglion (TG). Compared to the cells generated in response to peptide immunization alone, the peptide/CXCL10 prime/pull vaccine generated frequent polyfunctional gamma interferon-positive (IFN-γ+) CD107+ CD8+ T cells that infiltrated both the cornea and TG. CD8+ T cell mobilization into the cornea and TG of prime/pull-vaccinated rabbits was associated with a significant reduction in corneal herpesvirus infection and disease following an ocular HSV-1 (strain McKrae) challenge. These findings draw attention to the novel prime/pull vaccine strategy for mobilizing antiviral CD8+ T cells into tissues to protect against herpesvirus infection and disease.

IMPORTANCE There is an urgent need for a vaccine against widespread herpes simplex virus infections. The present study demonstrates that immunization of HLA transgenic rabbits with a peptide/CXCL10 prime/pull vaccine triggered mobilization of HSV-specific CD8+ T cells locally into the cornea and TG, the sites of acute and latent herpesvirus infections, respectively. Mobilization of antiviral CD8+ T cells into the cornea and TG of rabbits that received the prime/pull vaccine was associated with protection against ocular herpesvirus infection and disease following an ocular HSV-1 challenge. These results highlight the importance of the prime/pull vaccine strategy to bolster the number and function of protective CD8+ T cells within infected tissues.

KEYWORDS

HSV-1, ocular, herpes, HLA transgenic rabbit, CD8+ T cell, prime/pull vaccine, CXCL10, herpes simplex, prime/pull

Title

Human Asymptomatic Epitope Peptide/CXCL10-Based Prime/Pull Vaccine Induces Herpes Simplex Virus-Specific Gamma Interferon-Positive CD107+ CD8+ T Cells That Infiltrate the Corneas and Trigeminal Ganglia of Humanized HLA Transgenic Rabbits and Protect against Ocular Herpes Challenge

Author

Arif A. Khan,a Ruchi Srivastava,a Hawa Vahed,a Soumyabrata Roy,a Sager S. Walia,a Grace J. Kim,a Mona A. Fouladi,a Taikun Yamada,a Vincent T. Ly,a Cynthia Lam,a Anthony Lou,a Vivianna Nguyen,a Undariya Boldbaatar,a Roger Geertsema,b Nigel W. Fraser,a and Lbachir BenMohamedcorresponding authora,c,d

Publish date

2018 Aug 15;


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