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1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 1036278-65-5 Structure
  • Basic information

    1. Product Name: 1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol
    2. Synonyms: 1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol
    3. CAS NO:1036278-65-5
    4. Molecular Formula:
    5. Molecular Weight: 622.91
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 1036278-65-5.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: 1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol(CAS DataBase Reference)
    10. NIST Chemistry Reference: 1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol(1036278-65-5)
    11. EPA Substance Registry System: 1,1,1-triphenyl-14,17,20,23-tetraoxa-2-thiapentacosan-25-ol(1036278-65-5)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 1036278-65-5(Hazardous Substances Data)

1036278-65-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1036278-65-5 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,0,3,6,2,7 and 8 respectively; the second part has 2 digits, 6 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 1036278-65:
(9*1)+(8*0)+(7*3)+(6*6)+(5*2)+(4*7)+(3*8)+(2*6)+(1*5)=145
145 % 10 = 5
So 1036278-65-5 is a valid CAS Registry Number.

1036278-65-5Relevant articles and documents

Functionalized polyethyleneimine-coated nano gold particle composite material and preparation method thereof

-

, (2021/10/02)

The invention relates to a functional polyethyleneimine coated nano-gold particle composite material and a preparation method thereof. The preparation method comprises the following steps: adding EDCand a hyperbranched polyethyleneimine solution into mPEG

SELF-POWERED ENZYME MICROPUMPS

-

, (2017/04/12)

Drug delivery devices, sensors, and micropumps provided herein can utilize a reaction of an analyte triggered by an enzyme to drive fluid flow. In some cases, a drug delivery device can include a reservoir including a drug (e.g., insulin) and have an enzyme (e.g., glucose oxidase) positioned adjacent to said reservoir. The enzyme can catalyze a reaction of said analyte to drive a fluid flow adjacent to said reservoir to increase a release of the drug from said reservoir. A sensor for an analyte can include an enzyme bound to a surface and a flow meter to detect a flow of fluids adjacent to said surface. A self-powered enzyme micropump provided herein can provide precise control over flow rate in response to specific signals.

Zwitterionic Ligands Bound to Cdse/Zns Quantum Dots Prevent Adhesion to Mammalian Cells

Landis, Ryan F.,Tang, Rui,Hou, Singyuk,Yazdani, Mahdieh,Lee, Yiwei,Rotello, Vincent M.

, p. 2302 - 2306 (2015/12/20)

Zwitterionic materials are useful tools in material science and biology as they provide high water solubility while preventing nonspecific interactions. Quantum dots (QDs) functionalized with zwitterionic and quaternary ammonium ligands were synthesized to investigate their interactions with the outer membrane of HeLa cells. Quaternary ammonium functionalized quantum dots adhered strongly to the cell surface while zwitterionic QDs had no cell adhesion. These results demonstrate that future noninteracting nanoparticles based on this design are possible.

Regulating exocytosis of nanoparticles via host-guest chemistry

Kim, Chaekyu,Tonga, Gulen Yesilbag,Yan, Bo,Kim, Chang Soo,Kim, Sung Tae,Park, Myoung-Hwan,Zhu, Zhengjiang,Duncan, Bradley,Creran, Brian,Rotello, Vincent M.

, p. 2474 - 2479 (2015/03/04)

Prolonged retention of internalized nanoparticulate systems inside cells improves their efficacy in imaging, drug delivery, and theranostic applications. Especially, regulating exocytosis of the nanoparticles is a key factor in the fabrication of effective nanocarriers for chemotherapeutic treatments but orthogonal control of exocytosis in the cellular environment is a major challenge. Herein, we present the first example of regulating exocytosis of gold nanoparticles (AuNPs), a model drug carrier, by using a simple host-guest supramolecular system. AuNPs featuring quaternary amine head groups were internalized into the cells through endocytosis. Subsequent in situ treatment of a complementary cucurbit[7]uril (CB[7]) to the amine head groups resulted in the AuNP-CB[7] complexation inside cells, rendering particle assembly. This complexation induced larger particle assemblies that remained sequestered in the endosomes, inhibiting exocytosis of the particles without any observed cytotoxicity. This journal is

Rapid and simple preparation of remarkably stable binary nanoparticle planet-satellite assemblies

Borsley, Stefan,Flook, Sarah,Kay, Euan R.

, p. 7812 - 7815 (2015/05/13)

We demonstrate a straightforward nonbiomolecular approach for self-assembly of binary NP planet-satellite superstructures, which display remarkable colloidal and structural stability under variations in temperature, pH, ionic strength and solvent. The rea

Reversible control of nanoparticle functionalization and physicochemical properties by dynamic covalent exchange

Della Sala, Flavio,Kay, Euan R.

, p. 4187 - 4191 (2015/03/31)

Existing methods for the covalent functionalization of nanoparticles rely on kinetically controlled reactions, and largely lack the sophistication of the preeminent oligonucleotide-based noncovalent strategies. Here we report the application of dynamic covalent chemistry for the reversible modification of nanoparticle (NP) surface functionality, combining the benefits of non-biomolecular covalent chemistry with the favorable features of equilibrium processes. A homogeneous monolayer of nanoparticle-bound hydrazones can undergo quantitative dynamic covalent exchange. The pseudomolecular nature of the NP system allows for the in situ characterization of surface-bound species, and real-time tracking of the exchange reactions. Furthermore, dynamic covalent exchange offers a simple approach for reversibly switching - and subtly tuning - NP properties such as solvophilicity.

Ligand conjugation of chemically exfoliated MoS2

Chou, Stanley S.,De, Mrinmoy,Kim, Jaemyung,Byun, Segi,Dykstra, Conner,Yu, Jin,Huang, Jiaxing,Dravid, Vinayak P.

, p. 4584 - 4587 (2013/05/22)

MoS2 is a two-dimensional material that is gaining prominence due to its unique electronic and chemical properties. Here, we demonstrate ligand conjugation of chemically exfoliated MoS2 using thiol chemistry. With this method, we modulate the ζ-potential and colloidal stability of MoS2 sheets through ligand designs, thus enabling its usage as a selective artificial protein receptor for β-galactosidase. The facile thiol functionalization route opens the door for surface modifications of solution processable MoS2 sheets.

Enzyme-amplified array sensing of proteins in solution and in biofluids

Miranda, Oscar R.,Chen, Hung-Ting,You, Chang-Cheng,Mortenson, David E.,Yang, Xiao-Chao,Bunz, Uwe H. F.,Rotello, Vincent M.

supporting information; experimental part, p. 5285 - 5289 (2010/06/18)

We have developed an enzyme-nanoparticle sensor array where the sensitivity is amplified through enzymatic catalysis. In this approach cationic gold nanoparticles are electrostatically bound to an enzyme (β-galactosidase, β-Gal), inhibiting enzyme activity. Analyte proteins release the β-Gal, restoring activity and providing an amplified readout of the binding event. Using this strategy we have been able to identify proteins in buffer at a concentration of 1 nM, substantially lower than current strategies for array-based protein sensing. Moreover, we have obtained identical sensitivity in studies where the proteins are spiked into the complex protein matrix provided by desalted human urine (~1.5 μM total protein; spiked protein concentrations were 0.067% of the overall protein concentration), demonstrating the potential of the method for diagnostic applications.

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