Description
Autophagy is the bulk degradation of cellular proteins through the autophagosomic-lysosomal pathway. This process is important for normal cell growth, and may be disrupted in tumor cells. Beclin is a Bcl-2 binding protein that is homologous to the yeast autophagy gene, apg6/vps30. The structure of beclin includes a Bcl-2 binding coiled-coil region, and a leucine-rich nuclear export signal (NES). Beclin protein colocalizes with intracytoplasmic organelles and nuclei in normal COS7 and MCF7 cells. However, inhibition of CRM1-dependent nuclear export leads to beclin localization primarily in the nucleus. Mutation of the NES domain of beclin also prevents nuclear export, as well as suppresses beclin-mediated nutrient deprivation-induced autophagy. In addition, these beclin mutants can not inhibit in vitro clonigenicity and in vivo tumorigenicity of MCF7 cells. Beclin interaction with Bcl-2 may be involved with host viral defense, since overexpression of beclin inhibits Sindbis virus replication and expression of beclin lacking the Bcl-2 binding domain has no antiviral effects. Thus, beclin may be an important component of complexes involved in autophagy.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Format
- FormatPurified
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Preparation and Storage
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.Store undiluted at -20°C.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/pharmingen/protocols for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.