Anti-phospho-Akt (pThr³⁰⁸) antibody produced in rabbit

The AKT/protein kinase B gene has three homologues, namely PKBα (Akt1), PKBβ (Akt2), and PKBγ (Akt3), which are localized to human chromosome 14q32, 19q13, and 1q44, respectively. The members of AKT family contain an amino-terminal pleckstrin homology (PH) domain, a short α-helical linker, and a carboxyl-terminal kinase domain. The AKT1 and AKT2 genes are expressed highly in insulin-responsive tissues, such as brown fat.

The antiserum was produced against synthesized peptide derived from human Akt around the phosphorylation site of Thr308.

Immunogen Range: 276-325

Anti-phospho-Akt (pThr308) antibody produced in rabbit has been used in immunoblotting.

AKT is activated in a multistep process that involves its translocation across the membrane and its phosphorylation. The 3′-phosphorylated phosphoinositides, 3,4,5-trisphosphate (PI-3,4,5-P3) and PI-3,4,-P2 produced by PI3K bind to the PH (pleckstrin homology) domain and this binding facilitates the localization of AKT kinases to the plasma membrane. Once localized, PDK1 (3-phosphoinositide-dependent kinase) phosphorylates Thr-308/309 residue on the AKT molecule, which is essential for its activation. Another residue, Ser- 473/474 on AKT, is also phosphorylated by PDK2. This phosphorylation, although not necessary, increases the activity of AKT. It plays a role in cell survival by regulating the effect of growth factors. AKT may facilitate phosphorylation and inactivation of glycogen synthase kinase-3 by insulin. In adipocytes, it may be involved in the activation of glucose transporter translocation. It is involved in the regulation of several proteins that are involved in cellular processes, such as metabolism, apoptosis, and proliferation. Variations in PI3K-AKT signaling have been observed in several types of cancer, such as human gastric cancer, prostate and breast cancers.

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Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.5% BSA, 0.02% sodium azide and 50% glycerol.

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