PI3Ka plays a specific role in apoptosis in human colon cancer cells. Injection of neutralizing antibodies specific to PI3Ka into adenocarcinoma cells induced apoptosis, a response that was reverted by treating cells with caspase inhibitor. It was also shown that PI3Ka mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka is a key regulator of the initiation of keratinocyte differentiation. A decrease in PI3Ka activity results in a loss of keratinocyte adhesion to the extracellular membrane and the initiation of early phase differentiation.
The PI3Ka catalytic and regulatory subunits are coexpressed in Sf9 insect cells. Phosphoinositide 3-kinase alpha Bovine Recombinant is a glycosilated protein having a molecular weight as follows: p85a chain 83.5 kDa, p110 chain 124.3 kDa.
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