AKT3

The following AKT3 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

AKT3 Antibodies

AKT3 Antibodies for Homo sapiens (Human)

AKT3 Proteins

AKT3 Proteins for Rattus norvegicus (Rat)

AKT3 Proteins for Mus musculus (Mouse)

AKT3 Background

The AKT3 gene directs the generation of RAC-gamma serine/threonine-protein kinase (AKT3), which mediates many processes including metabolism, proliferation, cell survival, growth, and angiogenesis through serine and/or threonine phosphorylation of a range of downstream substrates. The encoding gene of AKT3 produces two almost identical variants via differential splicing of C-terminal exons, making AKT3 distinguishes from the otherwise similar AKT1 and AKT2 [1]. AKT3 is a key regulator in the PI3K-AKT-mTOR pathway. Studies have shown that AKT3 is closely associated with the progression of several tumor types especially melanomas, accompanied by widespread PTEN mutations [2][3]. Downregulated microRNA-217 promotes the occurrence and progression of non-small cell lung cancer (NSCLC) through upregulating AKT3 via the PI3K pathway [4]. By using a powerful clinical molecular diagnostic assay, Matissek KJ et al. identified AKT3 gene fusion and expression is associated with treatment resistance and poor outcome in the hormone receptor-positive breast cancer [5]. AKT3 isoform expression is found in triple-negative breast cancer. AKT3 splice variant lacking serine-472 phosphorylation site promotes apoptosis and suppresses mammary tumorigenesis [6]. Kim M et al. also observed that AKT3 knockdown caused severe structural defects in the mitochondria and an AKT3 deficiency-induced decrease in mitochondrial respiration in A549 lung cancer cells [7]. They concluded that AKT isoforms play distinct roles in mitochondrial function and that AKT3 is critical for proper mitochondrial respiration in human cancer cells [7].

[1] Brodbeck D, Hill MM, et al. Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain [J]. J Biol Chem 2001;276:29550-8.
[2] Robertson GP. Functional and therapeutic significance of Akt deregulation in malignant melanoma [J]. Cancer Metastasis Rev 2005;24:273-5.
[3]Madhunapantula SV, Robertson GP. Targeting protein kinase-b3 (akt3) signaling in melanoma [J]. Expert Opin Ther Targets 2017;21:273-0.
[4] Qi YJ, Zha WJ, et al. MicroRNA-217 alleviates development of non-small cell lung cancer by inhibiting AKT3 via PI3K pathway [J]. Eur Rev Med Pharmacol Sci. 2018 Sep;22(18):5972-5979.
[5] Matissek KJ, Onozato ML, et al. Expressed Gene Fusions as Frequent Drivers of Poor Outcomes in Hormone Receptor-Positive Breast Cancer [J]. Cancer Discov. 2018 Mar;8(3):336-353.
[6] Suyama K, Yao J, et al. An Akt3 Splice Variant Lacking the Serine 472 Phosphorylation Site Promotes Apoptosis and Suppresses Mammary Tumorigenesis [J]. Cancer Res. 2018 Jan 1;78(1):103-114.
[7] Kim M, Kim YY, et al. Akt3 knockdown induces mitochondrial dysfunction in human cancer cells [J]. Acta Biochim Biophys Sin (Shanghai). 2016 May;48(5):447-53.

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