AKT2 purified human protein
- Known as:
- AKT2 enriched H. sapiens protein
- Catalog number:
- RP10172
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- AKT2 purified human protein
Related genes to: AKT2 purified human protein
- 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 purified human protein
Related articles to: AKT2 purified human protein
- Protein kinase B, more commonly known as Akt, is a family of three serine/threonine kinases (Akt1, Akt2, and Akt3) that play a central role in regulating processes such as proliferation, survival, metabolism, and migration through phosphorylation of downstream targets. Given its involvement in numerous cellular processes, aberrant Akt signaling is prevalent across multiple cancer types, underscoring the need for Akt kinase assays to assess activity, regulatory mechanisms, and the efficacy of targeted interventions. Most existing Akt kinase assays rely on expensive commercial kits, some of which employ pre-purified, constitutively active Akt expressed in insect cells, bypassing physiologic autoinhibition of Akt; therefore, they are not suitable for evaluating allosteric inhibitors or context-dependent regulation. Here, we describe a detailed, step-by-step protocol for a nonradioactive Akt kinase assay using epitope-tagged, recombinant Akt1 expressed in a mammalian cell line and isolated by immunoprecipitation. This method eliminates the need to co-express Akt with upstream regulatory kinases or to purify active enzyme from insect cells, a time-consuming and technically demanding process, particularly when analyzing multiple Akt mutants. Because Akt is assayed in a regulated, autoinhibited state, this protocol enables direct evaluation of allosteric inhibitors that cannot be assessed using active Akt purified from insect cells. We note, however, that Akt1 kinase activity in this assay is measured from epitope-tagged, transiently overexpressed protein, which could influence cellular signaling dynamics. Despite this limitation, the cellular context preserves key regulatory features of Akt1 autoinhibition and membrane-dependent activation that are absent in assays using purified, pre-activated kinase. Together, this protocol supports analysis of Akt kinase activity under diverse experimental conditions, including receptor stimulation, pharmacologic treatment, allosteric inhibitor exposure, and mutations, using an accessible, economical, and physiologically relevant approach. Key features • This protocol is broadly accessible, requiring only standard laboratory equipment and commonly used techniques without specialized instrumentation or purified kinase preparations. • This protocol measures Akt1 catalytic output by assessing substrate phosphorylation following immunoprecipitation of transiently expressed, epitope-tagged Akt1 from cells. • The assay is performed in a low-throughput format and provides a semiquantitative readout. • This protocol can be adapted to other mammalian cell lines and optimized for other protein kinases of choice. - Source: PubMed
Publication date: 2026/07/05
Peek AmberMehta Jay NBhandari Deepali - The serine/threonine kinase AKT is a key regulator of glucose and energy metabolism. Prevailing dogma suggests that AKT is an obligate intermediate for glucose uptake in all metabolic tissues and that impaired AKT signalling is a major molecular driver of insulin resistance in obesity. However, whether AKT is universally required for insulin-stimulated glucose uptake across tissues in vivo has remained unresolved. - Source: PubMed
Jaiswal NatashaGavin MatthewLantier LouiseOng Olivia Yu YuWasserman David HTitchenell Paul M - Targeting aberrantly activated kinases in pleural mesothelioma (PM) is a promising therapeutic strategy. To identify potential candidates, we characterized recurrent chromosomal gains in PM and subsequently evaluated the specific inhibition of kinases that were activated by amplification and/or overexpression. - Source: PubMed
Publication date: 2026/06/28
Kalla ClaudiaMönch DinaSteinlein SophiaPastore AlessandroHorn HeikeFalkenstern-Ge RogerSchüler JuliaOtt GermanPreissler Gerhard - Pyrola incarnata, a medicinal herb and functional food with diverse bioactive compounds, was systematically screened for in vitro anti-RSV activities of its constituents, combined with antiviral assays and computational analyses. Among ten compounds, pyrolin, gallic acid, and quercetin as main phytochemicals showed the most potent efficacy, with IC values of 0.56 ± 0.08 μM, 10.60 ± 1.08 μM, and 12.63 ± 1.00 μM, respectively, outperforming positive control ribavirin. Indirect immunofluorescence and high-content analysis indicated these three compounds target the early RSV replication cycle. Gallic acid showed inhibited RSV infection during virus pretreatment and adsorption, with inhibition rates of 72.79% and 48.25% (P < 0.01), respectively. Furthermore, gallic acid suppressed early post-infection replication, and mechanistically it disrupted RSV-F protein mediated membrane fusion, reducing cell-cell fusion to 22.52%, consistent with docking results. Moreover, exploratory network pharmacology suggests that gallic acid might exert anti-RSV effects by modulating targets such as MAPK, AKT1, and AKT2. In additional, it was discovered for the first time that pyrolin as the one of the component indicators from P. incarnata, markedly inhibited RSV infection during virus pretreatment and adsorption, with inhibition rates of 94.50% and 43.50% (P < 0.01) respectively. While quercetin also exhibited direct virucidal activity. In conclusion, P. incarnata acts as promising natural inhibitors targeting the early stages of RSV replication. These findings establish a scientific basis for future in vivo validation and the development of new drugs against respiratory syncytial virus. - Source: PubMed
Publication date: 2026/06/26
Yang XiliangWu LiWan GuoqingChen RuiLiu ChenxuZhang HaiweiZhang ZheZhou YiDuan LixinGong Rui - This study aimed to investigate the effects and mechanism of polysaccharides (SLPs) on hepatic glucose metabolism disorders induced by a high-fat diet combined with streptozotocin (STZ) in mice. A mouse model of hepatic glucose metabolism disorder was established and treated with different doses of SLPs (100, 200, and 400 mg/kg) via gavage for 8 weeks, alongside control, model, and positive control groups (metformin hydrochloride). The effects of SLPs were systematically evaluated through pyruvate tolerance tests (PTT), hepatic glycogen content measurement, liver histomorphological analysis (HE and oil red O staining), transcriptomics, and validation of key signaling pathways using RT-qPCR and Western blot. The results showed that, compared to the model group, medium and high doses of SLPs significantly reduced area under the curve (AUC) of PTT, increased hepatic glycogen content, and ameliorated liver histopathological damage and lipid accumulation in the liver. Transcriptomic analysis revealed that SLPs intervention significantly modulated differentially expressed genes related to glucose and lipid metabolism, which were enriched in signaling pathways such as phosphatidylinositol-3-kinase (PI3K)/protein kinase B (AKT)/forkhead box O1 (FOXO1) signaling pathway. Further validation demonstrated that SLPs up-regulated mRNA expression levels of insulin-like growth factor 1 receptor (), protein kinase B2 (), and phosphatidylinositol-3-kinase regulatory subunit 1 () in the liver of mice with glucose metabolism disorders, and down-regulated the mRNA expression levels of and fructose-1,6-bisphosphatase 1 (). Additionally, SLPs up-regulated p-FOXO1 protein expression level and down-regulated phosphoenolpyruvate carboxykinase (PEPCK) protein expression level. These results suggest that SLPs can effectively improve hepatic glucose metabolism disorders in mice induced by a high-fat diet combined with STZ by activating the PI3K/AKT/FOXO1 signaling pathway, involving the inhibition of key gluconeogenic enzymes and promotion of glucose utilization. - Source: PubMed
Yang Er-ChenJia Feng-YingZhang Li-MinJin Li-YangRen Dao-QinJiang YueYun Shao-JunFeng Cui-Ping