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Catalogue Number : AV-H10017
Specification : 98%
CAS number : 22172-17-4
Formula : C15H12O6
Molecular Weight : 288.25
PUBCHEM ID : 5281653
Volume : 20mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystalline powder

Botanical Source

Centaurium cachanlahuen, Canscora decussata, Swertia connata, Swertia angustifolia and Swertia perennis

Structure Type


Standards;Natural Pytochemical;API




1,8-dihydroxy-2,6-dimethoxyxanthen-9-one/7-O-methyl swertianin/Swertiaperennin/Xanthen-9-one,1,8-dihydroxy-2,6-dimethoxy/metylswertianin/Methylswertianin/9H-Xanthen-9-one, 1,8-dihydroxy-2,6-dimethoxy-/1,8-Dihydroxy-2,6-dimethoxy-9H-xanthen-9-one/1,8-dihydroxy-3,7-dimethoxyxanthone/swertsiaperennin/1,8-Dihydroxy-2,6-dimethoxyxanthone/2-O-Methylswertianin




1.5±0.1 g/cm3


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

Flash Point

210.7±23.6 °C

Boiling Point

546.3±50.0 °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#:22172-17-4) 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.




Antimicrobial peptides are important as the first line of innate defense, through their tendency to disrupt bacterial membranes or intracellular pathways and potentially as the next generation of antibiotics. How they protect wet epithelia is not entirely clear, with most individually inactive under physiological conditions and many preferentially targeting Gram-positive bacteria. Tears covering the surface of the eye are bactericidal for Gram-positive and -negative bacteria. Here we narrow much of the bactericidal activity to a latent C-terminal fragment in the prosecretory mitogen lacritin and report that the mechanism combines membrane permeabilization with rapid metabolic changes, including reduced levels of dephosphocoenzyme A, spermidine, putrescine, and phosphatidylethanolamines and elevated alanine, leucine, phenylalanine, tryptophan, proline, glycine, lysine, serine, glutamate, cadaverine, and pyrophosphate. Thus, death by metabolic stress parallels cellular attempts to survive. Cleavage-dependent appearance of the C-terminal cationic amphipathic α-helix is inducible within hours by Staphylococcus epidermidis and slowly by another mechanism, in a chymotrypsin- or leupeptin protease-inhibitable manner. Although bactericidal at low micromolar levels, within a biphasic 1-10 nm dose optimum, the same domain is mitogenic and cytoprotective for epithelia via a syndecan-1 targeting mechanism dependent on heparanase. Thus, the C terminus of lacritin is multifunctional by dose and proteolytic processing and appears to play a key role in the innate protection of the eye, with wider potential benefit elsewhere as lacritin flows from exocrine secretory cells.


Bacterial Metabolism, Cornea, Eye, Innate Immunity, Phosphatidylethanolamine, Protein Targeting, Serine Protease, Lacritin, Tears


A Cleavage-potentiated Fragment of Tear Lacritin Is Bactericidal*


Robert L. McKown,‡ Erin V. Coleman Frazier,‡ Kaneil K. Zadrozny,‡ Andrea M. Deleault,‡ Ronald W. Raab,‡ Denise S. Ryan,§ Rose K. Sia,§ Jae K. Lee,¶? and Gordon W. Laurie**‡‡§§,1

Publish date

2014 Aug 8




A new virulent phage belonging to the Siphoviridae family and able to infect Lactococcus garvieae strains was isolated from compost soil. Phage GE1 has a prolate capsid (56 by 38 nm) and a long noncontractile tail (123 nm). It had a burst size of 139 and a latent period of 31 min. Its host range was limited to only two L. garvieae strains out of 73 tested. Phage GE1 has a double-stranded DNA genome of 24,847 bp containing 48 predicted open reading frames (ORFs). Putative functions could be assigned to only 14 ORFs, and significant matches in public databases were found for only 17 ORFs, indicating that GE1 is a novel phage and its genome contains several new viral genes and encodes several new viral proteins. Of these 17 ORFs, 16 were homologous to deduced proteins of virulent phages infecting the dairy bacterium Lactococcus lactis, including previously characterized prolate-headed phages. Comparative genome analysis confirmed the relatedness of L. garvieae phage GE1 to L. lactis phages c2 (22,172 bp) and Q54 (26,537 bp), although its genome organization was closer to that of phage c2. Phage GE1 did not infect any of the 58 L. lactis strains tested. This study suggests that phages infecting different lactococcal species may have a common ancestor.


A Virulent Phage Infecting Lactococcus garvieae, with Homology to Lactococcus lactis Phages


Giovanni Eraclio,a Denise M. Tremblay,b Alexia Lacelle-C?te,b,c Simon J. Labrie,b,c Maria Grazia Fortina,a and Sylvain Moineaucorresponding authorb,c

Publish date

2015 Dec;




The nucleotide sequence of a 2505 bp region of the Escherichia coli chromosome containing the LexA regulated ruv gene has been determined. A sequence of 1631 bp encoding two non-overlapping open reading frames that constitute a single operon and which specify polypeptides with predicted molecular weights of 22172 daltons and 37177 daltons respectively, was identified as the most probable sequence for ruv. Each of the two open reading frames, designated ruvA and ruvB, is preceded by a reasonable Shine-Dalgarno sequence. Two 16 bp sequences (SOS boxes) that match the consensus sequence for binding LexA protein are located 5′ to ruvA in a region that provides a possible single promoter for expression of both ruvA and ruvB, with the second SOS box overlapping the putative -35 region. A possible transcriptional terminator is located 137 bp downstream of ruvB. The amino acid sequence predicted for RuvB contains a region that matches a highly conserved sequence found in several DNA repair and recombination proteins that bind ATP.


Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genes.


F E Benson, G T Illing, G J Sharples, and R G Lloyd

Publish date

1988 Feb 25