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Catalogue Number
AV-H24046
Analysis Method
HPLC,NMR,MS
Specification
98%
Storage
-20℃
Molecular Weight
591.77
Appearance
Powder
Botanical Source
Fritillaria walujewii Regel; Fritillaria pallidiflora Schrenk/ Alkaloid from Petilium eduardii (Liliaceae)
Structure Type
Alkaloids
Category
Standards;Natural Pytochemical;API
SMILES
CC1CCC2C(C3CCC4C(C3CN2C1)CC5C4CC(=O)C6C5(CCC(C6)OC7C(C(C(C(O7)CO)O)O)O)C)(C)O
Synonyms
(3β,5α)-20-Hydroxy-6-oxocevan-3-yl β-D-glucopyranoside/SipeiMine-3Beta-D-glucoside/Cevan-6-one, 3-(β-D-glucopyranosyloxy)-20-hydroxy-, (3β,5α)-/Edpetiline
IUPAC Name
(1R,2S,6S,9S,10S,11S,14S,15S,18S,20S,23R,24S)-10-hydroxy-6,10,23-trimethyl-20-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4-azahexacyclo[12.11.0.02,11.04,9.015,24.018,23]pentacosan-17-one
Applications
Edpetiline is a principal alkaloid from P. eduardi. Edpetiline has significant antiinflammatory effects[1].
Density
1.3±0.1 g/cm3
Solubility
Methanol; Water
Flash Point
403.0±32.9 °C
Boiling Point
742.7±60.0 °C at 760 mmHg
Melting Point
272-276℃ (methanol )
InChl
InChI=1S/C33H53NO8/c1-16-4-7-27-33(3,40)22-6-5-18-19(21(22)14-34(27)13-16)11-23-20(18)12-25(36)24-10-17(8-9-32(23,24)2)41-31-30(39)29(38)28(37)26(15-35)42-31/h16-24,26-31,35,37-40H,4-15H2,1-3H3/t16-,17-,18+,19+,20-,21-,22-,23-,24+,26+,27-,28+,29-,30+,31+,32+,33-/m0/s1
InChl Key
DHQFYEJMFMYGCV-RRIRULBESA-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#:32685-93-1) 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.
24089517
Endocannabinoid signaling has been implicated in modulating insulin release from β cells of the endocrine pancreas. β Cells express CB1 cannabinoid receptors (CB1Rs), and the enzymatic machinery regulating anandamide and 2-arachidonoylglycerol bioavailability. However, the molecular cascade coupling agonist-induced cannabinoid receptor activation to insulin release remains unknown. By combining molecular pharmacology and genetic tools in INS-1E cells and in vivo, we show that CB1R activation by endocannabinoids (anandamide and 2-arachidonoylglycerol) or synthetic agonists acutely or after prolonged exposure induces insulin hypersecretion. In doing so, CB1Rs recruit Akt/PKB and extracellular signal-regulated kinases 1/2 to phosphorylate focal adhesion kinase (FAK). FAK activation induces the formation of focal adhesion plaques, multimolecular platforms for second-phase insulin release. Inhibition of endocannabinoid synthesis or FAK activity precluded insulin release. We conclude that FAK downstream from CB1Rs mediates endocannabinoid-induced insulin release by allowing cytoskeletal reorganization that is required for the exocytosis of secretory vesicles. These findings suggest a mechanistic link between increased circulating and tissue endocannabinoid levels and hyperinsulinemia in type 2 diabetes.
Cannabinoid Receptors, Cytoskeleton, Endocannabinoids, Exocytosis, Focal Adhesion Kinase, Insulin Release
CB1 Cannabinoid Receptors Couple to Focal Adhesion Kinase to Control Insulin Release*
Katarzyna Malenczyk,‡§,1 Magdalena Jazurek,‡,2 Erik Keimpema,§,2 Cristoforo Silvestri,¶ Justyna Janikiewicz,‡ Ken Mackie,? Vincenzo Di Marzo,¶ Maria J. Redowicz,‡ Tibor Harkany,§**,3 and Agnieszka Dobrzyn‡,4
2013 Oct 2
2690996
The clinical immunobiology of interleukin-2: potential modified uses for improved cancer treatment.
S. D. Voss, G. Weil-Hillman, J. A. Hank, J. A. Sosman, and P. M. Sondel
1989 Jan
8643678
Recombination repair protein 1 (Rrp1) includes a C-terminal region homologous to several DNA repair proteins, including Escherichia coli exonuclease III and human APE, that repair oxidative and alkylation damage to DNA. The nuclease activities of Rrp1 include apurinic/apyrimidinic endonuclease, 3′-phosphodiesterase, 3′-phosphatase, and 3′-exonuclease. As shown previously, the C-terminal nuclease region of Rrp1 is sufficient to repair oxidative- and alkylation-induced DNA damage in repair-deficient E. coli mutants. DNA strand-transfer and single-stranded DNA renaturation activities are associated with the unique N-terminal region of Rrp1, which suggests possible additional functions that include recombinational repair or homologous recombination. By using the Drosophila w/w+ mosaic eye system, which detects loss of heterozygosity as changes in eye pigmentation, somatic mutation and recombination frequencies were determined in transgenic flies overexpressing wild-type Rrp1 protein from a heat-shock-inducible transgene. A large decrease in mosaic clone frequency is observed when Rrp1 overexpression precedes treatment with gamma-rays, bleomycin, or paraquat. In contrast, Rrp1 overexpression does not alter the spot frequency after treatment with the alkylating agents methyl methanesulfonate or methyl nitrosourea. A reduction in mosaic clone frequency depends on the expression of the Rrp1 transgene and on the nature of the induced DNA damage. These data suggest a lesion-specific involvement of Rrp1 in the repair of oxidative DNA damage.
Overexpression of a Rrp1 transgene reduces the somatic mutation and recombination frequency induced by oxidative DNA damage in Drosophila melanogaster.
A Szakmary, S M Huang, D T Chang, P A Beachy, and M Sander
1996 Feb 20