Akt2 Antibody
- Known as:
- Akt2 Antibody
- Catalog number:
- 3155-100
- Product Quantity:
- 100 µg
- Category:
- Antibodies
- Supplier:
- Biovis
- Gene target:
- Akt2 Antibody
Related genes to: Akt2 Antibody
- Gene:
- AKT2 NIH gene
- Name:
- AKT serine/threonine kinase 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1992-11-05
- Date modifiied:
- 2016-10-05
Related products to: Akt2 Antibody
Related articles to: Akt2 Antibody
- 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 - AKT (protein kinase B, PKB) coordinates the balance between anabolic and catabolic signaling in skeletal muscle through distinct ubiquitin chain types. Some E3 ubiquitin ligases (E3s) and deubiquitinases (DUBs) form stable binary complexes via non-catalytic interfaces, adding a regulatory layer unavailable to either enzyme alone. This mechanistic synthesis review presents a systematic literature analysis (inception to May 2026; 26 eligible studies). It identified four E3-DUB pairs proposed to regulate AKT in skeletal muscle. These are TRAF6-CYLD (plasma-membrane K63-ubiquitination), MUL1-USP9X (mitochondrial K48-ubiquitination of AKT2), CHIP-UCH37 (proteasome-proximal quality control), and SCF-Skp2-USP37 (PHLPP1/2-dependent control of AKT Ser473 phosphorylation). All four interfaces are structurally separate from the catalytic sites and are regulated by upstream kinase phosphorylation. Evidence for the four pairs is markedly uneven. TRAF6-CYLD is supported by endogenous co-immunoprecipitation and functional data in muscle models. CHIP and UCH37 each act on AKT-related substrates independently and are individually well documented, but a direct CHIP-UCH37 interaction has not itself been demonstrated. SCF-Skp2-USP37 interaction data rest on a real but non-muscle direct interaction, whereas MUL1-USP9X has no reported direct interaction at all; CHIP-UCH37, SCF-Skp2-USP37, and MUL1-USP9X are therefore all presented as testable hypotheses of varying strength. In chronic atrophy, available data are consistent with disruption of these complexes contributing to AKT suppression through parallel, largely independent mechanisms. However, simultaneous disruption of all four has not been demonstrated in a single system. Available gene expression and protein datasets from sarcopenic muscle broadly support these predictions, though direct experimental validation in human tissue remains pending. This complex-centric framework recasts AKT ubiquitination as an integrated regulatory framework. Each structurally autonomous interface may represent a potentially distinct target for muscle-wasting conditions that currently lack approved therapies. - Source: PubMed
Dabur Rajesh - Although Angiotensin-(1-7) [Ang-(1-7)], a non-classical peptide of the renin-angiotensin system (RAS), is widely recognized for alleviating cardiovascular stress through activation of the Mas receptor. we identified a largely Mas receptor-independent pathway that expands its therapeutic potential in cardiac diseases. Our study demonstrated that Ang-(1-7) stimulated cardiomyocytes to release small extracellular vesicles (sEV), which exhibit enhanced cardioprotective effects compared with Ang-(1-7) administration alone. In both wild-type C57BL/6J mice and cardiac-specific Mas receptor knockout (cMas-KO) mice subjected to myocardial ischemia/reperfusion injury (MIRI), we found that enriched sEV preserved cardiac function by attenuating cardiomyocyte apoptosis and oxidative stress following MIRI. These protective effects remained evident even when Mas receptor signaling was pharmacologically inhibited or genetically ablated. Moreover, in wild-type mice with MIRI, enriched sEV provided significantly greater therapeutic efficacy in improving cardiac function than direct administration of Ang-(1-7). In AC16 human cardiomyocytes subjected to hypoxia/reoxygenation (H/R), enriched sEV enhanced Akt2 phosphorylation, increased sarco/endoplasmic reticulum Ca-ATPase (SERCA) activity, maintained calcium homeostasis, suppressed endoplasmic reticulum stress signaling (CHOP and p-JNK), and protected AC16 cells against H/R-induced apoptosis. sEV also attenuated oxidative stress under these conditions. Importantly, the protective effects of sEV remained after Mas receptor knockdown. Separately, Akt2 knockdown (Akt2KD) substantially weakened these benefits. These findings identify sEV as an promising therapeutic candidate, offering an effective, largely Mas-independent mechanism to combat MIRI with cardiomyocyte protection. - Source: PubMed
Publication date: 2026/08/28
Wu YalinWang XinZhao JianliYang HuiyuZhang WenjingYao ZhongSun YaoWang YajingLiang BinYang Zhiming - Akt1 and Akt2 isoforms reveal distinct immune-regulatory roles in HSV-1 pathogenesis. Akt3 is a developmentally important protein, and mutations in Akt3 gene are associated with a wide spectrum of developmental disorders, including extreme megalencephaly; however, its role in corneal homeostasis and pathologies remains poorly understood. Here we investigated the role of Akt3 in HSV-1 infection. - Source: PubMed
Publication date: 2026/08/12
Kadam RashmiPatil Chandrashekhar DBorase HemantRahangdale RakeshVolety IpsitaAkinsiku SoromidayoShukla Deepak - : Uterine dysfunction contributes to infertility in PCOS. Jiawei Qi Gong Wan (JQGW) is used to improve endometrial homeostasis, but its mechanism is unclear. This study investigated whether JQGW improves uterine function via gut microbiota and metabolites. : Letrozole-induced PCOS mice received JQGW (low/high dose), metformin, or vehicle for 35 days. Endometrial morphology, receptivity genes, Akt2/NF-κB signaling, gut microbiota (16S rRNA), and serum metabolites (LC-MS) were assessed. : PCOS mice showed reduced endometrial thickness (126.4 ± 10.8 μm vs. 215.6 ± 12.3 μm in controls, < 0.001) and fewer glands (12.6 ± 1.8 vs. 28.4 ± 2.1, < 0.001). JQGW-H increased endometrial thickness (189.3 ± 11.2 μm, < 0.01 vs. PCOS) and gland number (23.1 ± 1.9, < 0.01 vs. PCOS), restored the receptivity markers (, , , and ) toward normal levels, suppressed Akt2/NF-κB activation, and reduced inflammatory cytokines. JQGW shifted the β-diversity structure of the gut microbiota toward the control pattern, with enrichment (LDA > 4). Four metabolites (PA(20:0/16:1(9Z)), 7-methylguanosine, methoxyacetic acid, 8.11-eicosadiynoic acid) showed nominal elevation in PCOS and negative correlations with endometrial thickness (r = -0.73 to -0.89, unadjusted < 0.01), although none survived FDR correction. : JQGW ameliorates PCOS-associated uterine dysfunction, potentially via gut microbiota and metabolite modulation. Future studies should validate causality using fertility-based outcomes and microbiota transplantation. - Source: PubMed
Publication date: 2026/07/24
Zheng RuqunSong JinlongLi JieShen YingyanLiu QiqiShi MengjiaZhuo YuxuanLuo HaoyuLi JingMa HongxiaHu MinWang Chi ChiuLi Juan