Recombinant Human STIP1 Homology and U-Box Containing Protein 1
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| Amount : | 50 µg |
| Purification : | Greater than 90.0% as determined by SDS-PAGE. |
| Content : | The STUB1 protein solution contains 20mM Tris-HCl, pH-7.5, 10% glycerol and 5mM DTT. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. |
| AA sequence : | MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV EDY. |
| Alternative Name : | CHIP, UBOX1, HSPABP2, NY-CO-7, SDCCAG7, STUB1, STIP1 homology and U box-containing protein 1, Carboxy terminus of Hsp70-interacting protein, E3 ubiquitin-protein ligase CHIP, CLL-associated antigen KW-8, Antigen NY-CO-7. |
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.
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