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Background
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Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1), are structurally related to ubiquitin and can be ligated to target proteins in a similar manner as ubiquitin.1,2 However, covalent attachment of UBLs does not result in degradation of the modified proteins.. Like ubiquitin, UBLs are synthesized as precursor proteins, with 1 or more amino acids following the C-terminal glycine-glycine residues of the mature UBL protein. Thus, the tail sequences of the UBL precursors need to be removed by UBL-specific proteases such as SUMO1-specific protease 1 (SUSP1) prior to their conjugation to target proteins.
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Background
References
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- Bailey, D., et al., J. Biol. Chem. 279(1):692-703 (2004).
- Kim, K.I., et al., J. Biol. Chem. 275(19):14102-14106 (2000).
- Yeh, E.T., et al., Gene 248 (1-2), 1-14 (2000)
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