Biotin-Ahx-Ub-Dha
an activity-based probe for Ub E1, E2 and (HECT/RBR) E3 ligases, labeled with biotin on the N-terminus
Additional information
| Weight | 0.005 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling, Target inhibitor profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C; solution at −80°C. Protect from light. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€300.00
- Description
- Additional information
- references
Description
Biotin-Ahx-Ub-Dha (UbiQ-102) is an activity-based probe for Ub E1, E2 and (HECT/RBR) E3 ligases. It is based on the Ub sequence in which the C-terminal Gly76 has been replaced by a dehydroalanine (Dha) residue. The N-terminus is labeled with biotin; an aminohexanoic acid (Ahx) linker is used to create extra space between the biotin and Ub protein for efficient access of biotin binding entities. It has been prepared by total chemical synthesis and is therefore well-defined in terms of biotinylation site. UbiQ-102 is processed in a native manner by Ub E1, E2 and (HECT/RBR) E3 ligases and during this process, it forms an electrophilic intermediate that can react with the active site Cys residue of the E1, E2 and (HECT/RBR) E3 enzyme, thereby creating a covalent bond.
Additional information
| Weight | 0.005 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, Pull down, Purification, Western Blot, Phenotypic protein profiling, Target inhibitor profiling |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C; solution at −80°C. Protect from light. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
Mulder et al., A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes. Nature Chem Bio (2016) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108872/