HA-Ahx-Ahx-Ub-VS
a potent and specific inhibitor of deubiquitinating enzymes (DUBs), labeled with HA on the N-terminus
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Purification, Western Blot, Phenotypic protein profiling, DUB activity profiling |
| target | |
| source | |
| shipping | |
| purity | |
| storage | upon arrival, powder at −20°C; buffered solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€200.00
- Description
- Additional information
- references
Description
HA-Ahx-Ahx-Ub-VS (UbiQ-187) is a potent and specific inhibitor of deubiquitinating enzymes (DUBs) based on a C-terminal electrophilic vinyl sulfone (VS) group. UbiQ-187 can be used for activity profiling experiments and determining DUB inhibitor specificity. UbiQ-187 contains an N-terminal HA-tag (YPYDVPDYA), which is a peptide sequence derived from the influenza hemagglutinin protein and allows for the sensitive identification or purification by anti-HA antibodies and/or anti-HA-agarose. The HA tag is separated from the Ub N-terminus by two aminohexanoic acid (Ahx) linkers for efficient recognition of the tag. To eliminate Met1 oxidation, Met1 is replaced by norleucine, a well validated Met mimic.
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Purification, Western Blot, Phenotypic protein profiling, DUB activity profiling |
| target | |
| source | |
| shipping | |
| purity | |
| storage | upon arrival, powder at −20°C; buffered solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
Galardy, P., et al. Mechanism-based proteomics tools based on ubiquitin and ubiquitin-like proteins: crystallography, activity profiling, and protease identification. Methods in Enzymology. 399, 120-131 (2005).
http://www.ncbi.nlm.nih.gov/pubmed/16338352
de Jong, A., et al. Ubiquitin-based probes prepared by total synthesis to profile the activity of deubiquitinating enzymes. ChemBiochem 13, 2251-2258 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/23011887
Wrigley, J.D. et al. Enzymatic characterisation of USP7 deubiquitinating activity and inhibition. Cell Biochem. Biophys. 60, 99-111 (2011)
http://www.ncbi.nlm.nih.gov/pubmed/21468692