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1-O-Methylnataloe-emodin

$1,671

  • Brand : BIOFRON

  • Catalogue Number : BD-D0044

  • Specification : HPLC≥98%

  • CAS number : 103392-51-4

  • Formula : C16H12O5

  • Molecular Weight : 284.26

  • PUBCHEM ID : 10902125

  • Volume : 5mg

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Quantity
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Catalogue Number

BD-D0044

Analysis Method

HPLC,NMR,MS

Specification

HPLC≥98%

Storage

2-8°C

Molecular Weight

284.26

Appearance

Powder

Botanical Source

Structure Type

Anthraquinones

Category

Standards;Natural Pytochemical;API

SMILES

CC1=CC2=C(C(=C1)O)C(=O)C3=C(C2=O)C=CC(=C3OC)O

Synonyms

2,8-Dihydroxy-1-methoxy-6-methyl-anthrachinon/4.6-Dihydroxy-5-methoxy-2-methyl-anthrachinon/2,8-dihydroxy-1-methoxy-6-methyl-anthraquinone/nataloe-emodin-8-methyl ether

IUPAC Name

2,8-dihydroxy-1-methoxy-6-methylanthracene-9,10-dione

Applications

Density

Solubility

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

Flash Point

Boiling Point

Melting Point

InChl

InChI=1S/C16H12O5/c1-7-5-9-12(11(18)6-7)15(20)13-8(14(9)19)3-4-10(17)16(13)21-2/h3-6,17-18H,1-2H3

InChl Key

OCZOZMSHTPWVFR-UHFFFAOYSA-N

WGK Germany

RID/ADR

HS Code Reference

2933990000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:103392-51-4) 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.

PMID

30186693

Abstract

Background
Jasmonic acid (JA) and its derivative, methyl JA (MeJA) are hormonal cues released by plants that signal defense response to curb damages from biotic and abiotic stresses. To study such response, a tropical herbal plant, Persicaria minor, which possesses pungent smell and various bioactivities including antimicrobial and anticancer, was treated with MeJA. Such elicitation has been performed in hairy root cultures and plants such as Arabidopsis and rice, yet how MeJA influenced the proteome of an herbal species like P. minor is unknown.

Method
In this study, P. minor plants were exogenously elicited with MeJA and leaf samples were subjected to SWATH-MS proteomics analysis. A previously published translated transcriptome database was used as a reference proteome database for a comprehensive protein sequence catalogue and to compare their differential expression.

Results
From this proteomics informed by transcriptomics approach, we have successfully profiled 751 proteins of which 40 proteins were significantly different between control and MeJA-treated samples. Furthermore, a correlation analysis between both proteome and the transcriptome data sets suggests that significantly upregulated proteins were positively correlated with their cognate transcripts (Pearson’s r = 0.677) while a weak correlation was observed for downregulated proteins (r = 0.147).

Discussion
MeJA treatment induced the upregulation of proteins involved in various biochemical pathways including stress response mechanism, lipid metabolism, secondary metabolite production, DNA degradation and cell wall degradation. Conversely, proteins involved in energy expensive reactions such as photosynthesis, protein synthesis and structure were significantly downregulated upon MeJA elicitation. Overall protein-transcript correlation was also weak (r = 0.341) suggesting the existence of post-transcriptional regulation during such stress. In conclusion, proteomics analysis using SWATH-MS analysis supplemented by the transcriptome database allows comprehensive protein profiling of this non-model herbal species upon MeJA treatment.

KEYWORDS

LC-MS/MS, Label-free proteomics, Methyl jasmonate, Polygonum minus, SWATH-MS analysis

Title

Proteomics (SWATH-MS) informed by transcriptomics approach of tropical herb Persicaria minor leaves upon methyl jasmonate elicitation

Author

Wan Mohd Aizat,corresponding author Sarah Ibrahim, Reyhaneh Rahnamaie-Tajadod, Kok-Keong Loke, Hoe-Han Goh, and Normah Mohd Noorcorresponding author

Publish date

2018;

PMID

30086762

Abstract

Background
The board certification system serves as a quality assurance system for physicians, and its design and operation are important health policy issues. In Japan, board certification was established and operated independently by academic societies and has not been directly linked to reimbursement systems. The phenomenon of younger physicians seeking specialist careers has raised concerns about acceleration of the tendency of fewer physicians working in rural areas and the maldistribution of physicians. Little is known about the associations between physicians’ geographical migration patterns and board certification status changes or between the continuation of urban/rural practice and the maintenance of board certification. This study aimed to identify these associations and to discuss their policy implications.

Methods
We analyzed 2012 and 2014 data from the Survey of Physicians, Dentists, and Pharmacists, a national census survey. To analyze geographical migration patterns, transitions in practice location (rural, intermediate, and urban) were analyzed by board certification status change (new, lost, consistently certified, and consistently uncertified). Logistic regression analysis was conducted to assess whether the odds of migrating to more urban/rural municipalities were associated with board certification status changes, adjusting for covariates, and whether practicing in a rural area was associated with maintaining board certification.

Results
Among 18,726 newly board-certified physicians, 94.9% (13,435/14,150) of those working in urban areas before certification remained in urban areas, whereas 64.6% (393/608) of those working in rural areas stayed in rural areas. Those who were newly certified had higher odds of moving to more urban areas, adjusting for covariates. Those who stayed in rural areas showed lower odds of maintaining board certification, adjusting for covariates.

Conclusions
Newly board-certified physicians are more likely to migrate to other types of areas, particularly more urban areas, than other physicians. Allocating more training quotas to rural areas could be one option for leveling the distribution of specialists. It also appeared that those practicing in rural areas have difficulty maintaining their certification, so the need to establish a support system for already-certified physicians in rural areas should be emphasized.

Electronic supplementary material
The online version of this article (10.1186/s12913-018-3441-y) contains supplementary material, which is available to authorized users.

KEYWORDS

Board certification, Maintenance of board certification, Urban-rural migration, Physician distribution

Title

Board certification and urban-rural migration of physicians in Japan

Author

Soichi Koike,corresponding author1,2 Masatoshi Matsumoto,3 Hideaki Kawaguchi,4 Hiroo Ide,5 Hidenao Atarashi,6 Kazuhiko Kotani,7 and Hideo Yasunaga8

Publish date

2018;

PMID

24803923

Abstract

Background
Numerous spider toxins are of interest as tools for neurophysiological research or as lead molecules for the development of pharmaceuticals and insecticides. Direct detection and identification of the interacting proteins of a spider toxin are helpful for its action-mechanism analysis and practical application. The present study employed a combinative strategy for the analysis of interacting proteins of huwentoxin-IV (HWTX-IV), a peptidic neurotoxin from the venom of the spider Selenocosmia huwena.

Results
HWTX-IV was first lightly labeled with biotin under the optimized mild experimental conditions and the toxin labeled with a single biotin group (monobiotinylated HWTX-IV) was demonstrated by electrophysiological experiments to retain its original bioactivity and was used in combination with far-western blotting to detect its interacting proteins. Comparative experiments indicated that some membrane proteins from rat neuromuscular junction preparations bind to monobiotinylated HWTX-IV after being transferred onto a PVDF membrane from the SDS-gel. With capillary high performance liquid chromatography-tandem mass spectrometry, several membrane proteins with which HWTX-IV potentially interacted were identified from the preparations and then bioinformatically analyzed.

Conclusions
This work has provided not only a new insight into the action mechanism of HWTX-IV but also a reference technology for the relevant researches.

KEYWORDS

Biotin labeling, Huwentoxin-IV, Far-western blotting, Interacting protein, Mass spectrometry

Title

Detection and identification of huwentoxin-IV interacting proteins by biotin-avidin chemistry combined with mass spectrometry

Author

Hai Yu,1 Hui Liu,1 Yizhong Yan,1 Zhigui Duan,1 and Xianchun Wangcorresponding author1

Publish date

2014