|Calculated MW||17.139 kDa (Band migrates faster on gels)|
|Assay&Purity||Western Blot; ≥95%|
|Storage||-80°C; 2.5 mg/ml in 20 mM Tris-HCl, pH 7.5, 0.15 M NaCl and 1 mM EDTA.|
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Provided below are standard protocols that you may find useful for product applications.
Poly-ubiquitylation of target proteins through linkage at K48, is now the most thoroughly studied of the various chain linkages, and was 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 di-ubiquitin chains are generated from the enzymatic linkage (E2-25K) of wild-type ubiquitin through lysine 48. The most distal ubiquitin contains an arginine substitution for a lysine at position 48, limiting the chain length.
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