Recombinant production enables lot-to-lot consistency and is animal-cruelty-free
Western blot analysis of PI 3 Kinase p85 beta on different lysates. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody (ET1609-30, 1/500) was used in 5% BSA at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:200,000 dilution was used for 1 hour at room temperature.
Lane 1: Raji cell lysate
Lane 2: Hela cell lysate
Lane 1: MCF-7 cell lysate
Lane 2: U937 cell lysate
Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at Tyr-655 by PTPN13. Phosphorylation of Tyr-655 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination.; Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2.
Phosphatidylinositol 3-kinase (PI 3-kinase) is composed of p85 and p110 subunits. p85 lacks PI 3-kinase activity and acts as an adapter, coupling p110 to activated protein tyrosine kinase. Two forms of p85 have been described (p85α and p85β), each possessing one SH3 and two SH2 domains. Various p110 isoforms have been identified. p110α and p110β interact with p85α, and p110α has also been shown to interact with p85β in vitro. p110α expression is restricted to white blood cells. It has been shown to bind p85α and p85β, but it apparently does not phosphorylate these subunits. p110α seems to have the capacity to autophosphorylate. p110α does not interact with the p85 subunits. It has been shown to be activated by α and β heterotrimeric G proteins.
Just like the interactions between antigens and antibodies, the higher the affinity between you and us the better.