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Background
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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro.
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Background
References
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- Moynihan, T.P., et al., Genomics 51(1):124-127 (1998).
- Moynihan, T.P., et al., Mamm. Genome 7(7):520-525 (1996).
- Nuber, U., et al., J. Biol. Chem. 271(5):2795-2800 (1996).
- Robinson, P.A., et al., Mamm. Genome 6(10):725-731 (1995).
- Ardley, H.C., et al., Biochim. Biophys. Acta 1491 (1-3), 57-64 (2000).
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