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NEDD8-Vinyl Methyl Ester, human recombinant
Cat. # SI640
Background:
Application:
Interferon stimulated gene 15 (ISG15) is a member of the ubiquitin-like protein family whose
expression is increased following stimulation with type 1 Interferons. ISG15-VME is synthesized by
the conjugation of 4-amino-but-2-enoic acid methyl ester to the C-terminus of ISG15G156. Binding
of ISG15-VME by deISGenylases positions the reactive vinyl bond next to the sulfhydryl-group of the
active site cysteine. Nucleophilic attack by the sulfhydryl on the vinyl bond produces a stable,
covalent thioether linkage between ISG15 and the deISGenylase. Thus ISG15-VME is a potent
suicide inhibitor of deISGenylases.
This inhibitor is useful for labeling deISGenylases in situ as well as preserving the ISGenylated
proteins for analysis or purification.
Product Information
Purity:
> 95% by HPLC
Molecular Weight:
9100 Da by MS
Physical State:
Lyophilized powder
Quantity:
50 g
Solubility:
> 1 mg/mL in aqueous buffer
Storage:
Dry, -20 C. Solution, -80 C. Avoid repeated freeze/thaw cycles
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References
1)
Borodovsky A., et al. Small-molecule inhibitors and probes for ubiquitin- and ubiquitin-like-specific proteases. Chem. Biochem. 2005 6: p287291
2)
Hemelaar J., et al. Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Mol. Cell. Bio. 2004 24:
p84-95
3)
Gan-Erdene T., et al. Identification and characterization of DEN1, a deneddylase of the ULP family. J. Biol. Chem. 2003 278: p28892-28900
4)
Mendoza H.M., et al. NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins. J. Biol. Chem. 2003 278: p25637-25643
5)
Wang G., et al. Solid-phase synthesis of peptide vinyl sulfones as potential inhibitors and activity-based probes of cysteine proteases. Org.
Lett. 2003 5: p737-740
6)
Wu K., et al. DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. J.
Biol. Chem. 2003 278: p28882-288891
7)
Borodovsky A., et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 2002
9: p1149-1159
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