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
- 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 - The Min pig, a representative northern Chinese indigenous breed, carries a unique ancestral background shaped by the historical phylogeography of Northeast Asia. This study aimed to dissect the population structure, temporal genetic divergence, and ancestral composition of Min pigs, trace their evolutionary origin, and identify trait-linked functional genes, providing information regarding their evolutionary history and conservation. We analyzed 61 Min pigs sampled across nearly 20 years and 701 reference pigs comprising other Chinese indigenous breeds, Western commercial lines, and Chinese wild boars, using PCA, NJ phylogenetic analysis, Admixture, TreeMix, D-statistic, f4-ratio, and combined selection signature scans (sliding-window F, XP-EHH, and π-ratio). Clear genetic stratification was observed among Min pig subpopulations, reflecting long-term divergence under natural and artificial selection. PCA and Admixture (K = 2-4) separated East Asian indigenous and Western ancestral components, verifying an admixed Northeast Asian origin with a dominant ancient East Asian component and a Western component. Compared with early-2000s Min pigs, contemporary individuals are genetically closer to Western breeds and exhibit a more scattered structure due to shifted ancestral component proportions, further confirmed by D-statistic and f4-ratio values. We identified 321 differentiated SNP loci based on the Animal QTL database, corresponding to core candidate genes (AKT3, ACACA, MAP3K5, FGFR4, C3, and SERPINC1) enriched for meat quality, growth, reproduction, immunity, energy metabolism, and MAPK/PI3K-Akt/AMPK pathways. This study reveals Min pigs' admixed origin and temporal divergence, clarifying their Northeast Asian evolution and providing molecular markers for genetic monitoring and conservation. - Source: PubMed
Jin LongDong FengyiFeng ChengyueNing JiayiZhang XiaoranLiu WuyangChen ChangyiWang DaliBie LuyaoBai ChunyanSun HaoSun Boxing - The Akt family of serine/threonine kinases plays a crucial role in various cellular processes, including proliferation, survival, and metabolism. Three Akt isoforms (Akt1, Akt2, and Akt3) have distinct physiological roles, and while individual isoform dysregulation is disease-linked, unselective Akt inhibition leads to side effects. Here, we report the development of selective covalent-allosteric Akt inhibitors (CAAIs) targeting Akt2 and Akt3 while sparing Akt1. Guided by protein x-ray crystallography and molecular modeling, key structural differences within the allosteric pockets of the isoforms were identified and exploited in a structure-based design strategy. By stabilizing the inactive kinase conformation, CAAIs overcome the intrinsic selectivity limitations of ATP-competitive inhibitors. After biological characterization, the pyrazole-containing inhibitors emerged as the most potent and selective Akt2 inhibitors, while inhibitors with pyridines as an isoform-selective element were predominantly targeting Akt3 selectively. Importantly, these new inhibitors were also evaluated in patient-derived colorectal cancer organoids. Co-crystal structures of inhibitors bound to an engineered construct mimicking the Akt2 allosteric pocket elucidated the molecular basis of isoform selectivity, guiding further optimization. This work not only establishes a framework for the development of isoform-selective therapeutics but also highlights the potential for unraveling isoform-specific functions in signaling pathways relevant to cancer biology. - Source: PubMed
Publication date: 2026/09/07
D'Angelo Giovanni DaniloPervanidis Kosmas AlexandrosAthanasiadis IoannisLukianchikov VladimirScrima AndreaDepta LauraStier SaraMüller Matthias PFarin Henner FQuambusch LenaRauh Daniel - The 6th edition of the WHO Classification of Digestive System Tumours distinguishes amphicrine-like carcinomas (ALCs) from mixed neuroendocrine-non-neuroendocrine neoplasms (MiNENs). Acinar cell carcinomas (ACCs) with an intimately admixed and not separated neuroendocrine component comprising >30% of the tumour are classified as amphicrine-like ACCs (AL-ACCs). We characterised the genomic landscape of pancreatic ACCs and AL-ACCs to validate current classification and identify therapeutic targets. - Source: PubMed
Publication date: 2026/09/04
Kim ChankyungYun Hyun-NamKim DeokhoonJeong Byung-KwanShin JinhoYoo ChanghoonOh DongwookKim Kyu-PyoSong Tae JunSong Ki ByungLee Seung SooKim Song CheolHong Seung-Mo - Uterine leiomyomas (fibroids) are the third most common, hormone-dependent benign tumors characterized by abnormal cell proliferation and dysregulation of signalling pathways, particularly PI3K/AKT. S-Allylcysteine (SAC), a bioactive compound from aged garlic (Allium sativum), possesses anti-inflammatory and anticancer properties, but its effects on leiomyoma cells remain poorly understood. - Source: PubMed
Publication date: 2026/09/03
Narwal SoniaVashist AnumehaHooda ReetuSiwach KiranKaushik RohitRohilla GulshanKhatri NishaVashist Minakshi