Specifications
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. K48 di-ubiquitin or K48 linked di-ubiquitin was at the forefront of this research. 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
Species | Human |
Source | E. coli |
Tag | None |
Molecular Weight | 17,139.7 Da |
Quantity | 100 µg |
Concentration | Variable |
Formulation | 20 mM Tris pH 7.5, 150 mM NaCl, 1 mM EDTA |
Storage | -80°C, avoid freeze/thaw cycles |
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