Reference
BCL2L1
BCL2L1 brief description and product highlight
BCL2L1 (also known as BCLX) was isolated by
Boise et al. (1993) , who showed that it can function as a BCL2 -independent regulator of apoptosis. The gene is highly conserved in vertebrate evolution, and plays an important role in both positive and negative regulation of apoptosis.
In 1999,
Shimizu et al. (1999) showed recombinant
Bax [AP1302a ] and
Bak [AP1301a] accelerate the opening of the mitochondrial porin channel
VDAC [AT4508a ], whereas the antiapoptotic protein BCLXL (long isoform) closes VDAC by binding to it directly. They concluded that the Bcl2 family of proteins bind to VDAC in order to regulate the mitochondrial membrane potential and release cytochrome C during apoptosis.
Chipuk et al. (2005) demonstrated that BCLXL sequestered cytoplasmic p53 after genotoxic stress. Nuclear p53 caused expression of
PUMA [AP1317a], which then displaced p53 from BCLXL, allowing p53 to induce mitochondrial permeabilization.
Bivona et al. (2006) found that the subcellular localization and function of Kras [
AT2650a,
AT2651a] in mammalian cells was modulated by
Pkc [ AP7015a]. Phosphorylation of Kras by Pkc agonists induced rapid translocation of Kras from the plasma membrane to several intracellular membranes, including the outer mitochondrial membrane, where Kras associated with Bclxl. Phosphorylated Kras required Bclxl for induction of apoptosis.
We offer antibodies for BCL2L1:
AP7958a : Rabbit anti Human BCL2L1 (N-Terminal)
AP7958c: Rabbit anti Human BCL2L1 (Center)
AT1282a: Mouse anti Human BCL2L1
