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Jaslanceoside B

$1,056

  • Brand : BIOFRON

  • Catalogue Number : BN-O0901

  • Specification : 97%(HPLC)

  • CAS number : 188300-82-5

  • Formula : C26H30O14

  • Molecular Weight : 566.51

  • PUBCHEM ID : 45359788

  • Volume : 5mg

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Catalogue Number

BN-O0901

Analysis Method

HPLC,NMR,MS

Specification

97%(HPLC)

Storage

2-8°C

Molecular Weight

566.51

Appearance

Powder

Botanical Source

Structure Type

Iridoids

Category

Standards;Natural Pytochemical;API

SMILES

COC(=O)CC1C(=COC(C1=CCOC(=O)C=CC2=CC=C(C=C2)O)OC3C(C(C(C(O3)CO)O)O)O)C(=O)O

Synonyms

Jaslanceoside B/(2S,3E,4S)-2-(β-D-Glucopyranosyloxy)-3-(2-{[(2E)-3-(4-hydroxyphenyl)-2-propenoyl]oxy}ethylidene)-4-(2-methoxy-2-oxoethyl)-3,4-dihydro-2H-pyran-5-carboxylic acid/2H-Pyran-4-acetic acid, 5-carboxy-2-(β-D-glucopyranosyloxy)-3,4-dihydro-3-[2-[[(2E)-3-(4-hydroxyphenyl)-1-oxo-2-propen-1-yl]oxy]ethylidene]-, α-methyl ester, (2S,3E,4S)-

IUPAC Name

(4S,5Z,6S)-5-[2-[(E)-3-(4-hydroxyphenyl)prop-2-enoyl]oxyethylidene]-4-(2-methoxy-2-oxoethyl)-6-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4H-pyran-3-carboxylic acid

Density

1.5±0.1 g/cm3

Solubility

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

Flash Point

268.7±27.8 °C

Boiling Point

811.6±65.0 °C at 760 mmHg

Melting Point

InChl

InChI=1S/C26H30O14/c1-36-20(30)10-16-15(8-9-37-19(29)7-4-13-2-5-14(28)6-3-13)25(38-12-17(16)24(34)35)40-26-23(33)22(32)21(31)18(11-27)39-26/h2-8,12,16,18,21-23,25-28,31-33H,9-11H2,1H3,(H,34,35)/b7-4+,15-8+/t16-,18+,21+,22-,23+,25-,26-/m0/s1

InChl Key

MGEVYVDQMTWJNV-KMSMSTEWSA-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#:188300-82-5) 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

29344086

Abstract

Background
The ascomycete fungus Trichoderma reesei is the predominant source of enzymes for industrial conversion of lignocellulose. Its glycoside hydrolase family 7 cellobiohydrolase (GH7 CBH) TreCel7A constitutes nearly half of the enzyme cocktail by weight and is the major workhorse in the cellulose hydrolysis process. The orthologs from Trichoderma atroviride (TatCel7A) and Trichoderma harzianum (ThaCel7A) show high sequence identity with TreCel7A, ~ 80%, and represent naturally evolved combinations of cellulose-binding tunnel-enclosing loop motifs, which have been suggested to influence intrinsic cellobiohydrolase properties, such as endo-initiation, processivity, and off-rate.

Results
The TatCel7A, ThaCel7A, and TreCel7A enzymes were characterized for comparison of function. The catalytic domain of TatCel7A was crystallized, and two structures were determined: without ligand and with thio-cellotriose in the active site. Initial hydrolysis of bacterial cellulose was faster with TatCel7A than either ThaCel7A or TreCel7A. In synergistic saccharification of pretreated corn stover, both TatCel7A and ThaCel7A were more efficient than TreCel7A, although TatCel7A was more sensitive to thermal inactivation. Structural analyses and molecular dynamics (MD) simulations were performed to elucidate important structure/function correlations. Moreover, reverse conservation analysis (RCA) of sequence diversity revealed divergent regions of interest located outside the cellulose-binding tunnel of Trichoderma spp. GH7 CBHs.

Conclusions
We hypothesize that the combination of loop motifs is the main determinant for the observed differences in Cel7A activity on cellulosic substrates. Fine-tuning of the loop flexibility appears to be an important evolutionary target in Trichoderma spp., a conclusion supported by the RCA data. Our results indicate that, for industrial use, it would be beneficial to combine loop motifs from TatCel7A with the thermostability features of TreCel7A. Furthermore, one region implicated in thermal unfolding is suggested as a primary target for protein engineering.

Electronic supplementary material
The online version of this article (10.1186/s13068-017-1006-7) contains supplementary material, which is available to authorized users.

KEYWORDS

Cellobiohydrolase, Trichoderma atroviride, Trichoderma harzianum, Trichoderma reesei, Cellulase engineering

Title

Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Author

Anna S. Borisova,1,2 Elena V. Eneyskaya,2 Suvamay Jana,3 Silke F. Badino,4 Jeppe Kari,4 Antonella Amore,5 Magnus Karlsson,6 Henrik Hansson,1 Mats Sandgren,1 Michael E. Himmel,5 Peter Westh,4 Christina M. Payne,corresponding author3,8 Anna A. Kulminskaya,corresponding author2,7 and Jerry Stahlbergcorresponding author1

Publish date

2018

PMID

20070850

Abstract

Parkinson disease (PD) is a chronic neurodegenerative disorder with a cumulative prevalence of greater than one per thousand. To date three independent genome-wide association studies (GWAS) have investigated the genetic susceptibility to PD. These studies have also implicated several genes as PD risk loci with strong, but not genome-wide significant, associations.

In this study, we combined data from two previously published GWAS of Caucasian subjects with our GWAS of 604 cases and 619 controls for a joint analysis with a combined sample size of 1752 cases and 1745 controls. SNPs in SNCA (rs2736990, p-value = 6.7×10−8; genome-wide adjusted p = 0.0109, odds ratio (OR) = 1.29 [95% CI: 1.17-1.42] G vs. A allele, population attributable risk percent (PAR%) = 12%) and the MAPT region (rs11012, p-value = 5.6×10−8; genome-wide adjusted p = 0.0079, OR = 0.70 [95% CI: 0.62-0.79] T vs. C allele, PAR% = 8%) were genome-wide significant. No other SNPs were genome-wide significant in this analysis. This study confirms that SNCA and the MAPT region are major genes whose common variants are influencing risk of PD

KEYWORDS

Parkinson disease, Association study, Alpha-synuclein, Microtubule associated protein tau

Title

Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease

Author

Todd L. Edwards,1 William K. Scott,1 Cherylyn Almonte,1 Amber Burt,1 Eric H. Powell,1 Gary W. Beecham,1 Liyong Wang,1 Stephan Zuchner,1 Ioanna Konidari,1 Gaofeng Wang,1 Carlos Singer,3 Fatta Nahab,3 Burton Scott,4 Jeffrey M. Stajich,4 Margaret Pericak-Vance,1 Jonathan Haines,2 Jeffery M. Vance,1 and Eden R. Martin1

Publish date

2011 Mar 1.

PMID

30397526

Abstract

The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 a resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.

KEYWORDS

single particle analysis, high-resolution cryo-electron microscopy, structural biology, cytochrome c nitrite reductase

Title

Three-Dimensional Structure of Cytochrome c Nitrite Reductase As Determined by Cryo-Electron Microscopy

Author

T. N. Baymukhametov, Y. M. Chesnokov, E. B. Pichkur, K. M. Boyko, T. V. Tikhonova, A. G. Myasnikov, A. L. Vasiliev, A. V. Lipkin, V. O. Popov, and M. V. Kovalchuk

Publish date

2018 Jul-Sep;


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