H2A(5-21) K13Ub
an H2A(5-21) peptide which is modified at K13 via a native isopeptide bond with ubiquitin
Additional information
| Weight | 0.05 kg |
|---|---|
| Applications | Crystallization, Pull down, Western Blot, DUB activity profiling, Target inhibitor profiling |
| target | |
| source | human sequence, synthetic |
| shipping | |
| purity | |
| storage | upon arrival powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement | |
| aliquot size |
€250.00
- Description
- Additional information
- references
Description
UbiQ-172 is an H2A(5-21) peptide which is modified at K13 via a native isopeptide bond with ubiquitin (Ub). It can be used as a substrate for ubiquitin proteases, to investigate mechanism of binding and recognition by proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs (UIMs) and as antigen for immunizations.
Additional information
| Weight | 0.05 kg |
|---|---|
| Applications | Crystallization, Pull down, Western Blot, DUB activity profiling, Target inhibitor profiling |
| target | |
| source | human sequence, synthetic |
| shipping | |
| purity | |
| storage | upon arrival powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement | |
| aliquot size |
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
Faesen, A.C., et al. The Differential Modulation of USP Activity by Internal Regulatory Domains, Interactors and Eight Ubiquitin Chain Types. Chem. Biol. 18, 1550-1561 (2011).
http://www.ncbi.nlm.nih.gov/pubmed/22195557
Dikic, I., et al. Ubiquitin-binding domains – from structures to functions. Nat. Rev. Mol. Cell. Biol. 10, 659-671 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/19773779
Licchesi, J.D., et al. An ankyrin-repeat ubiquitin-binding domain determines TRABID’s specificity for atypical ubiquitin chains. Nat. Struct. Mol. Biol. 19, 62-71 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/22157957