84-9343-85　［取扱停止］Recombinant Human pan-AKT protein （His Tag） 20ug　PDEH100034

特徴

• 背景：downstream of phosphatidylinositol 3-kinase （PI3K） to mediate the effects of various growth factors such as platelet-derived growth factor （PDGF）, epidermal growth factor （EGF）, insulin and insulin-like growth factor I （IGF-I） .
• AKT mediates the antiapoptotic effects of IGF-I （By similarity）.
• Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly .
• May be involved in the regulation of the placental development （By similarity）.
• Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its： kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3 .
• Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its： cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation.
• Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation.
• Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity.
• Phosphorylation of BAD stimulates its pro-apoptotic activity .
• Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53.
• Phosphorylates palladin （PALLD）, modulating cytoskeletal organization and cell motility.
• Phosphorylates prohibitin （PHB）, playing an important role in cell metabolism and proliferation.
• Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization .
• These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation.
• Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation .
• Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor.