Recombinant Human His6-MBP-HOIP/RNF31 Catalytic Domain, CF

HOIP (HOIL-1 Interacting Protein, also known as RNF31) is a RING domain ubiquitin E3 ligase and component of the LUBAC complex. LUBAC, a large (approximately 600 kDa) heteromultimeric assembly consisting of at least HOIP, HOIL-1, and Sharpin, conjugates linear polyubiquitin chains to various substrates and plays a key role in NF-kappa B activation and signaling events mediated through TNF alpha and IFN. Both the catalytic activity and specificity for linear ubiquitin chain formation of LUBAC are contained within the C-terminal RBR (RING-IBR-RING) and LDD (linear ubiquitin chain determining domain) domains of HOIP. HOIL-1 and Sharpin are essential for full-length HOIP activity, but not for HOIP truncation mutants consisting of the RBR and LDD domains. This protein contains N-terminal 6-His and MBP tags, and is useful for generating unanchored linear polyubiquitin chains without the requirement for HOIL-1 or Sharpin. HOIP catalytic domain contains aa’s 699-1072.