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  • Brand : BIOFRON

  • Catalogue Number : AV-H25200

  • Specification : 98%

  • CAS number : 94492-24-7

  • Formula : C31H38O16

  • Molecular Weight : 666.62

  • PUBCHEM ID : 21629996

  • Volume : 20mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystalline powder

Botanical Source

Cistanche deserticola Ma/Cistanches herba

Structure Type



Standards;Natural Pytochemical;API




2-(3,4-Dihydroxyphenyl)ethyl (4ξ)-2-O-acetyl-3-O-(6-deoxy-α-L-mannopyranosyl)-4-O-[(2E)-3-(3,4-dihydroxyphenyl)-2-propenoyl]-β-D-xylo-hexopyranoside/2'-Acetylacteoside/2-Acetylacteoside/2'-O-acetylverbascoside/β-D-xylo-Hexopyranoside, 2-(3,4-dihydroxyphenyl)ethyl 3-O-(6-deoxy-α-L-mannopyranosyl)-4-O-[(2E)-3-(3,4-dihydroxyphenyl)-1-oxo-2-propen-1-yl]-, 2-acetate, (4ξ)-


[(2R,3R,4S,5R,6R)-5-acetyloxy-6-[2-(3,4-dihydroxyphenyl)ethoxy]-2-(hydroxymethyl)-4-[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxyoxan-3-yl] (E)-3-(3,4-dihydroxyphenyl)prop-2-enoate


1.6±0.1 g/cm3


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

Flash Point

283.9±27.8 °C

Boiling Point

892.2±65.0 °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#:94492-24-7) 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.




The aim of the present work was to tackle the solubility issue of a biopharmaceutics classification system (BCS)-II drug, aceclofenac. Although a number of attempts to increase the aqueous solubility have been made, none of the methods were taken up for scale-up. Hence size reduction technique by a top-down approach using wet milling process was utilized to improve the solubility and, consequently, the dissolution velocity of aceclofenac. The quality of the final product was ensured by Quality by Design approach wherein the effects of critical material attributes and critical process parameters were assessed on the critical quality attributes (CQAs) of nanocrystals. Box-Behnken design was applied to evaluate these effects on critical quality attributes. The optimized nanocrystals had a particle size of 484.7±54.12 nm with a polydispersity index (PDI) of 0.108±0.009. The solid state characterization of the formulation revealed that the crystalline nature of the drug was slightly reduced after the milling process. With the reduced particle size, the solubility of the nanocrystals was found to increase in both water and 0.1 N HCl when compared with that of unmilled pure aceclofenac. These results were further supported by in vitro release studies of nanocrystals where an appreciable dissolution velocity with 100.07%±2.38% release was observed for aceclofenac nanocrystals compared with 47.66%±4.53% release for pure unmilled aceclofenac at the end of 2 h. The in vivo pharmacokinetic data generated showed a statistically significant increase in the Cmax for aceclofenac nanocrystals of 3.75±0.28 ?g/mL (for pure unmilled aceclofenac Cmax was 1.96±0.17 ?g/mL). The results obtained indicated that the developed nanocrystals of aceclofenac were successful in improving the solubility, thus the absorption and bioavailability of the drug. Hence, it may be a viable and cost-effective alternative to the current therapy.


aceclofenac, nanocrystals, ball milling, QbD, DoE, box-behnken design


A top-down technique to improve the solubility and bioavailability of aceclofenac: in vitro and in vivo studies


Reema Narayan,1 Abhyuday Pednekar,1 Dipshikha Bhuyan,1,2 Chaitra Gowda,1,3 KB Koteshwara,1 and Usha Yogendra Nayak1

Publish date





Though similar to those of herpesvirus saimiri and Epstein-Barr virus (EBV), the Kaposi’s sarcoma-associated herpesvirus (KSHV) genome features more splice genes and encodes many genes with bicistronic or polycistronic transcripts. In the present study, the gene structure and expression of KSHV ORF56 (primase), ORF57 (MTA), ORF58 (EBV BMRF2 homologue), and ORF59 (DNA polymerase processivity factor) were analyzed in butyrate-activated KSHV+ JSC-1 cells. ORF56 was expressed at low abundance as a bicistronic ORF56/57 transcript that utilized the same intron, with two alternative branch points, as ORF57 for its RNA splicing. ORF56 was transcribed from two transcription start sites, nucleotides (nt) 78994 (minor) and 79075 (major), but selected the same poly(A) signal as ORF57 for RNA polyadenylation. The majority of ORF56 and ORF57 transcripts were cleaved at nt 83628, although other nearby cleavage sites were selectable. On the opposite strand of the viral genome, colinear ORF58 and ORF59 were transcribed from different transcription start sites, nt 95821 (major) or 95824 (minor) for ORF58 and nt 96790 (minor) or 96794 (major) for ORF59, but shared overlapping poly(A) signals at nt 94492 and 94488. Two cleavage sites, at nt 94477 and nt 94469, could be equally selected for ORF59 polyadenylation, but only the cleavage site at nt 94469 could be selected for ORF58 polyadenylation without disrupting the ORF58 stop codon immediately upstream. ORF58 was expressed in low abundance as a monocistronic transcript, with a long 5′ untranslated region (UTR) but a short 3′ UTR, whereas ORF59 was expressed in high abundance as a bicistronic transcript, with a short 5′ UTR and a long 3′ UTR similar to those of polycistronic ORF60 and ORF62. Both ORF56 and ORF59 are targets of ORF57 and were up-regulated significantly in the presence of ORF57, a posttranscriptional regulator.

Kaposi’s sarcoma-associated herpesvirus (KSHV) is a B-lymphocyte-tropic γ-herpesvirus with a genome of ∼165 kb that can encode up to 90 viral proteins (21, 28, 33, 41). Despite its similarity to the organization of other γ-herpesvirus genomes, the KSHV genome is unique in having multiple regions with gene clusters and more split (splice) genes than any other herpesvirus (45). Considerable insight has been gained from recent studies on the structure and expression of individual genes in the KSHV genome, including the identification of ORF50/K8/K8.1 as a cluster gene locus in which all three genes share a common poly(A) signal but utilize alternative promoters and alternative RNA splicing to express each gene (20, 22, 30, 39, 40, 43). ORF73/72/K13 is another cluster gene locus in which all three genes initiate their transcription from the same promoter and polyadenylation from the same poly(A) signal but utilize alternative RNA splicing and translation initiation for the expression of each gene (1, 9, 14, 35, 38). ORF34/35/36/37 was also identified recently as a cluster gene locus that responds to hypoxia for transcription activation, and the hypoxia-induced polycistronic transcripts are presumably polyadenylated from a common poly(A) signal (12, 13).

Several elegant studies have succeeded in mapping and characterizing the transcription start sites of representative genes from the KSHV genome. However, we know little about the 3′ ends of their transcripts except that they are presumed to contain poly(A) signals because such signals are located 3′ to the individual open reading frames (ORFs). Where the transcription of most KSHV genes starts and ends remains largely unknown. In the course of studying KSHV ORF57 gene expression and looking for ORF57 targets, we extensively analyzed the gene structures and expression of four KSHV early genes: ORF56, ORF57, ORF58, and ORF59. KSHV ORF56 encodes a primase protein for viral DNA replication (42) and is positioned immediately upstream of ORF57 on the sense strand of the KSHV genome. KSHV ORF57 has been characterized as a posttranscriptional regulator of viral gene expression (10, 15, 23, 25), as well as a cooperative transcriptional regulator (15, 24). KSHV ORF58 encodes an Epstein-Barr virus BMRF2 homologue of unknown function (18) and is positioned side-by-side with KSHV ORF59 in the reverse direction on the antisense strand of KSHV genome. KSHV ORF59 encodes a viral DNA polymerase processivity factor involved in viral DNA replication (4, 5, 19). Some limited knowledge has been obtained about ORF57, but very little is known about the gene structures and expression of ORF56, ORF58, and ORF59 in the context of the KSHV genome. In this study, we combined all available techniques to precisely map the transcription start sites and polyadenylation sites as well as the expression levels of these genes. We found that KSHV ORF56 and ORF59 are transcribed as bicistronic RNA transcripts and are targets of KSHV ORF57.


Gene Structure and Expression of Kaposi's Sarcoma-Associated Herpesvirus ORF56, ORF57, ORF58, and ORF59?


Vladimir Majerciak, Koji Yamanegi, and Zhi-Ming Zheng*

Publish date

2006 Dec;




Antihypertensive treatment of patients with diabetes should include those drugs with a positive effect on metabolic parameters. Most patients with diabetes require at least two antihypertensive agents. Combining a dihydropyridine calcium channel blocker with a renin-angiotensin-aldosterone system inhibitor is a rational approach. However, not all dihydropyridines are equal with respect to their effects on metabolic parameters. Thus, manidipine exerts a positive effect on insulin resistance. However, this effect has not been observed with amlodipine. On the other hand, the excessive activation of sympathetic nervous system has been related with an increase of insulin resistance, pulse pressure, and ankle edema rates. Compared with amlodipine, manidipine activates sympathetic nervous system to a lesser extent. As a result, treatment with manidipine represents a good option in hypertensive patients with diabetes.


amlodipine, antihypertensive drug, calcium channel blocker, diabetes, hypertension, insulin resistance, manidipine, sympathetic nervous system


Manidipine: an antihypertensive drug with positive effects on metabolic parameters and adrenergic tone in patients with diabetes


Margarita SaizSatjes1 and Francisco Javier Martinez-Martin2

Publish date


Description :

2'-Acetylacteoside is a phenylethanoid glycoside isolated from Brandisia hancei, inhibits free radical-induced hemolysis of red blood cells and exhibits free radical scavenging activity[1].