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Bombykol Sale

(Synonyms: (E,Z)-10,12-十六碳烯醇,Isobombycol) 目录号 : GC60093

Bombykol是第一个昆虫性信息素,是雌性蚕蛾Bombyxmori产生的性引诱剂。

Bombykol Chemical Structure

Cas No.:765-17-3

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5mg
¥585.00
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产品描述

Bombykol, the first insect sex pheromone, is identified as the female-produced sex attractant of the silkworm moth Bombyx mori[1][2][3].

[1]. Yasumasa KUWAHARA, et al. Flight Time of Bombyx mandarina Males to a Pheromone Trap Baited with Bombykol. J-STAGE home/Applied Entomology and Zoology/Volume 19 (1984) Issue 3. [2]. Yasumasa KUWAHARA, et al. Evaluation of Bombykol as the Sex Pheromone of Bombyx mandarina(Lepidoptera : Bombycidae). J-STAGE home/Applied Entomology and Zoology/Volume 19 (1984) Issue 2. [3]. Bombykol.

Chemical Properties

Cas No. 765-17-3 SDF
别名 (E,Z)-10,12-十六碳烯醇,Isobombycol
Canonical SMILES CCC/C=C\C=C\CCCCCCCCCO
分子式 C16H30O 分子量 238.41
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1 mM 4.1945 mL 20.9723 mL 41.9445 mL
5 mM 0.8389 mL 4.1945 mL 8.3889 mL
10 mM 0.4194 mL 2.0972 mL 4.1945 mL
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Research Update

A Bombykol electrochemical receptor sensor and its kinetics

Bioelectrochemistry 2019 Aug;128:263-273.PMID:31051432DOI:10.1016/j.bioelechem.2019.04.009.

This study aimed to explore the interaction between Bombykol and BmOR1 and also provide a paradigm for agroforestry pest control. The electrochemical biosensor signal amplification system was used: nanogold with horseradish peroxidase. An electrochemical bilayer nanogold membrane receptor sensor was developed using the following schemes and processes: twice self-assembly of nanogold and succeeding absorption of Bombyx mori olfactory receptor 1 (BmOR1); sex pheromone-binding protein; spectral scanning and transmission electron microscope to characterize nanogold sol; and atomic force microscope, cyclic voltammetry, and AC impedance methods to characterize individual processes of sensor assembly. The amperometric I-T curve was adopted to measure the response current upon interaction with different concentrations of Bombykol (diluted in phosphate-buffered saline) and BmOR1. The results demonstrated the receptor-ligand interaction pattern, which was similar to enzymatic reaction kinetics, with the activation constant Ka of up to 8.57 × 10-20 mol/L and signal magnification of about 10,000-fold. In this study, the simulation of intracellular receptor signaling cascade by an electrochemical signal amplification system helped in directly measuring BmOR1-bombykol ligand interaction and exploring the kinetics after the self-assembly of BmOR1 on the biosensor. It provided a novel platform for future studies on receptor-ligand interaction.

Study on Bombykol Receptor Self-Assembly and Universality of G Protein Cellular Signal Amplification System

ACS Sens 2019 Jan 25;4(1):257-264.PMID:30618240DOI:10.1021/acssensors.8b01446.

The G protein cascade amplification system couples with several receptors to sense/amplify the cellular signal, implying universal application. In order to explore whether GPCRs can trigger G protein signal amplification in tissues/cells from different species, Bombykol receptor was isolated and purified from antennas of male Bombyx mori, which subsequently self-assembled on the cell membrane in rat taste buds/rat vomeronasa/catfish tentacles/taste bud tissues of rabbits/pig/cattle in those lacking endogenous Bombykol receptor, followed by immobilization between two sheets of nucleopore membranes fixed by sodium alginate-starch gel, forming the sandwich-type sensing membrane, which in turn was immobilized on the glass-carbon electrode. Thus, Bombykol receptor sensors were established with different tissues. The response current of Bombykol receptor sensor toward Bombykol was measured with an electrochemical workstation. Every Bombykol receptor sensor could sense Bombykol based on enzyme-substrate kinetics. The double reciprocal plot and the activation constant values of Bombykol receptor sensors assembled with rat taste buds, rat vomeronasa, catfish tentacles, rabbit taste buds, pig taste buds, and cattle taste buds were calculated. Approximately 2-3 receptors could trigger the G protein cascade amplification system and achieve the maximum signal output. Moreover, the detection lower limit indicated that the Bombykol receptor self-assembled on the cell membranes of different tissues that transmitted and amplified the Bombykol signal with hypersensitivity. Also, cattle taste bud tissues served as an ideal system for heterogeneous GPCRs self-assembly and signal sensing/amplification. This sensing technique and method had promising potential in studies of biological pest control, sex pheromone detection, and receptor structure and function.

Bombykol receptors in the silkworm moth and the fruit fly

Proc Natl Acad Sci U S A 2010 May 18;107(20):9436-9.PMID:20439725DOI:10.1073/pnas.1003881107.

Male moths are endowed with odorant receptors (ORs) to detect species-specific sex pheromones with remarkable sensitivity and selectivity. We serendipitously discovered that an endogenous OR in the fruit fly, Drosophila melanogaster, is highly sensitive to the sex pheromone of the silkworm moth, Bombykol. Intriguingly, the fruit fly detectors are more sensitive than the receptors of the silkworm moth, although its ecological significance is unknown. By expression in the "empty neuron" system, we identified the fruit fly bombykol-sensitive OR as DmelOR7a (= DmOR7a). The profiles of this receptor in response to Bombykol in the native sensilla (ab4) or expressed in the empty neuron system (ab3 sensilla) are indistinguishable. Both WT and transgenic flies responded with high sensitivity, in a dose-dependent manner, and with rapid signal termination. In contrast, the same empty neuron expressing the moth Bombykol receptor, BmorOR1, demonstrated low sensitivity and slow signal inactivation. When expressed in the trichoid sensilla T1 of the fruit fly, the neuron housing BmorOR1 responded with sensitivity comparable to that of the native trichoid sensilla in the silkworm moth. By challenging the native Bombykol receptor in the fruit fly with high doses of another odorant to which the receptor responds with the highest sensitivity, we demonstrate that slow signal termination is induced by overdose of a stimulus. As opposed to the empty neuron system in the basiconic sensilla, the structural, biochemical, and/or biophysical features of the sensilla make the T1 trichoid system of the fly a better surrogate for the moth receptor.

Pheromonal activities of the Bombykol isomer, (10E,12E)-10,12-hexadecadien-1-ol, in the pheromone gland of the silkmoth Bombyx mori

J Insect Physiol 2020 Feb-Mar;121:104018.PMID:31987809DOI:10.1016/j.jinsphys.2020.104018.

Bombykol (EZ) is the single component of the female sex pheromone in the silkmoth Bombyx mori. EZ alone evokes full courtship behaviors from conspecific males; however, its geometric isomer (EE) was consistently detected in the pheromone glands (PG) of 16 B. mori strains and a field population of the wild silkmoth Bombyx mandarina, which also uses EZ as the single pheromone component. We investigated the pheromonal activities of EE using a commercial hybrid strain of B. mori, Kinshu × Showa. The behavioral assay demonstrated that a 104-105-fold higher dose of EE than EZ was able to elicit behavioral responses from males. To elucidate whether the trace contaminant of EZ in the EE standard is responsible for these responses, we examined the responses of male antennae to EE using a gas chromatograph-electroantennographic detector system (GC-EAD). The EE, at high doses elicited marginal responses from the male antennae. We next examined antennal and behavioral responses of B. mori whose BmOR1 gene, which is responsible for the reception of Bombykol, was knocked out. The knockout of BmOR1 resulted in the complete loss of antennal and behavioral responses to EE and EZ, demonstrating that if EE itself is active, it induces these responses via the incidental stimulation of BmOR1, not via the stimulation of EE-specific receptors. The existence of EE in the PG of B. mori and B. mandarina is discussed from the viewpoints of pheromone biosynthesis and the evolution of pheromone communication systems.

Molecular mechanisms underlying sex pheromone production in the silkmoth, Bombyx mori: characterization of the molecular components involved in Bombykol biosynthesis

J Insect Physiol 2007 Aug;53(8):752-9.PMID:17448494DOI:10.1016/j.jinsphys.2007.02.014.

Many species of female moths produce sex pheromones to attract conspecific males. To date, sex pheromones from more than 570 moth species have been chemically identified. Most moth species utilize Type I pheromones that consist of straight-chain compounds 10-18 carbons in length with a functional group of a primary alcohol, aldehyde, or acetate ester and usually with several double bonds. In contrast, some moth species use unsaturated hydrocarbons or hydrocarbon epoxides, classified as Type II lepidopteran pheromones, as sex pheromones. Studies over the past three decades have demonstrated that female moths usually produce sex pheromones as multi-component blends where the ratio of the individual components is precisely controlled, thus making it possible to generate species-specific pheromone blends. As for the biosynthesis of Type I pheromones, it is well established that they are de novo synthesized in the pheromone gland (PG) through modifications of fatty acid biosynthetic pathways. However, as many of the molecular components within the PG cells (i.e., enzymes, proteins, and small regulatory molecules) have not been functionally characterized, the molecular mechanisms underlying sex pheromone production in PG cells remain poorly understood. To address this, we have recently characterized some of the molecules involved in the biosynthesis of the sex pheromone Bombykol in the silkmoth, Bombyx mori. Characterization of these, and other, key molecules will facilitate our understanding of the precise mechanisms underlying lepidopteran sex pheromone production.