p62 is a cytoplasmic protein initially identified as a phosphotyrosine independent ligand of the SH2 domain of p56^lck.  p62 specifically interacts with ubiquitin and binds it non-covalently.  It shows homology to neither the ubiquitin C-terminal hydrolases nor with subunit Rpn 10 (S5a) of the 19S regulator complex of the 26S proteasome, the only proteins then known to bind to ubiquitin non-covalently.  Detailed analysis demonstrated the C-terminal region of p62 to be indispensable to the interaction, with subsequent studies demonstrating this sequence to contain a sequence motif – the ubiquitin-associated (UBA) domain – present in some members of the ubiquitination pathway, UV excision proteins, and certain protein kinases. Most recently p62 has been shown to be induced during apoptosis and proteasomal inhibition in neuronal cells and to be present in neuronal and glial inclusions in human tauopathies and synucleinopathies.

It has now been demonstrated that the UBA sequence motifs may function in isolated form and, consequently, may find utility in the isolation and characterisation of multi-ubiquitinylated species.

AFFINITI scientists have synthesised the p62 UBA domain and covalently conjugated this to agarose.  It has been demonstrated that this material will efficiently bind both isolated multi-ubiquitin chains as well as multi-ubiquitinylated conjugates.  It has proven possible to elute bound proteins under relatively mild conditions.  AFFINITI is pleased to make available this immobilised UBA domain for those wishing to study such binding mechanisms further.

UW9010       p62-derived UBA domain immobilised on agarose       0.5mL      £200.00

A detailed datasheet is available as a PDF file for immediate download by clicking on the product code above.  For further information please do not hesitate to contact AFFINITI Customer Service.