Rubicon (D8B2) Rabbit mAb

7151:

Western Blotting

Rubicon (D8B2) Rabbit mAb recognizes endogenous levels of total Rubicon protein. Background bands of unknown origin are detected between 60 and 65 kDa.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human Rubicon protein.

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with human Rubicon (hRubicon, +), using Rubicon (D8B2) Rabbit mAb. Rubicon construct was kindly provided by Dr. Qing Zhong, University of California, Berkeley, CA.

Western Blotting

Western blot analysis of extracts from various cell lines using Rubicon (D8B2) Rabbit mAb.

Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but is also associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, which are cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vsp34, including p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14L and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14L localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14L inhibits starvation-induced autophagy (11,12).

1. Reggiori, F. and Klionsky, D.J. (2002) Eukaryot Cell 1, 11-21.
2. Codogno, P. and Meijer, A.J. (2005) Cell Death Differ 12 Suppl 2, 1509-18.
3. Levine, B. and Yuan, J. (2005) J Clin Invest 115, 2679-88.
4. Corvera, S. (2001) Traffic 2, 859-66.
5. Yan, Y. and Backer, J.M. (2007) Biochem Soc Trans 35, 239-41.
6. Stack, J.H. et al. (1995) J Cell Biol 129, 321-34.
7. Zeng, X. et al. (2006) J Cell Sci 119, 259-70.
8. Liang, C. et al. (2006) Nat Cell Biol 8, 688-99.
9. Itakura, E. et al. (2008) Mol Biol Cell 19, 5360-72.
10. Sun, Q. et al. (2008) Proc Natl Acad Sci USA 105, 19211-6.
11. Zhong, Y. et al. (2009) Nat Cell Biol 11, 468-76.
12. Matsunaga, K. et al. (2009) Nat Cell Biol 11, 385-96.

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For Research Use Only. Not For Use In Diagnostic Procedures.