The reversible conjugation of ubiquitin and ubiquitin-like proteins to substrates regulates a large number of cellular processes. Deciphering these complex pathways is the focus of many researchers but the work has been slowed by the lack of high quality reagents. Deubiquitylating enzymes (DUBs) recognize and cleave the isopeptide bond between ubiquitin moieties or between ubiquitin and the target protein. Measurement of the activity of these enzymes for kinetic study or inhibitor screening has been traditionally carried out using ubiquitin conjugated to fluorescent leaving groups (AMC or Rhodamine) at the C-terminus. While these are suitable substrates for many deubiquitylating enzymes, the cleavage of the amide bond serves as a proxy for the true activity of isopeptidases, i.e. cleavage of an isopeptide bond. LifeSensors has produced a complete panel of all eight possible di-ubiquitin molecules (including C to N-linked linear molecules) for determining the linkage specific activity of individual DUBs. This kit is a convenient collection of these di-Ub molecules for the an initial survey of linkage-specificity.
|Quantity||5 µg each|
|Storage||-80°C, avoid freeze/thaw cycles|