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- Tel: 858.663.9055
- Email: info@nsjbio.com
Nedd4-binding partner-1 (N4BP1) has been identified as a protein interactor and a substrate of the homologous to E6AP C terminus (HECT) domain-containing E3 ubiquitin-protein ligase (E3), Nedd4. Here, we describe a previously unrecognized functional interaction between N4BP1 and Itch, a Nedd4 structurally related E3, which contains four WW domains, conferring substrate-binding activity. We show that N4BP1 association with the second WW domain (WW2) of Itch interferes with E3 binding to its substrates. In particular, we found that N4BP1 and p73?, a target of Itch-mediated ubiquitin/proteasome proteolysis, share the same binding site. By competing with p73? for binding to the WW2 domain, N4BP1 reduces the ability of Itch to recruit and ubiquitylate p73? and inhibits Itch autoubiquitylation activity both in in vitro and in vivo ubiquitylation assays.
Optimal dilution of the N4BP1 antibody should be determined by the researcher.
E. coli-derived recombinant human protein (amino acids M1-K885) was used as the immunogen for the N4BP1 antibody.
After reconstitution, the N4BP1 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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