Poly-ubiquitylation of target proteins through linkage at K48, is now the most thoroughly studied of the various chain linkages, and we once considered the hallmark of this post-translational modification. It is now clear that many, if not all, poly-Ub chain topologies likely play distinct and important roles in regulating cellular processes. Nevertheless, K48 linkage remains a critical pathway for the cells to maintain homeostasis through proteolytic degradation, and as such remains very intriguing for the study of DUBs that play a role in the degradation, as well as the proteasome itself.
These diubiquitin chains generated from the enzymatic linkage of wild-type ubiquitin through lysine 48. The most distal ubiquitin contains an arginine substitution for the lysine at position 48, limiting chain length.
Info
| Source | Human recombinant |
| Form | Liquid |
| Molecular Weight | 17,139.7 Da |
| Affinity Tag | None |
| Concentration | Lot specific |
| Buffer | 20 mM Tris, pH 7.5, 0.15 M NaCl, 1 mM EDTA |
| Storage | -80°C, avoid cycles of freeze/thaw |
| Stability | 1 year under recommended storage conditions |
Applications
- Investigation of DUB linkage specificity.
Documents
