Recombinant Human STIP1 Homology and U-Box Containing Protein 1

Source : Escherichia Coli. STUB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids and having a molecular mass of 34.8 kDa.STUB1 is expressed and purified by proprietary chromatographic techniques. STUB1, is a cytoplasmic protein whose amino acid sequence is highly preserved across species. STUB1 interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, whereas its U-box domain contains its E3 ubiquitin ligase activity. STUB1 interaction with these molecular chaperones lead to in client substrate ubiquitylation and degradation by the proteasome. therefore, STUB1 acts to tilt the folding-refolding mechanism towards the degradative pathway, and it serves as a link between the two. STUB1 inhibits anchorage-independent cell growth and metastatic potential by degrading oncogenic proteins including SRC-3. Inhibition of tyrosine kinase activity of Her-2/neu by quercetin specifies an lateration in the Her-2/neu structure which promotes STUB1 recruitments and down-regulation of Her-2/neu. STUB1 recognizes and mediates degradation of toxic, oligomeric forms of alphaSyn.