Beclin-1 antibody
Principal name
Beclin-1 antibody
Alternative names for Beclin-1 antibody
BECN1, GT197, Coiled-coil myosin-like BCL2-interacting protein, Protein GT197
Selected pictures


SwissProt ID
O88597 (Mouse), Q14457 (Human), Q4A1L4 (Bovin), Q4A1L5 (Pig), Q5ZKS6 (Chick), Q91XJ1 (Rat)
Gene ID
8678 (BECN1)
Ncbi ID
Available reactivities
Available hosts
Available applications
Immunocytochemistry/Immunofluorescence (ICC/IF), Paraffin Sections (P), Immunoprecipitation (IP), Western blot / Immunoblot (WB), Enzyme Immunoassay (E), Frozen Sections (C), Dot blot (Dot), Flow Cytometry (F)
Background of Beclin-1 antibody
Beclin 1 is the first identified mammalian gene to mediate autophagy and also has tumor suppressor and antiviral function. Autophagy, a process of bulk protein degradation through an autophagosomic-lysosomal pathway, is important for differentiation, survival during nutrient deprivation, and normal growth control, and is often defective in tumor cells. Beclin 1 was originally isolated in a yeast two hybrid screen to identify Bcl-2-binding partners and maps to a tumor susceptibility locus on human chromosome 17q21 that is frequently monoallelically deleted in human breast, ovarian and prostate cancer. Beclin 1 encodes an evolutionarily conserved 60 kDa coiled coil protein that is expressed in human muscle, epithelial cells and neurons. In gene transfer studies, beclin 1 promotes nutrient deprivation-induced autophagy, inhibits mammary tumorigenesis, and inhibits viral replication. Expression of the Beclin 1 protein is frequently decreased in malignant breast epithelial cells. Based upon these observations, it is speculated that beclin 1 may work through induction of autophagy to negatively regulate tumorigenesis and to control viral infections. Beclin 1 may also play a role in other biological processes in which autophagy is important such as cell differentiation and nutritional stress responses.
General readings
1. Klionsky, D.J., and Emr, S. Autophagy as a regulated pathway of cellular degradation. Science. 290: 1717-1721, 2000.
2. Liang, X.H., et al. Induction of autophagy and inhibition of tumorogenesis by beclin 1. Nature. 402(6762): 672-676, 1999.
3. Aita, V.M., et al. Cloning and genomic organization of Beclin 1, a candidate tumor suppressor gene on chromosome 17q21. Genomics. 59: 59-65, 1999.
4. Liang, X.H. et al. Protection against fatal Sindbis virus encephalitis by Beclin, a novel Bcl-2-interacting protein. Journal of Virology. 72(11): 8586-8596, 1998.
5.Massey, Ashish C., et al. Consequences of the selective blockage of chaperone-mediated autophagy. PNAS. 103:5805-5810, 2006 1. Personal communications with Dr. Beth Levine, Columbia University.
2. Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., and Cuervo, A. M. Consequences of the selective blockage of chaperone-mediated autophagy, 2006; 103, 5805-5810.
Antibodies
| Catalog No. | Host | Clone/Iso. | Pres. | React. | Applications | ||
|---|---|---|---|---|---|---|---|
| AP20054CP-N |
Beclin-1 Control Peptide | ||||||
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50 µg /
€130.00
|
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| Acris Antibodies GmbH | |||||||
| AP20057CP-N |
Beclin-1 Control Peptide | ||||||
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50 µg /
€130.00
|
||||||
| Acris Antibodies GmbH | |||||||
| NB500-249PEP |
Beclin-1 control peptide | ||||||
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Purified |
50 µg /
€120.00
|
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| Novus Biologicals Inc. | |||||||

