Protein Analysis
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  • 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