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S-Phenylsulfonylcysteine Sale

(Synonyms: SPSC) 目录号 : GC41219

A thiol blocker for thiosulfonate switch technique

S-Phenylsulfonylcysteine Chemical Structure

Cas No.:97512-83-9

规格 价格 库存 购买数量
1mg
¥599.00
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5mg
¥2,707.00
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10mg
¥4,797.00
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25mg
¥10,502.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

S-Nitrosylation reactions regulate protein function and mediate nitrosative stress. S-Phenylsulfonylcysteine is a reagent for blocking thiol (-SH) groups on proteins and peptides at room temperature. This is the first step of the thiosulfonate switch technique, in which thiosulfonates are fluorescently tagged with a probe bearing a reactive thiol, such as rhodamine-SH.

Chemical Properties

Cas No. 97512-83-9 SDF
别名 SPSC
Canonical SMILES O=S(C1=CC=CC=C1)(SC[C@H](N)C(O)=O)=O
分子式 C9H11NO4S2 分子量 261.3
溶解度 DMF: 0.1 mg/ml,DMSO: 0.5 mg/ml,PBS (pH 7.2): 0.5 mg/ml 储存条件 Store at -20°C
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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。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 3.827 mL 19.1351 mL 38.2702 mL
5 mM 0.7654 mL 3.827 mL 7.654 mL
10 mM 0.3827 mL 1.9135 mL 3.827 mL
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Research Update

Conversion of S-Phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection

Org Biomol Chem 2014 Oct 28;12(40):7942-56.PMID:24986430DOI:PMC4365953

A three step protocol for protein S-nitrosothiol conversion to fluorescent mixed disulfides with purified proteins, referred to as the thiosulfonate switch, is explored which involves: (1) thiol blocking at pH 4.0 using S-Phenylsulfonylcysteine (SPSC); (2) trapping of protein S-nitrosothiols as their S-phenylsulfonylcysteines employing sodium benzenesulfinate; and (3) tagging the protein thiosulfonate with a fluorescent rhodamine based probe bearing a reactive thiol (Rhod-SH), which forms a mixed disulfide between the probe and the formerly S-nitrosated cysteine residue. S-Nitrosated bovine serum albumin and the S-nitrosated C-terminally truncated form of AdhR-SH (alcohol dehydrogenase regulator) designated as AdhR*-SNO were selectively labelled by the thiosulfonate switch both individually and in protein mixtures containing free thiols. This protocol features the facile reaction of thiols with S-phenylsulfonylcysteines forming mixed disulfides at mild acidic pH (pH = 4.0) in both the initial blocking step as well as in the conversion of protein-S-sulfonylcysteines to form stable fluorescent disulfides. Labelling was monitored by TOF-MS and gel electrophoresis. Proteolysis and peptide analysis of the resulting digest identified the cysteine residues containing mixed disulfides bearing the fluorescent probe, Rhod-SH.