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>   home   >    Crown Insignt   >    Beclin1   



Beclin-1 is a Bcl-2-homology protein that has been shown to control the formation and maturation of autophagosomes. Beclin interacts with cofactors such as Atg14L, UVRAG, and Bif- 1, Ambra, leading to activation of the lipid kinase Vps-34 and formation of Beclin-Vps34-Vps15 complex, all promoting the nucleation of the autophagosome. This complex can be disrupted through the interaction of Beclin with Bcl-2 or Bcl-XL, which inhibits autophagy. The interaction of Beclin-1 with either Bcl-2 or Bcl-XL could also be inhibited when Beclin-1 is phosphorylated at Thr-119 by the death-associated protein kinase (DAPK) or by the phosphorylation of Bcl-2 by c-Jun kinase 1 (JNK-1). The null mutation of Beclin-1 is lethal during early embryonic development in mice. Several studies have shown that in normal human tissues the deletion of a single allele of Beclin-1 leads to 40-75% of sporadic breast and ovarian cancers.

Fluorescent image of U251 cells stained with AM1818a Beclin-1 antibody. U251 cells were treated with Chloroquine and incubated with AM1818a Beclin-1 antibody, showing Beclin-1 localized to autophagic vacuoles in the cytoplasm of U251 cells (green). Nuclei were counterstained with Hoechst 33342 (blue).

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