HA-Ahx-Ahx-Ub-VME
a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs), labeled with HA on the N-terminus
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | upon arrival powder at −20°C; solution at −80°C. Avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€220.00
- Description
- Additional information
- references
Description
UbiQ-035 (HA-Ahx-Ahx-Ub-VME) is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) that is prepared by chemical synthesis. It is N-terminally tagged with an HA-tag. The HA peptide sequence (YPYDVPDYA) is derived from the influenza hemagglutinin protein and allows for the sensitive identification or purification of DUBs since it is specifically recognized 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.
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | upon arrival powder at −20°C; solution at −80°C. Avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
El Oualid, F., et al. Chemical Synthesis of Ubiquitin, Ubiquitin-Based Probes, and Diubiquitin. Angewandte Chemie Int. Ed. 49, 10149-10153 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/21117055
Borodovsky, A., et al. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 20, 5187-5196 (2001).
http://www.ncbi.nlm.nih.gov/pubmed/11566882
Borodovsky, A., et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9, 1149-1159 (2002).
http://www.ncbi.nlm.nih.gov/pubmed/12401499
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