TAMRA-Ub-VME
a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs), labeled with TAMRA on the N-terminus
Additional information
| Weight | 0.005 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Solution at −80°C. Protect from light. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€250.00
- Description
- Additional information
- references
Description
TAMRA-Ub-VME (UbiQ-050) is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs), which is labeled on the N-terminus with a 5-carboxytetramethylrhodamine (TAMRA) dye. This ubiquitin-based activity probe can be used for activity profiling experiments and the control of DUB inhibitor specificity. Whereas the first-generation activity probes (such as HA tagged Ub-VME) require immunoblotting for detection, the second-generation TAMRA-Ub-VME probe allows detection of DUB labeling by in-gel fluorescence.
This direct and more sensitive read-out gives more distinct labeling patterns than can be achieved by immunoblotting. In addition, cross-reactivity of antibodies can lead to background labeling, something that is not observed with TAMRA-Ub-VME. Experimental details can be found in the open-access reference, see product sheet for details [de Jong et al].
Additional information
| Weight | 0.005 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Solution at −80°C. Protect from light. Please avoid multiple freeze/thaw cycles. |
| 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