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Product Description: Ubiquitin is a small (8.5kDa) regulatory protein that has been found in almost all tissues of eukaryotic organisms. The addition of ubiquitin to a substrate protein is called ubiquitination or ubiquitylation. Ubiquitination can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity and promote or prevent protein interactions. Removal of ubiquitin from a substrate protein occurs via deconjugating enzymes, of which there are nearly 100 known enzymes with various linkage specificities. This product consists of a fulllength human, mature ubiquitin polypeptide (amino acids 1-76), expressed in E.coli with a C-terminal warhead (Vinyl Phenyl Sulfone) and an N-terminal HA-Tag. HA-Ubiquitin vinyl pentyl sulfone is a potent, irreversible and specific inhibitor of deubiquitinating enzymes (DUBs) based on a C-terminal electrophilic vinyl sulfone group. It targets four of the five major DUB families: UCH (Ubiquitin c-terminal hydrolases), USP (Ubiquitin Specific Proteases), OTU (Ovarian Tumor Proteases), and MJD (Machado-Josephin domain proteases) while JAMM metalloproteases are not inhibited. HA-Ubiquitin vinyl pentyl sulfone can be used for activity profiling experiments and using the HA-Tag conveniently for Immunoprecipitations in search for new or novel enzymes reacting with the c-terminal warhead.
Alternate Names/Synonyms: HA-Ub-VPS; HA-Ubiquitin-VPS; HA-Ubiquitin-Vinyl pentyl sulfone
Product type: Protein
Source / Host: E. coli
Sequence: Human ubiquitin (aa1-76) (Accession Nr. P0CG47) with a C-terminal vinyl pentyl sulfone group and a N-terminal HA-Tag.
Species Crossreactivity: Human
Molecular Weight: ~10kDa
Purity: >97% (LCMS)
Concentration: Lot dependent.
Formulation: Liquid. In 50mM MES pH 6.0, 100mM sodium chloride.
Handling Advice: Aliquot to avoid freeze/thaw cycles.
Short Term Storage: -20°C
Long Term Storage: -80°C
Shipping: DRY ICE
Use & Stability: Stable for at least 1 year after receipt when stored at -80°C.
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