UVRAG Antibody

5320:

Immunoprecipitation , Western Blotting

UVRAG Antibody detects endogenous levels of total UVRAG protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to a region surrounding Leu555 of human UVRAG. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from various cell lines using UVRAG Antibody (upper) or β-Tubulin (9F3) Rabbit mAb #2128 (lower). HCT 116 cells have been reported to contain a monoallelic frameshift mutation resulting in significantly reduced levels of endogenous UVRAG expression (Ref. 11).

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected or transfected with human or mouse UVRAG cDNA constructs, using UVRAG Antibody.

Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It is generally activated by conditions of nutrient deprivation but has also been 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 referred to as autophagy-related (Atg) genes. These proteins are involved in the formation of cytoplasmic vacuoles called autophagasomes that are delivered to lysosomes for degradation.The class III type phosphoinositide 3-kinase (PI3KC3)/Vps34 regulates vacuolar trafficking as well as autophagy (4,5). Multiple proteins have been shown to be associated with Vsp34, including: p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, which can determine Vsp34 function (6-11). UVRAG (UV radiation resistance-associated gene) is associated with the Beclin-1/PI3KC3 complex and promotes PI3KC3 enzymatic activity and autophagy, while suppressing proliferation (11). Beclin-1 binding to UVRAG promotes both autophagosome maturation and endocytic trafficking (12). UVRAG is also a potential tumor suppressor protein with frameshift mutations observed in colon and gastric carcinomas (13,14).

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. Stack, J.H. et al. (1995) J Cell Biol 129, 321-34.
6. Liang, C. et al. (2008) Nat Cell Biol 10, 776-87.
7. Matsunaga, K. et al. (2009) Nat Cell Biol 11, 385-96.
8. Zhong, Y. et al. (2009) Nat Cell Biol 11, 468-76.
9. Sun, Q. et al. (2008) Proc Natl Acad Sci U S A 105, 19211-6.
10. Itakura, E. et al. (2008) Mol Biol Cell 19, 5360-72.
11. Liang, C. et al. (2006) Nat Cell Biol 8, 688-99.
12. Liang, C. et al. (2008) Nat Cell Biol 10, 776-87.
13. Ionov, Y. et al. (2004) Oncogene 23, 639-45.
14. Kim, M.S. et al. (2008) Hum Pathol 39, 1059-63.

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• 7071 Phototope^® -HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
• 7074 Anti-rabbit IgG, HRP-linked Antibody
• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide

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