Akt3 Antibody
- Known as:
- Akt3 Antibody
- Catalog number:
- 3163-100
- Product Quantity:
- 100 µg
- Category:
- Antibodies
- Supplier:
- Biovis
- Gene target:
- Akt3 Antibody
Related genes to: Akt3 Antibody
- Gene:
- AKT3 NIH gene
- Name:
- AKT serine/threonine kinase 3
- Previous symbol:
- -
- Synonyms:
- PKBG, RAC-gamma, PRKBG
- Chromosome:
- 1q43-q44
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-16
- Date modifiied:
- 2018-02-13
Related products to: Akt3 Antibody
Related articles to: Akt3 Antibody
- Akt is a central serine/threonine kinase in the PI3K/Akt/mTOR pathway that regulates cell survival, growth, and metabolic homeostasis. Although Akt1, Akt2, and Akt3 share high sequence homology, they perform distinct physiological and pathological functions, motivating the development of small-molecule isoform-selective chemical probes. Here, we first applied a molecular hybridization strategy to combine structural features that lead to Akt3-selectivity with the covalent pharmacophore of established covalent-allosteric Akt inhibitors, enabling selective and covalent targeting of Akt3. We then expanded the chemical space of covalent-allosteric Akt inhibitors to investigate how subtle structural differences influence selectivity across all three isoforms. Guided by structure-activity relationships and high-resolution co-crystal structures, systematic modifications of substituent patterns, linker geometry, and scaffold architecture revealed distinct isoform-selectivity profiles. Biochemical target inhibition, cellular target engagement, and covalent-binding studies further characterized these compounds and their selectivity. Collectively, these findings expand the covalent-allosteric Akt inhibitor toolbox, provide insight into the structural determinants governing Akt isoform selectivity, and establish molecular hybridization as a strategy for selective covalent targeting of Akt3. - Source: PubMed
Publication date: 2026/09/29
Pervanidis Kosmas AlexandrosD'Angelo Giovanni DaniloAthanasiadis IoannisJantzen HannahScrima AndreaSchäfer KatharinaQuambusch LenaMüller Matthias PRauh Daniel - Hydrophobic tag degraders (HyTDs) are a promising strategy for achieving targeted protein degradation (TPD). HyTDs are composed of a hydrophobic moiety conjugated via a linker to a ligand that binds to the protein of interest (POI). Binding induces a surface-exposed hydrophobic patch that mimics a misfolded protein, triggering degradation through the cell's diverse quality-control networks, including the ubiquitin-proteasome system (UPS), ubiquitin-independent proteasome degradation (UbInPD), the autophagy-lysosome pathway (ALP), and the unfolded protein response (UPR). This distinct multi-pathway mechanism distinguishes HyTDs from traditional TPD strategies such as PROTACs and molecular glue degraders (MGDs), which rely on a narrow pool of specific E3 ligases. The effectiveness of HyTDs is influenced by the chemical properties of the hydrophobic moiety, the linker, and the ligand's binding kinetics to the POI. To date, several relevant cancer targets, including the androgen receptor (AR), AKT serine/threonine kinase 3 (Akt3), and enhancer of zeste homolog 2 (EZH2), have been successfully targeted using HyTDs. Gaining deeper mechanistic insight into the nature of HyT degradation will be essential to further the potential of HyTDs as powerful tools in cancer research and therapeutics. - Source: PubMed
Publication date: 2026/09/17
Aguilera-Pineda TaniaKumar SiddharthaGhosal GargiNatarajan AmarnathKarpf Adam R - Bergenin (BN), a C-glucoside of 4-O-methyl gallic acid, exhibits a broad spectrum of pharmacological activities, including notable antioxidant, anti-inflammatory and anticancer effects. - Source: PubMed
Yang KaihuaZhou Leyuan - Insulin attenuates the effects of advanced glycation end products (AGEs) by inducing a disintegrin and metalloprotease 10 (ADAM10)-mediated cleavage of the receptor for AGEs (RAGE); however, the molecular mechanism underlying this process remains incompletely understood. We investigated the mechanism by which insulin promotes ADAM10-mediated RAGE shedding in cultured human aortic endothelial cells (HAECs). AGE-modified bovine serum albumin (AGE-BSA) increased intercellular adhesion molecule-1 (ICAM-1) expression, whereas insulin pretreatment (0.1-100 nM) attenuated this effect. Mechanistically, insulin activated AKT1, AKT2, and AKT3, promoted ADAM10 translocation to the cell surface, and enhanced RAGE ectodomain shedding. In contrast, treatment with GI254023X (an ADAM10 inhibitor) or ADAM10 knockdown using siRNA abolished insulin-induced RAGE ectodomain shedding. Likewise, knockdown of AKT1, AKT2, or AKT3 using siRNA, as well as treatment with the pan-AKT inhibitor MK-2206, inhibited insulin-induced ADAM10 cell surface translocation and RAGE ectodomain shedding. Co-immunoprecipitation analysis further demonstrated an interaction between Rab14 and ADAM10. Insulin enhanced this interaction and promoted the translocation of both Rab14 and ADAM10 to the cell surface. Conversely, Rab14 knockdown blocked insulin-induced ADAM10 cell surface translocation and RAGE ectodomain shedding, thereby abolishing the protective effect of insulin against AGE-BSA-induced ICAM-1 expression. Collectively, these findings demonstrate that insulin promotes Rab14-mediated trafficking of ADAM10 to the cell surface through AKT activation in HAECs, resulting in enhanced RAGE ectodomain shedding. - Source: PubMed
Publication date: 2026/09/18
Baek Chung HeeKim HyosangMoon Soo YoungLee Eun KyoungYang Won Seok - Non-small-cell lung cancer (NSCLC), the predominant histological subtype accounting for more than 85% of lung cancer cases, remains the leading cause of cancer-related mortality worldwide. Despite the clinical advances afforded by targeted therapies, the frequent emergence of oncogenic driver mutations drives drug resistance and therapeutic failure, underscoring the critical need for novel molecular targets and alternative therapeutic strategies. AKT1, a serine/threonine kinase and central effector of the PI3K/AKT/mTOR signaling cascade, regulates key oncogenic processes including cell growth, survival, proliferation, and apoptotic evasion, and dysregulated hyperactivation is observed in 30-75% of NSCLC cases. Selective allosteric inhibition of AKT1, which targets the unique PH-kinase domain interface rather than the highly conserved ATP-binding pocket, has emerged as a more isoform-specific and therapeutically advantageous strategy compared with pan-AKT or ATP-competitive inhibition. In the present study, a ChemDiv AKT1-targeted compound library comprising 14,043 small molecules was subjected to hierarchical structure-based virtual screening using sequential high-throughput virtual screening (HTVS), standard precision (SP), and extra precision (XP) docking protocols, followed by binding free energy calculations using the MM-GBSA method. The top XP-ranked compounds, compound 1 (docking score: -11.771 kcal/mol), compound 2 (-11.428 kcal/mol), and compound 3 (-11.167 kcal/mol), achieved more favourable XP docking scores at the AKT1 allosteric site (PDB ID: 3O96) than established pan-AKT inhibitors, including MK-2206, miransertib, Bay1125976, and vevorisertib, although MM-GBSA rescoring did not reproduce this ordering. Comparative docking against the allosteric sites of AKT2 and AKT3 revealed a consistent preference for AKT1 across all three compounds, with a magnitude closely comparable to that of the reference allosteric ligand Inhibitor VIII, whose experimentally determined isoform rank order the protocol reproduced. Comprehensive 300-ns all-atom molecular dynamics (MD) analysis, encompassing RMSD and RMSF profiling, principal component analysis, dynamic cross-correlation matrix analysis, free energy landscape evaluation, and protein-ligand contact profiling, consistently demonstrated that compounds 1 and 2 maintain stable, high-affinity interactions with AKT1, exhibiting persistent engagement with the critical allosteric residues Trp80 and Tyr272 throughout the simulation trajectory. Furthermore, both compounds exhibited favourable pharmacokinetic profiles with predicted human oral absorption values over 80%, supporting their potential for preclinical development. - Source: PubMed
Publication date: 2026/09/08
Das RajuSultana ArminDas KantuChowdhury DipannitaChoi Seong WooWoo Joohan