Anti-Rpn7 (S. cerevisiae) antibody, affinity purified

$440.00

SKU: 62-205 Research Area: Applications:

Description

The 26 S proteasome is a protein complex with a molecular mass of 2000 kDa and is highly conserved among eukaryotic organisms. It is essential for eliminating damaged or misfolded proteins and also for degrading short lived regulatory proteins involved in cell cycle regulation, DNA repair, signal transduction, apoptosis, and metabolic regulation (Ref.1). Rpn7 is one of the lid subunits of the 26 S proteasome regulatory particle (Ref.1, 2). The RPN7 gene is known to be essential and required for the integrity of the 26 S complex by establishing a correct lid structure (Ref.3, 4).

 

Applications

1) Western blot (~1000 fold dilution)

2) Immunoprecipitation

Not tested for other applications.

Specifications

Product: Rabbit polyclonal antibody affinity purified with recombinant Rpn7p

Immunogen: Recombinant yeast Rpn7p expressed in E. coli (Ref. 4)

Form: Purified IgG in 100 mM NaCl, 10 mM Tris-HCl pH 7.4, 0.05 % sodium azide

Reactivity: S. cerevisiae Rpn7p. Not tested with other species.

Storage: -20°C. To avoid repeated freezing and thawing, aliquot antibody solution.

Data Link: SGD RPN7/YPR108W

 

References: This product was used in Ref. 3 and 4

  1. Hershko A and Ciechanover A “THE UBIQUITIN SYSTEM.” Annu Rev Biochem 67: 425-479 (1998) PMID: 9759494
  2. Finley D et alUnified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle.” Trends Biochem Sci 23:244-245 (1998) PMID 9697412
  3. Isono E et alRpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae.” J Biol Chem 279:27168-76 (2004) PMID: 15102831
  4. Isono E et al “The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome.” Mol Biol Cell 18:569-76 (2007) PMID: 17135287

Fig.1 Detection of Rpn7 (49 kDa) in the crude extract of S. cerevisiae by Western blotting using this antibody.

Title Type Size
62-205 Anti-Rpn7_03222018 application/pdf 179 KB

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