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Desacetylcinobufagin

$687

  • Brand : BIOFRON

  • Catalogue Number : BD-P0671

  • Specification : 98.0%(HPLC)

  • CAS number : 4026-95-3

  • Formula : C24H32O5

  • Molecular Weight : 400.52

  • PUBCHEM ID : 11877495

  • Volume : 25mg

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Catalogue Number

BD-P0671

Analysis Method

HPLC,NMR,MS

Specification

98.0%(HPLC)

Storage

2-8°C

Molecular Weight

400.52

Appearance

Powder

Botanical Source

Structure Type

Steroids

Category

SMILES

CC12CCC(CC1CCC3C2CCC4(C35C(O5)C(C4C6=COC(=O)C=C6)O)C)O

Synonyms

Deacetylcinobufagin

IUPAC Name

5-[(1R,2S,4R,5R,6R,7R,10S,11S,14S,16R)-5,14-dihydroxy-7,11-dimethyl-3-oxapentacyclo[8.8.0.02,4.02,7.011,16]octadecan-6-yl]pyran-2-one

Applications

Density

1.3±0.1 g/cm3

Solubility

DMSO : ≥ 26 mg/mL (64.92 mM)
*"≥" means soluble, but saturation unknown.

Flash Point

208.1±25.0 °C

Boiling Point

601.9±55.0 °C at 760 mmHg

Melting Point

278-280ºC

InChl

InChI=1S/C24H32O5/c1-22-9-7-15(25)11-14(22)4-5-17-16(22)8-10-23(2)19(13-3-6-18(26)28-12-13)20(27)21-24(17,23)29-21/h3,6,12,14-17,19-21,25,27H,4-5,7-11H2,1-2H3

InChl Key

IXZHDDUFQVXHIL-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#:4026-95-3) 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

6575394

Abstract

Five integral plasma membrane glycoproteins (60, 80, 120, 140, and 160 kilodaltons) were isolated to homogeneity from rat liver by a four-step procedure: (i) extraction of plasma membranes with lithium diiodosalicylate, (ii) solubilization of glycoproteins with Nonidet P-40, (iii) affinity chromatography on concanavalin A-Sepharose, and (iv) semipreparative NaDodSO4/polyacrylamide gel electrophoresis. The glycoproteins contained 48.5–51.5% hydrophobic amino acids. Carbohydrate moieties contained N-acetyl-D-glucosamine, D-mannose, D-galactose, L-fucose, and N-acetylneuraminic acid. N-Acetyl-D-galactosamine was not detectable. Half-lives of degradation of the carbohydrate and protein moieties of the five glycoproteins were measured by pulse-chase experiments in vivo. Protein moieties had half-lives ranging from 52 to 88 hr in the five glycoproteins, with a mean of 73 +/- 15 hr. Terminal sugars, L-fucose, and N-acetylneuraminic acid had significantly shorter half-lives, averaging 18 +/- 2 hr and 29 +/- 3 hr, respectively. The half-life of D-mannose varied between that of the terminal sugars and that of the protein moiety, depending on the type of the glycoprotein. The data show that the carbohydrate moieties are degraded faster than the protein portion of the glycoproteins. As this finding was obtained in each of the five glycoproteins, intramolecular heterogeneity of breakdown may be a general characteristic of plasma membrane glycoproteins in liver.

Title

Intramolecular heterogeneity of degradation in plasma membrane glycoproteins: evidence for a general characteristic.

Author

R Tauber, C S Park, and W Reutter

Publish date

1983 Jul;

PMID

8526517

Abstract

A thermostable beta-galactosidase which catalyzed the production of galacto-oligosaccharide from lactose was solubilized from a cell wall preparation of Sterigmatomyces elviae CBS8119. The enzyme was purified to homogeneity by means of chromatography on DEAE-Toyopearl, Butyl-Toyopearl, Chromatofocusing, and p-aminobenzyl 1-thio-beta-D-galactopyranoside agarose columns. The molecular weight of the purified enzyme was estimated to be about 170,000 by gel filtration with a Highload-Superdex 200pg column and 86,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its isoelectric point, determined by polyacrylamide gel electrofocusing, was 4.1. The optimal temperature for enzyme activity was 85 degrees C. It was stable at temperatures up to 80 degrees C for 1 h. The optimal pH range for the enzyme was 4.5 to 5.0, it was stable at pH 2.5 to 7.0, and its activity was inhibited by Hg2+. The Km values for o-nitrophenyl-beta-D-galactopyranoside and lactose were 9.5 and 2.4 mM, respectively, and the maximum velocities for these substrates were 96 and 240 mumol/min per mg of protein, respectively. In addition, this enzyme possessed a high level of transgalactosylation activity. Galacto-oligosaccharides, including tri- and tetrasaccharides, were produced with a yield, by weight, of 39% from 200-mg/ml lactose.

Title

Purification and properties of a novel thermostable galacto-oligosaccharide-producing beta-galactosidase from Sterigmatomyces elviae CBS8119.

Author

N Onishi and T Tanaka

Publish date

1995 Nov;

PMID

2550811

Abstract

We have cloned the cellular sequence termed box DNA from the enhancer region of polyomavirus F9 mutant fPyF9. Box DNA functions as a negative transcriptional element (silencer) in undifferentiated F9 cells but not in differentiated L cells. Plasmid DNAs containing the origin and enhancer of polyomavirus were used to measure simultaneously transcriptional and replication activities in transfected cells. DNA replication activity was significantly reduced under conditions in which the silencer was able to reduce enhancer activity in F9 cells. On the other hand, when the silencer could not repress enhancer activity in MOP-8 cells, which are mouse NIH 3T3 cells producing polyomavirus T antigen constitutively, replication activity was still intact. The silencer itself had no effect on DNA replication or transcription in either type of cells. Furthermore, the insertion of a 6-base oligonucleotide within a consensus sequence of box DNA abolished the repressive effect of the silencer on DNA replication and enhancer activities. These results suggest that enhancer factors, interacting with silencer factors, may be closely associated with the mechanism of replication.

Title

Effect of silencer on polyomavirus DNA replication.

Author

K Ariizumi, H Takahashi, M Nakamura, and H Ariga

Publish date

1989 Sep;