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.
28575285
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.
infection control, Clostridium difficile, whole-genome sequencing, transmission, surveillance.
Comparison of Control of Clostridium difficile Infection in Six English Hospitals Using Whole-Genome Sequencing
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
2017 Aug 1;
9385635
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.
Kinase conformations: a computational study of the effect of ligand binding.
V. Helms and J. A. McCammon
1997 Nov
21583595
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.
Ammonium 2-(2,4-dichlorophenoxy)acetate hemihydrate
Hui-Lian Liu,a Shu-Hua Guo,a Yun-Ying Li,b and Fang-Fang Jianc,*
2009 Aug 1;
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