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Ginsenoside Rh4

$784

  • Brand : BIOFRON

  • Catalogue Number : BD-P0172

  • Specification : 95.0%(HPLC)

  • CAS number : 174721-08-5

  • Formula : C36H60O8

  • Molecular Weight : 620.9

  • PUBCHEM ID : 21599928

  • Volume : 25mg

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Catalogue Number

BD-P0172

Analysis Method

Specification

95.0%(HPLC)

Storage

-20℃

Molecular Weight

620.9

Appearance

Powder

Botanical Source

This product is isolated and purified from the roots of Panax ginseng C. A. Mey.

Structure Type

Category

SMILES

CC(=CCC=C(C)C1CCC2(C1C(CC3C2(CC(C4C3(CCC(C4(C)C)O)C)OC5C(C(C(C(O5)CO)O)O)O)C)O)C)C

Synonyms

β-D-Glucopyranoside, (3β,6α,12β,20E)-3,12-dihydroxydammara-20(22),24-dien-6-yl/(3β,6α,12β,20E)-3,12-Dihydroxydammara-20(22),24-dien-6-yl β-D-glucopyranosideGinsenoside Rh4

IUPAC Name

Applications

Planta Med. 1996 Feb;62(1):86-7. Ginsenoside Rh4, a genuine dammarane glycoside from Korean red ginseng.[Pubmed: 8720394]METHODS AND RESULTS:A genuine glycoside, named Ginsenoside Rh4, was isolated from Korean red ginseng (Panax ginseng C. A. Meyer) through repeated column chromatography, and its chemical structure was established to be 6-O-beta-D-glucopyranosyldammar-20(22),24-diene-3 beta,6 alpha,12 beta-triol by spectral and chemical methods. The stereochemistry of a double bond at C-20(22) of Ginsenoside Rh4 was characterized as (E) from a NOESY experiment in the 1H-NMR of the aglycone. CONCLUSIONS: Cytotoxic activities of Ginsenoside Rh4 and its aglycone against cancer cell lines were evaluated by use of the SRB method.

Density

1.2±0.1 g/cm3

Solubility

Methanol; Acetone; Ethyl Acetate

Flash Point

391.3±32.9 °C

Boiling Point

723.4±60.0 °C at 760 mmHg

Melting Point

InChl

InChl Key

OZTXYFOXQFKYRP-TXRYYSRHSA-N

WGK Germany

RID/ADR

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#:174721-08-5) 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

17400699

Abstract

The rat protein tyrosine phosphatase η, rPTPη, is a class I “classical” transmembrane RPTP, with an intracellular portion composed of a unique catalytic region. The rPTPη and the human homolog DEP-1 are downregulated in rat and human neoplastic cells, respectively. However, the malignant phenotype is reverted after exogenous reconstitution of rPTPη, suggesting that its function restoration could be an important tool for gene therapy of human cancers. Using small-angle x-ray scattering (SAXS) and biophysical techniques, we characterized the intracellular catalytic domain of rat protein tyrosine phosphatase η (rPTPηCD) in solution. The protein forms dimers in solution as confirmed by SAXS data analysis. The SAXS data also indicated that rPTPηCD dimers are elongated and have an average radius of gyration of 2.65 nm and a Dmax of 8.5 nm. To further study the rPTPηCD conformation in solution, we built rPTPηCD homology models using as scaffolds the crystallographic structures of RPTPα-D1 and RPTPμ-D1 dimers. These models were, then, superimposed onto ab initio low-resolution SAXS structures. The structural comparisons and sequence alignment analysis of the putative dimerization interfaces provide support to the notion that the rPTPηCD dimer architecture is more closely related to the crystal structure of autoinhibitory RPTPα-D1 dimer than to the dimeric arrangement exemplified by RPTPμ-D1. Finally, the characterization of rPTPηCD by fluorescence anisotropy measurements demonstrates that the dimer dissociation is concentration dependent with a dissociation constant of 21.6 ± 2.0 μM.

Title

Low-Resolution Structure and Fluorescence Anisotropy Analysis of Protein Tyrosine Phosphatase η Catalytic Domain

Author

Huita C. Matozo,* Maria A. M. Santos,* Mario de Oliveira Neto,* Lucas Bleicher,* Luis Mauricio T. R. Lima,† Rodolfo Iuliano,‡ Alfredo Fusco,§ and Igor Polikarpov*¶

Publish date

2007 Jun 15;

PMID

19440302

Abstract

Background
Methylotrophy describes the ability of organisms to grow on reduced organic compounds without carbon-carbon bonds. The genomes of two pink-pigmented facultative methylotrophic bacteria of the Alpha-proteobacterial genus Methylobacterium, the reference species Methylobacterium extorquens strain AM1 and the dichloromethane-degrading strain DM4, were compared.

Methodology/Principal Findings
The 6.88 Mb genome of strain AM1 comprises a 5.51 Mb chromosome, a 1.26 Mb megaplasmid and three plasmids, while the 6.12 Mb genome of strain DM4 features a 5.94 Mb chromosome and two plasmids. The chromosomes are highly syntenic and share a large majority of genes, while plasmids are mostly strain-specific, with the exception of a 130 kb region of the strain AM1 megaplasmid which is syntenic to a chromosomal region of strain DM4. Both genomes contain large sets of insertion elements, many of them strain-specific, suggesting an important potential for genomic plasticity. Most of the genomic determinants associated with methylotrophy are nearly identical, with two exceptions that illustrate the metabolic and genomic versatility of Methylobacterium. A 126 kb dichloromethane utilization (dcm) gene cluster is essential for the ability of strain DM4 to use DCM as the sole carbon and energy source for growth and is unique to strain DM4. The methylamine utilization (mau) gene cluster is only found in strain AM1, indicating that strain DM4 employs an alternative system for growth with methylamine. The dcm and mau clusters represent two of the chromosomal genomic islands (AM1: 28; DM4: 17) that were defined. The mau cluster is flanked by mobile elements, but the dcm cluster disrupts a gene annotated as chelatase and for which we propose the name “island integration determinant” (iid).

Conclusion/Significance
These two genome sequences provide a platform for intra- and interspecies genomic comparisons in the genus Methylobacterium, and for investigations of the adaptive mechanisms which allow bacterial lineages to acquire methylotrophic lifestyles.

Title

Methylobacterium Genome Sequences: A Reference Blueprint to Investigate Microbial Metabolism of C1 Compounds from Natural and Industrial Sources

Author

Stephane Vuilleumier,# 1 , * Ludmila Chistoserdova,# 2 , * Ming-Chun Lee, 3 Francoise Bringel, 1 Aurelie Lajus, 4 Yang Zhou, 5 Benjamin Gourion, 6 Valerie Barbe, 7 Jean Chang, 5 Stephane Cruveiller, 4 Carole Dossat, 7 Will Gillett, 5 Christelle Gruffaz, 1 Eric Haugen, 5 Edith Hourcade, 1 Ruth Levy, 5 Sophie Mangenot, 7 Emilie Muller, 1 Thierry Nadalig, 1 Marco Pagni, 8 Christian Penny, 1 Remi Peyraud, 6 David G. Robinson, 3 David Roche, 4 Zoe Rouy, 4 Channakhone Saenampechek, 5 Gregory Salvignol, 4 David Vallenet, 4 Zaining Wu, 5 Christopher J. Marx, 3 Julia A. Vorholt, 6 Maynard V. Olson, 5 , 9 , 10 Rajinder Kaul, 5 , 10 Jean Weissenbach, 4 Claudine Medigue, 4 and Mary E. Lidstrom 2 , 11

Publish date

2009

PMID

19014550

Abstract

Background
While increasing data on bacterial evolution in controlled environments are available, our understanding of bacterial genome evolution in natural environments is limited. We thus performed full genome analyses on four Listeria monocytogenes, including human and food isolates from both a 1988 case of sporadic listeriosis and a 2000 listeriosis outbreak, which had been linked to contaminated food from a single processing facility. All four isolates had been shown to have identical subtypes, suggesting that a specific L. monocytogenes strain persisted in this processing plant over at least 12 years. While a genome sequence for the 1988 food isolate has been reported, we sequenced the genomes of the 1988 human isolate as well as a human and a food isolate from the 2000 outbreak to allow for comparative genome analyses.

Results
The two L. monocytogenes isolates from 1988 and the two isolates from 2000 had highly similar genome backbone sequences with very few single nucleotide (nt) polymorphisms (1 – 8 SNPs/isolate; confirmed by re-sequencing). While no genome rearrangements were identified in the backbone genome of the four isolates, a 42 kb prophage inserted in the chromosomal comK gene showed evidence for major genome rearrangements. The human-food isolate pair from each 1988 and 2000 had identical prophage sequence; however, there were significant differences in the prophage sequences between the 1988 and 2000 isolates. Diversification of this prophage appears to have been caused by multiple homologous recombination events or possibly prophage replacement. In addition, only the 2000 human isolate contained a plasmid, suggesting plasmid loss or acquisition events. Surprisingly, besides the polymorphisms found in the comK prophage, a single SNP in the tRNA Thr-4 prophage represents the only SNP that differentiates the 1988 isolates from the 2000 isolates.

Conclusion
Our data support the hypothesis that the 2000 human listeriosis outbreak was caused by a L. monocytogenes strain that persisted in a food processing facility over 12 years and show that genome sequencing is a valuable and feasible tool for retrospective epidemiological analyses. Short-term evolution of L. monocytogenes in non-controlled environments appears to involve limited diversification beyond plasmid gain or loss and prophage diversification, highlighting the importance of phages in bacterial evolution.

Title

Short-term genome evolution of Listeria monocytogenes in a non-controlled environment

Author

Renato H Orsi,1 Mark L Borowsky,2,7 Peter Lauer,3 Sarah K Young,2 Chad Nusbaum,2 James E Galagan,2,4 Bruce W Birren,2 Reid A Ivy,1 Qi Sun,5 Lewis M Graves,6 Bala Swaminathan,6 and Martin Wiedmanncorresponding author1

Publish date

2008