11-cis Vaccenyl Acetate
目录号 : GC40730Male mating pheromone of D. melanogaster
Cas No.:6186-98-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
The mating and social behaviors of insects are largely orchestrated by a suite of volatile hydrocarbon pheromones. 11-cis Vaccenyl acetate is the male-specific mating pheromone of the fruit fly D. melanogaster. It acts selectively through the Or67d odorant receptor to control mating behavior in both male and female fruit flies.
| Cas No. | 6186-98-7 | SDF | |
| Canonical SMILES | CCCCCC/C=C\CCCCCCCCCCOC(=O)C | ||
| 分子式 | C20H38O2 | 分子量 | 310.5 |
| 溶解度 | DMF: 25 mg/ml,DMSO: 20 mg/ml,Ethanol: 30 mg/ml,PBS (pH 7.2): 2.5 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.2206 mL | 16.1031 mL | 32.2061 mL |
| 5 mM | 0.6441 mL | 3.2206 mL | 6.4412 mL |
| 10 mM | 0.3221 mL | 1.6103 mL | 3.2206 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Wake up and smell the pheromones
Neuron 2005 Jan 20;45(2):179-81.PMID:15664166DOI:10.1016/j.neuron.2005.01.001.
Odorant binding proteins (OBPs) are abundant proteins of unknown function expressed at high levels in insect and vertebrate chemosensory organs. In this issue of Neuron, Xu et al. show that Drosophila OBP76a is necessary for fruit flies to respond to the aggregation pheromone 11-cis Vaccenyl Acetate. The results suggest a mechanism by which this OBP is intimately involved in pheromone signal transduction.
Odor and pheromone detection in Drosophila melanogaster
Pflugers Arch 2007 Aug;454(5):749-58.PMID:17205355DOI:10.1007/s00424-006-0190-2.
Drosophila melanogaster has proven to be a useful model system to probe the mechanisms underlying the detection, discrimination, and perception of volatile odorants. The relatively small receptor repertoire of 62 odorant receptors makes the goal of understanding odor responses from the total receptor repertoire approachable in this system, and recent work has been directed toward this goal. In addition, new work not only sheds light but also raises more questions about the initial steps in odor perception in this system. Odorant receptor genes in Drosophila are predicted to encode seven transmembrane receptors, but surprising data suggest that these receptors may be inverted in the plasma membrane compared to classical G-protein coupled receptors. Finally, although some Drosophila odorant receptors are activated directly by odorant molecules, detection of a volatile pheromone, 11-cis Vaccenyl Acetate requires an extracellular adapter protein called LUSH for activation of pheromone sensitive neurons. Because pheromones are used by insects to trigger mating and other behaviors, these insights may herald new approaches to control behavior in pathogenic and agricultural pest insects.
Volatile pheromone signalling in Drosophila
Physiol Entomol 2012 Mar 1;37(1):10.1111/j.1365-3032.2011.00813.x.PMID:24347807DOI:10.1111/j.1365-3032.2011.00813.x.
Once captured by the antenna, 11-cis Vaccenyl Acetate (cVA) binds to an extracellular binding protein called LUSH that undergoes a conformational shift upon cVA binding. The stable LUSH-cVA complex is the activating ligand for pheromone receptors present on the dendrites of the aT1 neurones, comprising the only neurones that detect cVA pheromone. This mechanism explains the single molecule sensitivity of insect pheromone detection systems. The receptor that recognizes activated LUSH consists of a complex of several proteins, including Or67d, a member of the tuning odourant receptor family, Orco, a co-receptor ion channel, and SNMP, a CD36 homologue that may be an inhibitory subunit. In addition, genetic screens and reconstitution experiments reveal additional factors that are important for pheromone detection. Identification and functional dissection of these factors in Drosophila melanogaster Meigen should permit the identification of homologous factors in pathogenic insects and agricultural pests, which, in turn, may be viable candidates for novel classes of compounds to control populations of target insect species without impacting beneficial species.
Quantitative analysis of pheromone-binding protein specificity
Insect Mol Biol 2013 Feb;22(1):31-40.PMID:23121132DOI:10.1111/j.1365-2583.2012.01167.x.
Many pheromones have very low water solubility, posing experimental difficulties for quantitative binding measurements. A new method is presented for determining thermodynamically valid dissociation constants for ligands binding to pheromone-binding proteins, using β-cyclodextrin as a solubilizer and transfer agent. The method is applied to LUSH, a Drosophila odorant-binding protein that binds the pheromone 11-cis Vaccenyl Acetate (cVA). Refolding of LUSH expressed in Escherichia coli was assessed by measuring N-phenyl-1-naphthylamine (NPN) binding and Förster resonance energy transfer between LUSH tryptophan 123 (W123) and NPN. Binding of cVA was measured from quenching of W123 fluorescence as a function of cVA concentration. The equilibrium constant for transfer of cVA between β-cyclodextrin and LUSH was determined from a linked equilibria model. This constant, multiplied by the β-cyclodextrin-cVA dissociation constant, gives the LUSH-cVA dissociation constant: ∼100 nM. It was also found that other ligands quench W123 fluorescence. The LUSH-ligand dissociation constants were determined to be ∼200 nM for the silk moth pheromone bombykol and ∼90 nM for methyl oleate. The results indicate that the ligand-binding cavity of LUSH can accommodate a variety ligands with strong binding interactions. Implications of this for the Laughlin, Ha, Jones and Smith model of pheromone reception are discussed.
Odor-Specific Deactivation Defects in a Drosophila Odorant-Binding Protein Mutant
Genetics 2019 Nov;213(3):897-909.PMID:31492805DOI:10.1534/genetics.119.302629.
Insect odorant-binding proteins (OBPs) are a large, diverse group of low-molecular weight proteins secreted into the fluid bathing olfactory and gustatory neuron dendrites. The best-characterized OBP, LUSH (OBP76a) enhances pheromone sensitivity enabling detection of physiological levels of the male-specific pheromone, 11-cis Vaccenyl Acetate. The role of the other OBPs encoded in the Drosophila genome is largely unknown. Here, using clustered regularly interspaced short palindromic repeats/Cas9, we generated and characterized the loss-of-function phenotype for two genes encoding homologous OBPs, OS-E (OBP83b) and OS-F (OBP83a). Instead of activation defects, these extracellular proteins are required for normal deactivation of odorant responses to a subset of odorants. Remarkably, odorants detected by the same odorant receptor are differentially affected by the loss of the OBPs, revealing an odorant-specific role in deactivation kinetics. In stark contrast to lush mutants, the OS-E/F mutants have normal activation kinetics to the affected odorants, even at low stimulus concentrations, suggesting that these OBPs are not competing for these ligands with the odorant receptors. We also show that OS-E and OS-F are functionally redundant as either is sufficient to revert the mutant phenotype in transgenic rescue experiments. These findings expand our understanding of the roles of OBPs to include the deactivation of odorant responses.