Description
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 (ref.1). 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.
This product is a rabbit polyclonal antibody affinity purified
Applications
1) Western blot 1/5,000~1/10,000
2) Immunoprecipitation
Other applications have not been tested.
Specification
Immunogen: Recombinant yeast Rpn12 expressed in E. coli
Form: Affinity purified IgG in PBS, 1 mg/ml BSA, 0.09 % sodium azide, 50% glycerol
Reactivity: S. cerevisiae Rpn12, not tested with other species
Storage: Ship at 4°C or -20°C and stores at -20°C
Data Link
SGD RPN12/YFR052W
References This antibody has been used in Ref. 2.
- Hershko A and Ciechanover A “THE UBIQUITIN SYSTEM.” Annu. Rev. Biochem. 67, 425-479 (1998) PMID: 9759494
- Takeuchi J and Toh-e A “Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutationin RPN12 (a lid component gene) with mutations in RPT1 (anATPase gene) causes synthetic lethality.” Mol Gen Genet 262:145-153(1999) PMID: 10503546
- Glickman MH “A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.” Cell. Sep 4;94(5):615-23 (1998) PMID:9741626
Fig.1. Detection of Rpn12 (32kD) in the crude extract of S. cerevisiae by Western blot using this antibody
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