This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Tone, Tanahashi, Tanaka, Fujimuro, Yokosawa, Toh-e: "Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells." in: Gene, Vol. 243, Issue 1-2, pp. 37-45, (2000) (PubMed).
Takeuchi, Toh-e et al.: "Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutation in RPN12 (a lid component gene) with mutations in RPT1 (an ATPase gene) causes synthetic ..." in: Molecular & general genetics : MGG, Vol. 262, Issue 1, pp. 145-53, (1999) (PubMed).
Hershko, Ciechanover: "The ubiquitin system." in: Annual review of biochemistry, Vol. 67, pp. 425-79, (1998) (PubMed).
Background: The 26 S proteasome is a protein complex with a molecular mass of 2,000 kDa. It is essential not only for eliminating damaged or misfolded proteins but also for degrading short lived regulatory proteins involved in cell cycle regulation, DNA repair, signal transduction, apoptosis, and metabolic regulation. The 26S proteasome is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP is further subdivided into lid and base sub-complexes. Rpn12 is one of the non-ATPase subunits of the lid. Rpn12 interacts with an ATPase subunit, Rpt1, of the base. Rpn12, Rpt1 double mutant becomes lethal, suggesting a strong interaction between Rpn12 and Rpt1. In the double mutant cells, the function of the 26S proteasome is completely eliminated.