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  • Brand : BIOFRON

  • Catalogue Number : BF-I1005

  • Specification : 98%

  • CAS number : 6817-41-0

  • Formula : C37H42N2O6

  • Molecular Weight : 610.747

  • PUBCHEM ID : 5274591

  • Volume : 20mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystalline powder

Botanical Source

Nelumbo nucifera

Structure Type



Standards;Natural Pytochemical;API




(1R)-1-(4-Hydroxy-3-{[(1R)-6-methoxy-1-(4-methoxybenzyl)-2-methyl-1,2,3,4-tetrahydro-7-isoquinolinyl]oxy}benzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydro-7-isoquinolinol/Isoliensinin/(1R)-1-(4-Hydroxy-3-{[(1R)-6-methoxy-1-(4-methoxybenzyl)-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-yl]oxy}benzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol/7-Isoquinolinol, 1,2,3,4-tetrahydro-1-[[4-hydroxy-3-[[(1R)-1,2,3,4-tetrahydro-6-methoxy-1-[(4-methoxyphenyl)methyl]-2-methyl-7-isoquinolinyl]oxy]phenyl]methyl]-6-methoxy-2-methyl-, (1R)-/Isoliensinine




1.2±0.1 g/cm3


Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.

Flash Point

391.1±32.9 °C

Boiling Point

723.1±60.0 °C at 760 mmHg

Melting Point




InChl Key


WGK Germany


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#:6817-41-0) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate




A rapid and specific HPLC method has been developed and validated for the simultaneous determination of liensinine (CAS 2586-96-1), isoliensinine (CAS 6817-41-0) and neferine (CAS 2292-16-2) in rat plasma. The sample was prepared by a liquid-liquid extraction with diethyl ether and the recovery was above 80% from the plasma for the three compounds. Chromatographic separation was achieved with a Hypersil BDS C18 column (4.0 mm x 250 mm, particle size 5 microm). A mobile phase consisting of methanol: 0.2 M KH2PO4:0.2 M NaOH:triethylamine (71:17:12:0.002, v/v/v/v, pH 9.2-9.3) was slowly delivered at 0.8 ml/min in isocratic mode with a detection wavelength of 282 nm. The linearity of calibration curves were good (r > 0.999) in the concentration range of 0.031-2.00 microg/ ml. The lower limit of quantification can reach 0.03 microg/ml for the three compounds. The intra-day and inter-day variations estimated with QC samples were less than 8% for the three tested concentration levels. This developed method was applied in the plasma pharmacokinetic study of total bisbenzylisoquinoline alkaloids (TAL) of the lotus flower (Lian Zi Xin) following a single oral and intravenous administration of TAL in rats.


Simultaneous determination of liensinine, isoliensinine and neferine from seed embryo of Nelumbo nucifera Gaertn. in rat plasma by a rapid HPLC method and its application to a pharmacokinetic study.


Huang Y1, Zhao L, Bai Y, Liu P, Wang J, Xiang J.

Publish date





The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.


Complete nucleotide sequence of the neuraminidase gene of influenza B virus.


M W Shaw, R A Lamb, B W Erickson, D J Briedis, and P W Choppin

Publish date

1982 Nov;




The nifLA operon of Klebsiella pneumoniae codes for the two antagonistic regulatory proteins which control expression of all other nitrogen fixation genes. NifA is a transcriptional activator, and NifL inhibits NifA. The importance of a correct NifL-NifA stoichiometry for efficient regulation of nitrogen fixation genes has been investigated by constructing a strain with an altered nifL-nifA gene dosage ratio, resulting from the integration of an extra copy of nifA. Results showed that a balanced synthesis of both gene products is essential for correct regulation. Effects of mutations provoking translation termination of nifL upstream or downstream of its natural stop codon, combined with overproduction of both proteins when the genes are transcribed and translated from signals of the phi10 gene of the phage T7, showed that, in addition to the previously reported transcriptional polarity, there is translational coupling between nifL and nifA. In spite of the apparently efficient ribosome binding site of nifA, its rate of independent translation is very low. This is due to a secondary structure masking the Shine-Dalgarno sequence of nifA, which could be melted by ribosomes translating nifL. Mutational analysis confirmed the functional significance of the secondary structure in preventing independent translation of nifA. Translational coupling between the two cistrons is proposed as an efficient mechanism to prevent production of an excess of NifA, which would affect the normal regulation of nitrogen fixation genes.


Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae.


F Govantes, J A Molina-Lopez, and E Santero

Publish date

1996 Dec

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