S-Glutathionylated Protein Detection Kit | Cayman Chemical
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S-Glutathionylated Protein Detection Kit

Item № 10010721
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     1 ea $300.00 0.00

Pricing updated 2018-08-14. Prices are subject to change without notice.

Description
Features
  • Direct visualization of S-glutathionylated proteins in whole (permeabilized) cells by flow cytometry and microscopy
  • Visualization using colorimetric or fluorescence detection
  • Reagents provided to test up to 30 samples
Synonyms
  • PSSG

Glutathione (GSH) is a tripeptide (γ-glutamylcysteinylglycine) widely distributed in both plants and animals.1,2 GSH is involved in maintenance of protein sulfhydryl reduction status.3,4 The concentration of GSH ranges from a few micromolar in plasma to several millimolar in tissues such as liver.5,6 Mixed protein glutathionyl disulfides are a post translational protein modification of growing interest.7,8,9 Protein S-glutathionylation (PSSG) may modify the activity of a large number of cell proteins, including metabolic, structural, cytoskeletal, and signaling proteins.10 PSSG detection methods can employ GSH adduct antibodies, GSH derivatives, and differential labeling systems based on the “Biotin-Switch” method.9,11,12 Cayman’s S-Glutathionylated Protein Detection Assay Kit provides a convenient method for the direct visualization of S-glutathionylated proteins in whole (permeabilized) cells by flow cytometry and microscopy as well as avidin overlay analysis.13 This cell-based assay starts with the modification of protein free-thiols groups followed by enzymatic cleavage of any protein-S-glutathione (PSSG) adducts present in the sample. Biotinylation of the newly-formed protein free-thiols provides the basis for visualization using streptavidin-based colorimetric or fluorescence detection. Reagents are provided to test three sets of 10 samples (most convenient) or up to thirty samples total at once if desired.

Needed but not supplied: Please download the kit booklet to verify if UltraPure Water (Milli-Q or equivalent) or any other components are needed for this assay.

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Technical Information
Synonyms
  • PSSG

Warning - this product is not for human or veterinary use.

Shipping & Storage
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
Stability
≥ 1 year
Downloads & Resources
Product Downloads

Download Kit Booklet

Download Safety Data Sheet (SDS)

Download free InChI Key generation software

Additional Information

View the Cayman Structure Database for chemical structure definitions for many Cayman products

Get Batch-Specific Data and Documents by Batch Number

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data pack, and GC-MS data.

References & Product Citations
Product Description References

1. Foyer, C.H., Lelandais, M., and Kunert, K.J. Photooxidative stress in plants. Physiologia Plantarum 92, 696-717 (1994).

2. Bedia, C. Glutathione: Metabolism and function. (1976).

3. Inoue, M., Saito, Y., Hirata, E., et al. Regulation of redox states of plasma proteins by metabolism and transport of glutathione and related compounds. Journal of Protein Chemistry 6, 207-225 (1987).

4. Inoue, M. Interorgan metabolism and membrane transport of glutathione and related compounds. Renal Biochemistry 225-269 (1985).

5. Lash, L.H., and Jones, D.P. Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma. Archives of Biochemistry and Biophysics 240, 583-592 (1985).

6. Wendel, A., and Cikryt, P. The level and half-life of glutathione in human plasma. FEBS Letters 120, 209-211 (1980).

7. Pompella, A., Visvikis, A., Paolicchi, A., et al. The changing faces of glutathione, a cellular protagonist. Biochemical Pharmacology 66, 1499-1503 (2003).

8. Cotgreave, I.A. Analytical developments in the assay of intra-and extracellular GSH homeostsis: Specific protein S-glutathionylation, cellular GSH and mixed disulphide compartmentalisation and interstitial GSH redox balance. BioFactors 17, 269-277 (2003).

9. Ying, J., Clavreul, N., Sethuraman, M., et al. Thiol oxidation in signaling and response to stress: Detection and quantification of physiological and pathophysiological thiol modifications. Free Radical Biology & Medicine 43, 1099-1108 (2007).

10. Dalle-Donne, I., Rossi, R., Colombo, G., et al. Protein S-glutathionylation: A regulatory device from bacteria to humans. Trends in Biochemical Sciences 34(2), 85-96 (2008).

11. Jaffrey, S.R., Erdjument-Bromage, H., Ferris, C.D., et al. Protein S-nitrosylation: A physiological signal for neuronal nitric oxide. Nature Cell Biology 3(2), 193-197 (2001).

12. Ckless, K., Reynaert, N.L., Taatjes, D.J., et al. In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: Identification of Ran GTPase as a target for S-nitrosylation. Nitric Oxide: Biology and Chemistry 11, 216-227 (2004).

13. Reynaert, N.L., Ckless, K., Guala, A.S., et al. In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization. Biochemica et Biophysica Acta 1760, 380-387 (2006).

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Ann Arbor, Michigan 48108 USA

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