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Lucidal

$1,248

  • Brand : BIOFRON

  • Catalogue Number : BN-O0988

  • Specification : 98%(HPLC)

  • CAS number : 252351-96-5

  • Formula : C30H46O3

  • Molecular Weight : 454.68

  • PUBCHEM ID : 10366713

  • Volume : 5mg

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Catalogue Number

BN-O0988

Analysis Method

HPLC,NMR,MS

Specification

98%(HPLC)

Storage

-20℃

Molecular Weight

454.68

Appearance

Powder

Botanical Source

This product is isolated and purified from the fruit body of Ganoderma lucidum

Structure Type

Triterpenoids

Category

Standards;Natural Pytochemical;API

SMILES

CC(CCC=C(C)C=O)C1CCC2(C1(CCC3=C2C(=O)CC4C3(CCC(C4(C)C)O)C)C)C

Synonyms

LUCIALDEHYDE C

IUPAC Name

(E,6R)-6-[(3S,5R,10S,13R,14R,17R)-3-hydroxy-4,4,10,13,14-pentamethyl-7-oxo-1,2,3,5,6,11,12,15,16,17-decahydrocyclopenta[a]phenanthren-17-yl]-2-methylhept-2-enal

Density

1.1±0.1 g/cm3

Solubility

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

Flash Point

312.6±26.6 °C

Boiling Point

570.0±50.0 °C at 760 mmHg

Melting Point

InChl

InChI=1S/C30H46O3/c1-19(18-31)9-8-10-20(2)21-11-16-30(7)26-22(12-15-29(21,30)6)28(5)14-13-25(33)27(3,4)24(28)17-23(26)32/h9,18,20-21,24-25,33H,8,10-17H2,1-7H3/b19-9+/t20-,21-,24?,25+,28-,29-,30+/m1/s1

InChl Key

PIOYBULRRJNPSG-WOXSLIATSA-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#:252351-96-5) 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

28575285

Abstract

Variation in Clostridium difficile infection (CDI) rates between healthcare institutions suggests overall incidence could be reduced if the lowest rates could be achieved more widely.

Methods.
We used whole-genome sequencing (WGS) of consecutive C. difficile isolates from 6 English hospitals over 1 year (2013-14) to compare infection control performance. Fecal samples with a positive initial screen for C. difficile were sequenced. Within each hospital, we estimated the proportion of cases plausibly acquired from previous cases.

Results.
Overall, 851/971 (87.6%) sequenced samples contained toxin genes, and 451 (46.4%) were fecal-toxin-positive. Of 652 potentially toxigenic isolates >90-days after the study started, 128 (20%, 95% confidence interval [CI] 17-23%) were genetically linked (within ≤2 single nucleotide polymorphisms) to a prior patient’s isolate from the previous 90 days. Hospital 2 had the fewest linked isolates, 7/105 (7%, 3-13%), hospital 1, 9/70 (13%, 6-23%), and hospitals 3-6 had similar proportions of linked isolates (22-26%) (P ≤ .002 comparing hospital-2 vs 3-6). Results were similar adjusting for locally circulating ribotypes. Adjusting for hospital, ribotype-027 had the highest proportion of linked isolates (57%, 95% CI 29-81%). Fecal-toxin-positive and toxin-negative patients were similarly likely to be a potential transmission donor, OR = 1.01 (0.68-1.49). There was no association between the estimated proportion of linked cases and testing rates.

Conclusions.
WGS can be used as a novel surveillance tool to identify varying rates of C. difficile transmission between institutions and therefore to allow targeted efforts to reduce CDI incidence.

KEYWORDS

infection control, Clostridium difficile, whole-genome sequencing, transmission, surveillance.

Title

Comparison of Control of Clostridium difficile Infection in Six English Hospitals Using Whole-Genome Sequencing

Author

David W. Eyre, Warren N. Fawley, Anu Rajgopal, Christopher Settle, Kalani Mortimer, Simon D. Goldenberg, Susan Dawson, Derrick W. Crook, Tim E. A. Peto, A. Sarah Walker, Mark H. Wilcox

Publish date

2017 Aug 1;

PMID

9385635

Abstract

Protein function is often controlled by ligand-induced conformational transitions. Yet, in spite of the increasing number of three-dimensional crystal structures of proteins in different conformations, not much is known about the driving forces of these transitions. As an initial step toward exploring the conformational and energetic landscape of protein kinases by computational methods, intramolecular energies and hydration free energies were calculated for different conformations of the catalytic domain of cAMP-dependent protein kinase (cAPK) with a continuum (Poisson) model for the electrostatics. Three protein kinase crystal structures for ternary complexes of cAPK with the peptide inhibitor PKI(5-24) and ATP or AMP-PNP were modeled into idealized intermediate and open conformations. Concordant with experimental observation, we find that the binding of PKI(5-24) is more effective in stabilizing the closed and intermediate forms of cAPK than ATP. PKI(5-24) seems to drive the final closure of the active site cleft from intermediate to closed state because ATP does not distinguish between these two states. Binding of PKI(5-24) and ATP is energetically additive.

Title

Kinase conformations: a computational study of the effect of ligand binding.

Author

V. Helms and J. A. McCammon

Publish date

1997 Nov

PMID

21583595

Abstract

The title compound, NH4 +·C8H7Cl2O6 −·0.5H2O, was prepared by the reaction of 2-(2,4-dichloro­phen­oxy)­acetic acid and ammonia in water at 367 K. The mol­ecular structure and packing are stabilized by N—H⋯O and O—H⋯O inter­molecular hydrogen-bond inter­actions.

Title

Ammonium 2-(2,4-dichloro­phen­oxy)acetate hemihydrate

Author

Hui-Lian Liu,a Shu-Hua Guo,a Yun-Ying Li,b and Fang-Fang Jianc,*

Publish date

2009 Aug 1;


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