Rubicon (E5J5V) Rabbit mAb #68261
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 130 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:200 |
Storage
Protocol
Specificity / Sensitivity
Rubicon (E5J5V) Rabbit mAb recognizes endogenous levels of total Rubicon protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala943 of human Rubicon protein.
Background
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 Vps34, including p105/Vps15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14 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, Atg14 localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).
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- Levine, B. and Yuan, J. (2005) J Clin Invest 115, 2679-88.
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- Yan, Y. and Backer, J.M. (2007) Biochem Soc Trans 35, 239-41.
- Stack, J.H. et al. (1995) J Cell Biol 129, 321-34.
- Zeng, X. et al. (2006) J Cell Sci 119, 259-70.
- Liang, C. et al. (2006) Nat Cell Biol 8, 688-99.
- Itakura, E. et al. (2008) Mol Biol Cell 19, 5360-72.
- Sun, Q. et al. (2008) Proc Natl Acad Sci USA 105, 19211-6.
- Zhong, Y. et al. (2009) Nat Cell Biol 11, 468-76.
- Matsunaga, K. et al. (2009) Nat Cell Biol 11, 385-96.
Limited Uses
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