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Eichlerianic acid


  • Brand : BIOFRON

  • Catalogue Number : BN-O1544

  • Specification : 98%(HPLC)

  • CAS number : 56421-13-7

  • Formula : C30H50O4

  • Molecular Weight : 474.7

  • PUBCHEM ID : 12315516

  • Volume : 5mg

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Catalogue Number


Analysis Method






Molecular Weight




Botanical Source

This product is isolated and purified from the twig of Dysoxylum lenticellatum

Structure Type



Standards;Natural Pytochemical;API




3,4-Secodammar-4(28)-en-3-oic acid, 20,24-epoxy-25-hydroxy-, (24S)-/1H-Benz[e]indene-6-propanoic acid, dodecahydro-6,9a,9b-trimethyl-7-(1-methylethenyl)-3-[(2S,5S)-tetrahydro-5-(1-hydroxy-1-methylethyl)-2-methyl-2-furanyl]-, (3S,3aR,5aR,6S,7S,9aR,9bR)-/3-{(3S,3aR,5aR,6S,7S,9aR,9bR)-3-[(2S,5S)-5-(2-Hydroxy-2-propanyl)-2-methyltetrahydro-2-furanyl]-7-isopropenyl-6,9a,9b-trimethyldodecahydro-1H-cyclopenta[a]naphthalen-6-yl}propanoic acid/Shoreic acid


3-[(3S,3aR,5aR,6S,7S,9aR,9bR)-3-[(2S,5S)-5-(2-hydroxypropan-2-yl)-2-methyloxolan-2-yl]-6,9a,9b-trimethyl-7-prop-1-en-2-yl-1,2,3,3a,4,5,5a,7,8,9-decahydrocyclopenta[a]naphthalen-6-yl]propanoic acid


1.0±0.1 g/cm3


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

Flash Point

174.3±22.2 °C

Boiling Point

568.3±45.0 °C at 760 mmHg

Melting Point



InChl Key


WGK Germany


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#:56421-13-7) 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.




Acylphosphatase can be converted in vitro, by addition of trifluoroethanol (TFE), into amyloid fibrils of the type observed in a range of human diseases. The propensity to form fibrils has been investigated for a series of mutants of acylphosphatase by monitoring the range of TFE concentrations that result in aggregation. We have found that the tendency to aggregate correlates inversely with the conformational stability of the native state of the protein in the different mutants. In accord with this, the most strongly destabilized acylphosphatase variant forms amyloid fibrils in aqueous solution in the absence of TFE. These results show that the aggregation process that leads to amyloid deposition takes place from an ensemble of denatured conformations under conditions in which non-covalent interactions are still favoured. These results support the hypothesis that the stability of the native state of globular proteins is a major factor preventing the in vivo conversion of natural proteins into amyloid fibrils under non-pathological conditions. They also suggest that stabilizing the native states of amyloidogenic proteins could aid prevention of amyloidotic diseases.


acylphosphatase/amyloid fibrils/conformational stability/protein engineering/protein misfolding


Mutational analysis of the propensity for amyloid formation by a globular protein


Fabrizio Chiti,1,2 Niccolò Taddei,3 Monica Bucciantini,3 Paul White,1 Giampietro Ramponi,3 and Christopher M. Dobson1,4

Publish date

2000 Apr 3;




Human Calcitonin (hCt) is a peptide hormone which has a regulatory action in calcium-phosphorus metabolism. It is currently used as a therapeutic tool in bone pathologies such as osteoporosis and Paget’s disease. However, due to its amphiphilic property tends to form a gelatinous solution in water which consists of fibrils that limits its therapeutic use. Here we show that sodium dodecyl sulfate (SDS), an anionic detergent able to induce and stabilize α-helices in polypeptides, at a monomeric concentration ranging between 0.26 mM-5 pM (all concentrations are below the CMC), increases the rate and number of hCt channel formation in planar lipid membranes, at both high and low hCt concentrations, with a maximum increase at a molecular hCt/SDS ratio of 1000:1. This effect could be interpreted as a counteraction to the fibrillation process of hCt molecules by removing molecules available for aggregation from the fluid; furthermore, this action, independently of channel formation in the cell membrane, could improve the peptide-receptor interaction. The action of SDS could be attributable to the strength of the sulfate negative charge and the hydrophobic chain; in fact, a similar effect was obtained with lauryl sarcosine and not with a neutral detergent such as n-dodecyl-β-d-maltoside. The very low molecular ratio between SDS and peptide is suggestive of a possible catalytic action of SDS that could induce α-helices, the appropriate structures for interacting with the membrane. Moreover, in the experimental conditions investigated, the addition of SDS does not modify the membrane’s electrical properties and most of the channel properties. This finding may contribute to the knowledge of environment-folding diseases due to protein and peptides.


Effect of Nanomolar Concentrations of Sodium Dodecyl Sulfate, a Catalytic Inductor of α-Helices, on Human Calcitonin Incorporation and Channel Formation in Planar Lipid Membranes


Silvia Micelli,* Daniela Meleleo,* Vittorio Picciarelli,† Maria G. Stoico,* and Enrico Gallucci*

Publish date

2004 Aug;




A high propensity to aggregate into intractable deposits is a common problem limiting the production and use of many peptides and proteins in a wide range of biotechnological and pharmaceutical applications. Many therapeutic polypeptides are frequently abandoned at an early stage in their development because of problems with stability and aggregation. It has been shown recently that parameters describing the physicochemical properties of polypeptides can be used as predictors of protein aggregation. Here we demonstrate that these and similar tools can be applied to the rational redesign of bioactive molecules with a significantly reduced aggregation propensity without loss of physiological activity. This strategy has been exemplified by designing variants of the hormone calcitonin that show a significantly reduced aggregation propensity, yet maintain, or even increase, their potency when compared to the current therapeutic forms. The results suggest that this approach could be used successfully to enhance the solubility and efficacy of a wide range of other peptide and protein therapeutics.


protein aggregation, protein design, biopharmaceuticals, amyloid, misfolding


Rational design of aggregation-resistant bioactive peptides: Reengineering human calcitonin


Susan B. Fowler,*† Stephen Poon,*† Roman Muff,†‡ Fabrizio Chiti,§ Christopher M. Dobson,*¶ and Jesús Zurdo*¶∥

Publish date

2005 Jul 19;

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