Coelenterazine h
(Synonyms: 腔肠素-H,2-Deoxycoelenterazine; CLZN-h) 目录号 : GC43292A synthetic bioluminescent luciferin
Cas No.:50909-86-9
Sample solution is provided at 25 µL, 10mM.
Quality Control & SDS
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- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Coelenterazine is a luciferin, a light-emitting biomolecule that serves as a substrate for luciferases or as a constituent of photoproteins, including aequorin. Coelenterazine can be used to reconstitute the aequorin complex both in vivo and in vitro, emitting blue light when bound to calcium ions. Coelenterazine h is a synthetic derivative of native coelenterazine that exhibits 16-fold higher luminescence intensity (emission maximum ~466 nm; half-total time of 0.6-1.2 sec) than native coelenterazine. Aequorin complexes reconstituted with coelenterazine h are reported to be more sensitive to calcium ions than those employing the native constituent, providing a useful indicator for small changes in Ca2+ concentrations.
Cas No. | 50909-86-9 | SDF | |
别名 | 腔肠素-H,2-Deoxycoelenterazine; CLZN-h | ||
Canonical SMILES | OC1=CC=C(C2=CN3C(N=C(CC4=CC=CC=C4)C3=O)=C(CC5=CC=CC=C5)N2)C=C1 | ||
分子式 | C26H21N3O2 | 分子量 | 407.5 |
溶解度 | Ethanol: 0.5 mg/ml*,Methanol: 0.5 mg/ml* | 储存条件 | Store at -20°C ,protect from light |
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 | |||
1 mg | 5 mg | 10 mg | |
1 mM | 2.454 mL | 12.2699 mL | 24.5399 mL |
5 mM | 0.4908 mL | 2.454 mL | 4.908 mL |
10 mM | 0.2454 mL | 1.227 mL | 2.454 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。
An enzymatically-sensitized sequential and concentric energy transfer relay self-assembled around semiconductor quantum dots
Nanoscale 2015 May 7;7(17):7603-14.PMID:25804284DOI:10.1039/c5nr00828j.
The ability to control light energy within de novo nanoscale structures and devices will greatly benefit their continuing development and ultimate application. Ideally, this control should extend from generating the light itself to its spatial propagation within the device along with providing defined emission wavelength(s), all in a stand-alone modality. Here we design and characterize macromolecular nanoassemblies consisting of semiconductor quantum dots (QDs), several differentially dye-labeled peptides and the enzyme luciferase which cumulatively demonstrate many of these capabilities by engaging in multiple-sequential energy transfer steps. To create these structures, recombinantly-expressed luciferase and the dye-labeled peptides were appended with a terminal polyhistidine sequence allowing for controlled ratiometric self-assembly around the QDs via metal-affinity coordination. The QDs serve to provide multiple roles in these structures including as central assembly platforms or nanoscaffolds along with acting as a potent energy harvesting and transfer relay. The devices are activated by addition of Coelenterazine h substrate which is oxidized by luciferase producing light energy which sensitizes the central 625 nm emitting QD acceptor by bioluminescence resonance energy transfer (BRET). The sensitized QD, in turn, acts as a relay and transfers the energy to a first peptide-labeled Alexa Fluor 647 acceptor dye displayed on its surface. This dye then transfers energy to a second red-shifted peptide-labeled dye acceptor on the QD surface through a second concentric Förster resonance energy transfer (FRET) process. Alexa Fluor 700 and Cy5.5 are both tested in the role of this terminal FRET acceptor. Photophysical analysis of spectral profiles from the resulting sequential BRET-FRET-FRET processes allow us to estimate the efficiency of each of the transfer steps. Importantly, the efficiency of each step within this energy transfer cascade can be controlled to some extent by the number of enzymes/peptides displayed on the QD. Further optimization of the energy transfer process(es) along with potential applications of such devices are finally discussed.