Protein Analysis

Applications of IPL

Return to Peptide Ligation

Since IPL allows the fusion of synthetic peptides, as well as bacterially expressed proteins, with an N-terminal cysteine, to a protein expressed in the IMPACT system, IPL has been used in a variety of ways including:

  • The expression of cytotoxic proteins (1). 
  • The labeling of proteins with radioactive compounds as well as with synthetic peptides containing biotin or fluorescein (1-3). 
  • The study of protein-protein interactions (4). 
  • The generation of kinase substrates by varying the kinase recognition site at the protein level instead of at the DNA level (5, 6).
  •  The generation of phosphatase substrates (7).
  • The isotopic labeling of proteins for NMR analysis (8). 
  • Generation of substrates for protein arrays (9). 
  • Site specifically incorporating lipid moieties into a protein (10).

References

  1. Evans, T. et al. (1998) Protein Sci.7: 2256-2264. PMID: 9827992 
  2. Chong, S. et al. (1997) Gene 192: 271-281. PMID:  9224900
  3. Muir, T. et al. (1998) Proc. Natl. Acad. Sci. USA 95:6705-6710. PMID: 9618476 
  4. Severinov, K. et al. (1998) J. Biol. Chem. 273:16205-16209. PMID: 9632677 
  5. Ghosh, I. et al. (2004) J. of Imm. Methods. 293:85-95. PMID: 15541279 
  6. Xu, J., Sun, L., Ghosh, I., and Xu, M.-Q. (2004) Biotechniques. 36:976-998. PMID: 15211748 
  7. Kochinyan, S. et. al. (2007) Biotechniques 42(1): 63-9. PMID: 17269486 
  8. Xu, R. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 388-393. PMID: 9892643 
  9. Sun, L., et al. (2004) Biotechniques. 37: 430-443. PMID: 15470898
  10. Rak, A. et al. (2003) Science 302, 646-650. PMID: 14576435