CY5-N3
(Synonyms: Sulfo-Cyanine5-azide) 目录号 : GC30247
CY5-N3是一种Cy5-叠氮化物，是一种荧光染料。
Cas No.:1621101-43-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
CY5-N3 is a Cy5-azide, which is a fluorescent dye.
CY5-N3 can be used to monitor the CuAAC of branched DNA with Cy5-azide by HPLC[1].
[1]. Finke A, et al. Designer Extracellular Matrix Based on DNA-Peptide Networks Generated by Polymerase ChainReaction. Angew Chem Int Ed Engl. 2016 Aug 16;55(34):10136-40.
| Cas No. | 1621101-43-6 | SDF | |
| 别名 | Sulfo-Cyanine5-azide | ||
| Canonical SMILES | CC1(C)/C(N(C2=CC=C(S(=O)(O)=O)C=C21)CCCCCC(NCCCN=[N+]=[N-])=O)=C\C=C\C=C\C(C(C)(C3=CC(S(=O)([O-])=O)=CC=C43)C)=[N+]4CC | ||
| 分子式 | C36H46N6O7S2 | 分子量 | 738.92 |
| 溶解度 | DMSO : 25 mg/mL (33.83 mM) | 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 | 1.3533 mL | 6.7666 mL | 13.5333 mL |
| 5 mM | 0.2707 mL | 1.3533 mL | 2.7067 mL |
| 10 mM | 0.1353 mL | 0.6767 mL | 1.3533 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。
Programmed Synthesis by Stimuli-Responsive DNAzyme-Modified Mesoporous SiO2 Nanoparticles
DNAzyme-capped mesoporous SiO2 nanoparticles (MP SiO2 NPs) are applied as stimuli-responsive containers for programmed synthesis. Three types of MP SiO2 NPs are prepared by loading the NPs with Cy3-DBCO (DBCO=dibenzocyclooctyl), Cy5-N3 , and Cy7-N3 , and capping the NP containers with the Mg(2+) , Zn(2+) , and histidine-dependent DNAzyme sequences, respectively. In the presence of Mg(2+) and Zn(2+) ions as triggers, the respective DNAzyme-capped NPs are unlocked, leading to the "click" reaction product Cy3-Cy5. In turn, in the presence of Mg(2+) ions and histidine as triggers the second set of DNAzyme-capped NPs is unlocked leading to the Cy3-Cy7 conjugated product. The unloading of the respective NPs and the time-dependent formation of the products are followed by fluorescence spectroscopy (FRET). A detailed kinetic model for the formation of the different products is formulated and it correlates nicely with the experimental results.
A combination of metabolic labeling and 2D-DIGE analysis in response to a farnesyltransferase inhibitor facilitates the discovery of new prenylated proteins
Protein prenylation is a post-translational modification required for proper cellular localization and activity of many important eukaryotic proteins. Farnesyltransferase inhibitors (FTIs) have been explored extensively for their antitumor activity. To assist in identifying potentially new and more useful markers for therapeutic applications, we developed a strategy that uses a combination of metabolic labeling and 2D DIGE (differential gel electrophoresis) to discover new prenylated proteins whose cellular levels are influenced by FTIs. In this approach, metabolic labeling of prenylated proteins was first carried out with an alkyne-modified isoprenoid analog, C15Alk, in the presence or absence of the FTI L-744,832. The resulting alkyne-tagged proteins were then labeled with Cy3-N3 and Cy5-N3 and subjected to 2D-DIGE. Multiple spots having altered levels of labeling in presence of the FTI were observed. Mass spectrometric analysis of some of the differentially labeled spots identified several known prenylated proteins, along with HisRS, PACN-3, GNAI-1 and GNAI-2, which are not known to be prenylated. In vitro farnesylation of a C-terminal peptide sequence derived from GNAI-1 and GNAI-2 produced a farnesylated product, suggesting GNAI-1 and GNAI-2 are potential novel farnesylated proteins. These results suggest that this new strategy could be useful for the identification of prenylated proteins whose level of post-translational modification has been modulated by the presence of an FTI. Additionally, this approach, which decreases sample complexity and thereby facilitates analysis, should be applicable to studies of other post-translational modifications as well.