Phospho-Beclin-1 (Ser90) (E3X1I) Rabbit mAb #29362
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Beclin-1 (Ser90) (E3X1I) Rabbit mAb recognizes endogenous levels of Beclin-1 protein only when phosphorylated at Ser90. This antibody may not recognize Beclin-1 when dually phosphorylated at Ser90 and Ser93.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser90 of human Beclin-1 protein.
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 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, e05289. doi: 10.7554/eLife.05289.
- Fujiwara, N. et al. (2016) J Biol Chem 291, 10858-66.
- Li, X. et al. (2017) Nat Commun 8, 1159.
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