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Sigma-Aldrich

S-Phenyl thioacetate

98%

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Linear Formula:
CH3COSC6H5
CAS Number:
Molecular Weight:
152.21
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22

assay

98%

form

liquid

refractive index

n20/D 1.57 (lit.)

bp

99-100 °C/6 mmHg (lit.)

density

1.124 g/mL at 25 °C (lit.)

storage temp.

2-8°C

SMILES string

CC(=O)Sc1ccccc1

InChI

1S/C8H8OS/c1-7(9)10-8-5-3-2-4-6-8/h2-6H,1H3

InChI key

WBISVCLTLBMTDS-UHFFFAOYSA-N

Related Categories

Application

S-Phenyl thioacetate was used as a substrate to measure the esterase activity.

wgk_germany

WGK 2

flash_point_f

closed cup

flash_point_c

closed cup


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Yu Yuan et al.
Journal of the American Chemical Society, 131(15), 5432-5437 (2009-04-22)
Described herein is the chemical synthesis of the Cys(29)-Gly(77) glycopeptide domain (22) of erythropoietin. Our initial ligation strategy targeted a C --> N termini condensation between glycopeptide 3 and peptide 4. However, the reaction was hindered by the "unattainable" reactivity
K Lorentz et al.
Clinica chimica acta; international journal of clinical chemistry, 308(1-2), 69-78 (2001-06-20)
Arylesterase (EC 3.1.1.2) activity in serum was specifically measured using thiophenyl acetate in a mechanized assay at 37 degrees C with 4-bromophenylboronic acid as inhibitor of cholinesterase and hexacyanoferrate-III as indicator. The systematic development of a routine method, apparent limitations
Anita Bosak et al.
Molecules (Basel, Switzerland), 25(1) (2020-01-18)
Mammalian paraoxonase-1 hydrolyses a very broad spectrum of esters such as certain drugs and xenobiotics. The aim of this study was to determine whether carbamates influence the activity of recombinant PON1 (rePON1). Carbamates were selected having a variety of applications:
D I Draganov et al.
The Journal of biological chemistry, 275(43), 33435-33442 (2000-08-10)
The paraoxonase gene family contains at least three members: PON1, PON2, and PON3. The physiological roles of the corresponding gene products are still uncertain. Until recently, only the serum paraoxonase/arylesterase (PON1) had been purified and characterized. Here we report the

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