来源于:KLH conjugated Synthesised phosphopeptide derived from human Akt around the phosphorylation site of Thr308:MK(p-T)FC 亚型:IgG 纯化方法:affinity purified by Protein A 储存液:0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. 别 名:AKT (phospho T308); p-AKT (pho...
Phosphorylation of Akt at S473 (ref. 5) and T308 (ref. 6) activates Akt. However, it remains unclear whether further mechanisms account for full Akt activation, and whether Akt hyperactivation is linked to misregulated cell cycle progression, another cancer hallmark. Here we report that Akt ...
Activation of mammalian AKT depends on its recruitment to the membrane through binding of phosphatidylinositol-3,4,5-trisphosphate (PIP3) to the PH domain of AKT, and subsequent phosphorylation at two key residues, Thr308 and Ser473, located at the catalytic domain and C-terminal regulatory ...
Target Protein:phospho-Akt (Thr308) IR:Immunogen Range:MK(p-T)FC Clonality:Polyclonal Isotype:IgG Entrez Gene:207 Swiss Prot:P31749 Source:KLH conjugated Synthesised phosphopeptide derived from human Akt around the phosphorylation site of Thr308:MK(p-T)FC ...
phosphorylation at T308 via disrupting the interaction between Akt and PDK1 [47]. As a result, this modification causes the suppression of tumor cell proliferation and migration. However, O-GlcNAcylation of Akt at T430 and T479 promotes Akt phosphorylation on S473 and activation by reducing the ...
Akt1, Akt2, and Akt3 appear to be controlled similarly. However, the regulatory serine/threonine residues that undergo inducible phosphorylation differ between the three isoforms (T308/T309/T305 and S473/S474/S472 on Akt1, Akt2, and Akt3, respectively) [43]. All isoforms are basally phosp...
Akt is partially activated by T308 phosphorylation by PDK1. Full activation requires S473 phosphorylation, which can be catalyzed by multiple proteins, including PDK239,40. To investigate the upstream component that mediates Akt regulation by LAMB3, we focused on PI3K and PDK2. In our study, ...
Retargeting was linked to differential AKT T308 and S473 phosphorylation, in turn controlled by GC-specific upregulation of phosphoinositide-dependent protein kinase PDK1 and the phosphatase PTEN. In GCBCs, AKT preferentially targeted CSK, SHP-1 and HPK1, which are negative regulators of BCR ...
We find that T450 phosphorylation has only a minimal part in these activities. In contrast, the phosphorylation of T308 and of S473 fulfills essential, distinct, and non-overlapping functions that we define with inactivating and with phosphomimetic mutations of these sites. 展开 ...
We show that intracellular calcium chelation attenuated the phosphorylation of Akt S473, but had no effect on the phosphorylation of Akt T308, which is consistent with previous findings (Farrer et al., 2013; Razmara et al., 2013). It has been shown that the S473 phosphorylation is less ...