Z-Rhodamine-SH

This S-nitrosothiol reactive dye can be used to attach the rhodamine fluorophore to proteins and peptides containing S-nitrosothiol modified cysteine residues.

Highlights:

  • Compatible with the Thiosulfonate Switch Technique (TST)
  • Solube in water

The thiosulfonate switch technique traps protein S-nitrosothiols as mixed disulfides bearing a fluorescent probe at pH 4.0. The protocol involves initial blocking of protein thiols by S-phenylsulfonylcysteine (SPSC), which forms cysteine bearing mixed disulfides. The byproduct of the initial blocking step is benzenesulfinate itself. Subsequent addition of PhSO2Na converts protein S-nitrosothiols into protein S-phenylthiosulfonates. Addition of a highly water soluble zwitterionic rhodamine based fluorophore incorporating a reactive thiol, denoted Z-Rhodamine-SH, reacts with protein S-phenylthiosulfonates, giving rise to a mixed disulfide between the probe and the formerly S-nitrosated cysteine residue.

Also available: S-phenylsulfonylcysteine (SPSC)

From the laboratory of Paul A. Grieco, PhD, Montana State University.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EMT025
Z-Rhodamine-SH
40ug (42nmol) In stock
Regular Price:$250.00
On Sale:
Specifications

Product Type: Small Molecule
Name: Z-Rhodamine-SH
Chemical Formula: C48H65N7O9S2
Molecular Weight: 948.21
Format: Pink powder
Purity: 95+% (NMR, HPLC)
Solubility: Good in water and polar organic solvents
Spectral Information: Excitation maximum: 562nmExtinction at max excitation: 86,000Emission maximum: 585nmFluorescence quantum yield: 0.07
Storage: -20C. Protect from light. Dessicate
Shipped: Cold packs

Provider
From the laboratory of Paul A. Grieco, PhD, Montana State University.
References
  1. Reeves BD, Joshi N, Campanello GC, Hilmer JK, Chetia L, Vance JA, Reinschmidt JN, Miller CG, Giedroc DP, Dratz EA, Singel DJ, Grieco PA.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.

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