Phospho-Beclin-1 (Ser90) Antibody #86455
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 60 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Ser90 of human Beclin-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of proteins activated in response to nutrient deprivation and in neurodegenerative conditions (1). One of the proteins critical to this process is Beclin-1, the mammalian orthologue of the yeast autophagy protein Apg6/Vps30 (2). Beclin-1 can complement defects in yeast autophagy caused by loss of Apg6 and can also stimulate autophagy when overexpressed in mammalian cells (3). Mammalian Beclin-1 was originally isolated in a yeast two-hybrid screen for Bcl-2 interacting proteins and has been shown to interact with Bcl-2 and Bcl-xL, but not with Bax or Bak (4). While Beclin-1 is generally ubiquitously expressed, research studies have shown it is monoallelically deleted in 40-75% of sporadic human breast and ovarian cancers (5). Beclin-1 is localized within cytoplasmic structures including the mitochondria, although overexpression of Beclin-1 reveals some nuclear staining and CRM1-dependent nuclear export (6). Investigators have demonstrated that Beclin-1-/- mice die early in embryogenesis and Beclin-1-/+ mice have a high incidence of spontaneous tumors. Stem cells from the null mice demonstrate an altered autophagic response, although responses to apoptosis appeared normal (7). Researchers have also found that overexpression of Beclin-1 in virally infected neurons in vivo resulted in significant protection against Sindbis virus-induced disease and neuronal apoptosis (4).
Several studies have indicated that autophagy is enhanced by phosphorylation of Beclin-1 at Ser90 triggered by stress-responsive kinases including MAPKAPK-2/MAPKAPK-3, DAPK3, and CaMKII (8-10).
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- Liang, X.H. et al. (1999) Nature 402, 672-6.
- Liang, X.H. et al. (1998) J Virol 72, 8586-96.
- Aita, V.M. et al. (1999) Genomics 59, 59-65.
- Liang, X.H. et al. (2001) Cancer Res 61, 3443-9.
- Yue, Z. et al. (2003) Proc Natl Acad Sci USA 100, 15077-82.
- Wei, Y. et al. (2015) Elife 4.
- Fujiwara, N. et al. (2016) J Biol Chem 291, 10858-66.
- Li, X. et al. (2017) Nat Commun 8, 1159.
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