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Synephrine hydrochloride

$78

  • Brand : BIOFRON

  • Catalogue Number : BF-S2023

  • Specification : 98%

  • CAS number : 5985-28-4

  • Formula : C9H14ClNO2

  • Molecular Weight : 203.666

  • PUBCHEM ID : 42609626

  • Volume : 20mg

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Catalogue Number

BF-S2023

Analysis Method

HPLC,NMR,MS

Specification

98%

Storage

-20℃

Molecular Weight

203.666

Appearance

Off-White crystalline powder

Botanical Source

Citrus

Structure Type

Alkaloids

Category

Standards;Natural Pytochemical;API

SMILES

CNCC(C1=CC=C(C=C1)O)O.Cl

Synonyms

DL-synephrine hydrochloride/Synephrine HCl/4-(1-Hydroxy-2-(methylamino)ethyl)phenol hydrochloride/Synephrine hydrochloride/4-[1-Hydroxy-2-(methylamino)ethyl]phenol hydrochloride (1:1)/2-methylamino-1-(4-hydroxyphenyl)-ethanol hydrochloride/Benzenemethanol, 4-hydroxy-α-[(methylamino)methyl]-, hydrochloride (1:1)/(+-)-1-(4-hydroxy-phenyl)-2-methylamino-ethanol,hydrochloride/Oxedrine hydrochloride/Ocuton (TN)/1-(4-Hydroxy-phenyl)-2-methylamino-aethanol,Hydrochlorid

IUPAC Name

4-[1-hydroxy-2-(methylamino)ethyl]phenol;hydrochloride

Density

Solubility

Soluble in DMSO > 10 mM

Flash Point

163.4ºC

Boiling Point

341.1ºC at 760 mmHg

Melting Point

147-150ºC

InChl

InChI=1S/C9H13NO2.ClH/c1-10-6-9(12)7-2-4-8(11)5-3-7;/h2-5,9-12H,6H2,1H3;1H

InChl Key

COTCEGYSNTWJQV-UHFFFAOYSA-N

WGK Germany

RID/ADR

HS Code Reference

2922290000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:5985-28-4) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

PMID

10653292

Abstract

Although magnetic resonance imaging (MRI) has improved the diagnostic accuracy of meniscal pathology, the authors believe that physical examination remains essential to the evaluation of knee pathology. In this study, the diagnostic accuracy of five clinical tests for meniscal pathology was prospectively evaluated in 160 patients, who thereafter underwent arthroscopy. 69% (109 knees) of the knees tested had associated ACL deficiency. There were 144 meniscal lesions in 130 of the 160 knees which were examined. The sensitivity of the tests was lower than the specificity. Conventional tests such as McMurray and Apley tests showed a low accuracy rate of 45% and 28% respectively. The diagnostic value of the axially loaded pivot shift test was significantly higher, indicating that this remains a useful diagnostic aid.

Title

M. Kurosaka, M. Yagi, S. Yoshiya, H. Muratsu, and K. Mizuno

Author

M. Kurosaka, M. Yagi, S. Yoshiya, H. Muratsu, and K. Mizuno

Publish date

1999 Dec;

PMID

8650206

Abstract

Expression of the epsilon-subunit gene of the acetylcholine receptor (AChR) by myonuclei located at the neuromuscular junction is precisely regulated during development. A key role in this regulation is played by the synaptic portion of the basal lamina, a structure that is also known to contain agrin, a component responsible for the formation of postsynaptic specializations. We tested whether agrin has a function in synaptic AChR gene expression. Synaptic basal lamina from native adult muscle and recombinant agrin bound to various substrates induced in cultured rat myotubes AChR clusters that were colocalized with epsilon-subunit mRNA. Estimation of transcript levels by Northern hybridization analysis of total RNA showed a significant increase when myotubes were grown on substrate impregnated with agrin, but were unchanged when agrin was applied in the medium. The effect was independent of the receptor aggregating activity of the agrin isoform used, and agrin acted, at least in part, at the level of epsilon-subunit gene transcription. These findings are consistent with a role of agrin in the regulation of AChR subunit gene expression at the neuromuscular junction, which would depend on its binding to the synaptic basal lamina.

Title

Substrate-bound agrin induces expression of acetylcholine receptor epsilon-subunit gene in cultured mammalian muscle cells.

Author

G Jones, A Herczeg, M A Ruegg, M Lichtsteiner, S Kroger, and H R Brenner

Publish date

1996 Jun 11;

PMID

6351071

Abstract

The topographical distributions and mobilities of the murine histocompatibility antigen H-2Kk and of concanavalin A (Con A) binding sites have been studied on a murine lymphoma cell line. The spatial distribution of H-2Kk antigens, the average distance between H-2Kk antigens and Con A binding sites, and the separation of different determinants on the H-2Kk antigen itself were determined by using fluorescence resonance energy-transfer measurements with a dual-laser flow sorter. From the lack of energy transfer between bound monoclonal anti-H-2Kk antibodies conjugated with fluorescein (donor) and rhodamine (acceptor), we conclude that the H-2Kk antigen exists without appreciable clustering on the cell surface. Substantial energy transfer between appropriately labeled Con A and antibodies bound to the H-2Kk antigen shows that the two populations are interspersed. Donor/acceptor pairs of monoclonal antibodies binding to different determinants on the same H-2Kk antigen exhibited a degree of energy transfer indicative of a mean separation of 8.6 nm between the sites. Time-resolved phosphorescence anisotropy measurements with anti-H-2Kk antibodies labeled with eosin or erythrosin yielded rotational mobility information for the antigen-antibody complexes on the cell membrane. The rotational correlation time of 10-20 mus and the finite residual anisotropy are compatible with an uniaxial mode of rotation of monomeric antigen around its transmembrane portion and, thus, provide additional evidence for an unclustered distribution. Capping by rabbit anti-mouse IgG immobilized the antigen-antibody complex. Fluorescence recovery after photobleaching was used to calculate an apparent lateral diffusion coefficient of 5 +/- 3 X 10(-10) cm2 . s-1 for the H-2Kk antigen labeled with fluoresceinated IgG or its corresponding Fab fragment.

Title

Distribution and mobility of murine histocompatibility H-2Kk antigen in the cytoplasmic membrane.

Author

S Damjanovich, L Tron, J Szollosi, R Zidovetzki, W L Vaz, F Regateiro, D J Arndt-Jovin, and T M Jovin

Publish date

1983 Oct;


Description :

Synephrine Hcl(Oxedrine) is an alkaloid; synephrine produces most of its biological effects by acting as an agonist at adrenergic receptors.IC50 value:Target: adrenergic receptor agonistThere is some evidence that synephrine also has weak activity at 5-HT receptors, and that it interacts with TAAR1 (trace adrenergic amine receptors). d-synephrine inhibited the uptake of [3H]-norepinephrine with an IC50 = 5.8 μM; l-synephrine was less potent (IC50 = 13.5 μM). d-Synephrine also competitively inhibited the binding of nisoxetine[m] to rat brain cortical slices, with a Ki = 4.5 μM; l-synephrine was less potent (Ki = 8.2 μM). In experiments on the release of [3H]-norepinephrine from rat brain cortical slices, however, the l-isomer of synephrine was a more potent enhancer of the release (EC50 = 8.2 μM) than the d-isomer (EC50 = 12.3 μM). This enhanced release by l-synephrine was blocked by nisoxetine.