Anti-Ubiquitin+1 monoclonal antibody (DMAB7760MH)


Host Species
Antibody Isotype
Species Reactivity
Synthetic peptide (KLH coupled) corresponding to C-terminal residues of human Ubiquitin +1.


Alternative Names
Ubiquitin+1; Ub+1; FLJ25987; MGC8385; Polyubiquitin B; RPS27A


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O-17 NMR Studies of Yeast Ubiquitin in Aqueous Solution and in the Solid State


Authors: Lin, Binyang; Hung, Ivan; Gan, Zhehong; Chien, Po-Hsiu; Spencer, Holly L.; Smith, Steven P.; Wu, Gang

We report a general method for amino acid-type specific O-17-labeling of recombinant proteins in Escherichia coli. In particular, we have prepared several [1-C-13,O-17]-labeled yeast ubiquitin (Ub) samples including Ub-[1-C-13,O-17]Gly, Ub-[1-C-13,O-17]Tyr, and Ub-[1-C-13,O-17]Phe using the auxotrophic E. coli strain DL39 GlyA lambda DE3 (aspC(-) tyrB(-) ilvE(-) glyA(-) lambda DE3). We have also produced Ub-[eta-O-17]Tyr, in which the phenolic group of Tyr59 is O-17-labeled. We show for the first time that O-17 NMR signals from protein terminal residues and side chains can be readily detected in aqueous solution. We also reported solid-state O-17 NMR spectra for Ub-[1-C-13,O-17]Tyr and Ub-[1-C-13,O-17]Phe obtained at an ultrahigh magnetic field, 35.2 T (1.5 GHz for H-1). This work represents a significant advance in the field of O-17 NMR studies of proteins.

KEAP1 Mutations Drive Tumorigenesis by Suppressing SOX9 Ubiquitination and Degradation


Authors: Shao, Na; Huang, Hong; Idris, Muhammad; Peng, Xu; Xu, Feng; Dong, Shiwu; Liu, Chungang

The transcription factor SOX9 is frequently amplified in diverse advanced-stage human tumors. Its stability has been shown to be tightly controlled by ubiquitination-dependent proteasome degradation. However, the exact underlying molecular mechanisms remain unclear. This work reports that SOX9 protein abundance is regulated by the Cullin 3-based ubiquitin ligase KEAP1 via proteasome-mediated degradation. Loss-of-function mutations in KEAP1 compromise polyubiquitination-mediated SOX9 degradation, leading to increased protein levels, which facilitate tumorigenesis. Moreover, the loss of critical ubiquitination residues in SOX9, by either a SOX9 (Delta K2) truncation or K249R mutation, leads to elevated protein stability. Furthermore, it is shown that the KEAP1/SOX9 interaction is modulated by CKI gamma-mediated phosphorylation. Importantly, it is demonstrated that DNA damage drugs, topoisomerase inhibitors, can trigger CKI activation to restore the KEAP1/SOX9 interaction and its consequent degradation. Collectively, herein the findings uncover a novel molecular mechanism through which SOX9 protein stability is negatively regulated by KEAP1 to control tumorigenesis. Thus, these results suggest that mitigating SOX9 resistance to KEAP1-mediated degradation can represent a novel therapeutic strategy for cancers with KEAP1 mutations.

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