Soltec Ventures Logo
 

"We React"

Soltec Ventures

office (978) 922-9446
  fax (978) 922-1666
sales@soltecventures.com

Protein Modification Reagents                      TCEP

 

Economically equivalent, odor free reductions at DTT prices . Available in large quantities with very high purity and stability. In addition, Soltec Ventures offers a TCEP stable solution. The solution is 0.5M and stable at room temperature under inert atmosphere.

Unit Price
1gm $22.00
2gm $30.00
5gm $52.00
10gm $95.00
25gm $230.00
  Download***Certificate of Analysis***

M115     Tris(2-carboxyethyl)phosphine hydrochloride, TCEP

                                     f.w.: 286.6daltons     [ 51805-45-9 ]

TCEP

 

 

 

 

 

Stability!
  • Odorless and non-volatile
  • Solid is stable in air for several months
  • Dilute TCEP solutions in air show no appreciable oxidation up to at least 72 hours pH<7.66

Solubility!

    310g/l in water

Reactivity!
  • TCEP reduces organic disulfides to thiols rapidly and quantitatively in water
  • More complete reductions than 1,4-dithiothreitol ( DTT ), Cleland's reagent
  • Even very stable alkyl disulfides are completely reduced at room temperature and pH 5 in less than 5 min.
  • Dilute (1mM) TCEP solutions react rapidly at room temperature
  • The strength of the phosphorus-oxygen bond makes the reaction irreversible
  • Kinetics rather than thermodynamics controls the reduction

Selectivity!

  • TCEP is selective for disulfides
  • TCEP does not react with other functional groups on proteins
  • Unreactive towards many common alkylating reagents so reductions have been carried out simultaneously with alkylations

    TCEP References:
  1. K. C., Dixon, J.E., Anal. Biochem, 161, 524-528 (1987).
  2. Schonberg, A., Chem Ber., 163-164 (1935).
  3. Rauhut, M., et. al., JACS, 81, 1103-1107 (1959).
  4. Chen, C.S., Fujimoto, Y, girdoukas, G., Sih, C.J., JACS, 109, 6825-6309 (1987).
  5. Kirley, T.L., Anal. Biochem, 180, 231-236 (1989).
  6. Andrews, P C., Dixon, J.E., Anal. Biochem., 161, 524-528 (1987).
  7. Y., Girdoukas, G.Sih, C.J., JACS, 109, 6825-6309 (1987).
  8. Houk, J., Whitesides, G.M., JACS, 109, 6825-6836 (1987).
  9. Grayson, M., Farley, C.E., Chimie Organique du Phophore, Collogues Int'l du Centre Nat'l de la Recherche Scientifique, No. 182  CNRS, Paris, 275-284 (1970).
  10. Overman, L.E., O'Conner, E.M., JACS, 98, 771-775 (1977).
  11. Rosenfield, R.E., Parthasarthy, R., Dunitis, J.D., JACS, 99, 4860-4862 (1977).
  12. Ruegg, U.T. and Rudinger, J., Methods Enzymology, 47, 111-126, (1977).
  13. Burns, J.A., et al, J. Org. Chem, 56, 2648-2650, (1991).
  14. Mery, J., et al,, Peptide Protein Research, 42, 44-52, (1993).
  15. Gray, W. R., Protein Science, 2, 1732-1748, (1993).
  16. Fisher, W.H., et al, Mass Spectrometry, 7, 225-228, (1993).
  17. Bieri, S, et al, Biochemistry, 34, 13059-13065, (1995).
  18. Tam, J., P,, et al, Proc. Natl Acad. Sci. USA, 92, 12485-12489, (1995).
  19. Blauenstein, P., et al, Eur. J. Nucl. Med., 22, 690-698 (1995).
  20. Gorman, J.J., et al, Rapid Communications Mass Spectrometry, 10, 529-536 (1996).
  21. Kiirsch, T., et al, Protein Expression Purification, 8, 75-84 (1996).
  22. Wu, J. and Watson, J.T., Protein Science, 6, 391-398 (1997).
  23. Bernard, C. L., et al, Exp. Brain Res., 113, 343-352 (1997).
  24. Huh, K. and Wenthold, R.J., Journal Biological Chemistry, 274, 151-151 (1999).
  25. Oda, Y. et al, Nature Biotech, 19, 379-382 (2001).