Purity: > 90% by SDS - PAGE Format: Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 30% glycerol, 1mM DTT . YOD1 is a highly conserved deubiquitinating enzyme of the ovarian tumor (otubain) family, whose function has yet to be assigned in mammalian cells. YOD1 is a constituent of a multiprotein complex with p97 as its nucleus, suggesting a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. Expression of a YOD1 variant deprived of its deubiquitinating activity imposes a halt on the dislocation reaction, as judged by the stabilization of various dislocation substrates. Recombinant human YOD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.