reagents

UbiQ-115 (Biotin-Ahx-K63 diUbiquitin VME) probe is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) based on K63 linked diUb. Here Lys63 has been replaced by a diaminobutyric acid residue equipped with a VME type warhead3.

UbiQ-093 is ubiquitin that is phosphorylated on Thr12.

UbiQ-057 (Ub-PA) is an activity-based probe for deubiquitinating enzymes (DUBs) and contains propargyl amide (PA) as an electrophile.

Biotin-Ahx-SUMO2-Dha (Dha= dehydroalanine) is a new and first of its kind activity based probe for the SUMO ligation pathway. [

UbiQ-092 is a ubiquitin protein that is phosphorylated on Thr7. Phosphoproteomic studies have identified several phosphorylated sites in ubiquitin, among them pThr7.

UbiQ-113 is ubiquitin that is phosphorylated on Ser57.

His6-Ahx-Ahx-SUMO2-VPS (UbiQ-237) is an activity-based probe for SUMO proteases.

Biotin-Ahx-SUMO2-VME is an activity-based probe for SUMO proteases.

UbiQ-094 is ubiquitin that is phosphorylated on Ser57.

Ub-VME is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs),

Potent, irreversible and specific inhibitor based on K63 linked diUb that targets the S2 pocket of deubiquitinating enzymes (DUBs). The C-terminus of the proximal Ub is equipped with the propargyl amide (PA) electrophile and the isopeptide bond between the two Ub proteins is replaced by a DUB resistant mimic.

UbiQ-091 is ubiquitin that is phosphorylated on Ser65, a ubiquitin variant which has been shown to activate Parkin E3 ligase mediated ubiquitination.

UbiQ-154 is a new crosslinking reagent based on ubiquitin in which Leu73 is replaced by the photoreactive analog photoleucine (photoLeu).

UbiQ-262 is an activity-based probe for and inhibitor of ISG15 proteases.

Biotin-ANP-Ub-PA (UbiQ-077) is a newly developed potent and specific inhibitor of deubiquitylating enzymes (DUBs). It is labeled on the N-terminus with biotin and contains the UV cleavable 3-amino-3-(2-nitrophenyl)propanoic acid (ANP) linker, allowing for UV mediated cleavage of the biotin tag.