K6 diUb-VME
a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) based on K6 linked diUb
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, MS, NMR, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C, solution at −80°C. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€350.00
- Description
- Additional information
- references
Description
UbiQ-081 (K6 linked di-Ubiquitin VME) is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) based on K6 linked diUb.
This DUB activity based probe can be used for activity profiling experiments and structural studies. Lys6 has been replaced by a diaminobutyric acid(vinylamide) residue as reactive mimic of the native isopeptidic linked Lys(Gly) residue.
Please note the native distance between the proximal and distal Ubiquitin is preserved as much as possible in our diUbiquitin probe.
Additional information
| Weight | 0.05 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, MS, NMR, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C, solution at −80°C. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
Misaghi, S., et al. Structure of the Ubiquitin Hydrolase UCH-L3 Complexed with a Suicide Substrate. J. Biol. Chem. 280, 1512-1520 (2005).
http://www.ncbi.nlm.nih.gov/pubmed/15531586
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
Altun, M., et al. Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes. Chem. Biol. 18, 1401-1412 (2011).
http://www.ncbi.nlm.nih.gov/pubmed/22118674
Mulder, M.P., et al. A native chemical ligation handle that enables the synthesis of advanced activity-based probes: diubiquitin as a case study. ChemBiochem 15, 946-949 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24623714
Haj-Yahya, N., et al. Dehydroalanine-based diubiquitin activity probes. Org. Lett. 16, 540-543 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24364494
Li, G., et al. Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes. Chem. Commun. 20, 216-218 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24225431
Iphöfer, A., et al. Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes. Chembiochem 13, 1416-1420 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/22689415
McGouran, J.F., et al. Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes. Chem. Biol. 20, 1447-1455 (2013).
http://www.ncbi.nlm.nih.gov/pubmed/24290882