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
- Host microRNAs (miRNAs) are widely proposed as innate antiviral effectors against SARS-CoV-2, yet whether they actually restrict infection in lung epithelial cells remains unresolved. Two of the most-cited candidates, miR-29a-3p and miR-15b-5p, are predicted to bind both the viral genome and key entry/trafficking factors such as Furin and ATG9A, but functional evidence is fragmented and often contradictory. Here, we put both miRNAs to the test in human Calu-3 cells infected with the SARS-CoV-2 Beta and Omicron BA.1 variants, using parallel gain- and loss-of-function strategies coupled to RT-qPCR of viral and cellular transcripts and back-titration of infectious progeny on VeroE6/TMPRSS2 cells. Both miRNAs transiently suppressed viral gene expression at 6 hpi, but this early dampening was followed by a marked transcript rebound at 24 hpi, especially for Omicron, with virtually no impact on total extracellular viral RNA. More strikingly, miR-15b modulation enhanced infectious virus output during Beta infection, and miR-29a overexpression boosted Omicron BA.1 infectivity, while Furin, ATG9A, AKT3, and TFEB showed only modest, condition-dependent shifts. Rather than acting as clean antiviral effectors, miR-29a and miR-15b emerge as context-dependent modulators that can paradoxically favor SARS-CoV-2 replication-a cautionary signal for miRNA-based antiviral strategies. - Source: PubMed
Publication date: 2026/06/29
Criscuolo ElenaMosca NicolaGiuliani BenedettaCastelli MatteoDi Palo ArmandoPezzullo MariacelesteBurioni RobertoRusso AnielloClementi NicolaPotenza Nicoletta - 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 - Gastric cancer (GC) remains a leading cause of cancer-related mortality worldwide, and the molecular mechanisms driving its progression are incompletely understood. Agmatinase (AGMAT) has recently emerged as a candidate oncogene in several malignancies; however, its functional role in GC has not been characterized. In this study, we investigated AGMAT's role in GC, focusing on its effects on cell proliferation, invasion, stemness, and the underlying signaling mechanisms. Using GC cell lines AGS and HGC-27, we demonstrate that AGMAT overexpression promotes proliferation and invasion of GC cells and enhances sphere formation, a hallmark of cancer stem-like properties. Conversely, AGMAT knockdown via shRNA markedly suppressed cell proliferative, invasive, and sphere-forming capacities. Mechanistically, AGMAT activates the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) signaling pathway, and pharmacological reactivation of this pathway using 740 Y-P rescued the proliferative, invasive, and stemness deficits caused by AGMAT depletion. In vivo studies using nude mice further corroborated our in vitro findings; AGMAT silencing led to a significant reduction in tumor volume and weight, accompanied by decreased expression of the proliferation marker Ki-67 and the stemness markers octamer-binding transcription factor 4 (OCT4) and SRY-box transcription factor 2 (SOX2) in AGMAT-silenced tumors. Furthermore, analysis of The Cancer Genome Atlas (TCGA) data revealed a correlation between elevated AGMAT expression and poor patient prognosis, reinforcing AGMAT's clinical significance in GC progression and patient outcomes. Collectively, our findings identify AGMAT as a novel oncogene that promotes GC cell proliferation, invasion, and stemness through PI3K/AKT pathway activation. These results suggest that AGMAT may serve as a potential therapeutic target and prognostic biomarker for GC. - Source: PubMed
Publication date: 2026/07/09
Li XinyuJia JingGuan ShenYang Chunkang - Psoriasis is a complex chronic inflammatory disease with cutaneous manifestations, driven by intricate interactions between genetic, immunological, and metabolic dysregulations. However, the integrated molecular networks connecting transcriptional alterations to metabolic reprogramming remain incompletely elucidated. - Source: PubMed
Publication date: 2026/07/07
Zheng HongkaiXue RujunLi WeiSima XiaonanLiang JingyaoZhang Sanquan - Sepsis-associated acute kidney injury (SA-AKI) is a significant clinical challenge due to its prevalence in intensive care units. This study evaluated the diagnostic utility of serum miR-151a-3p for SA-AKI, aiming to provide new insights into early diagnosis and mechanistic research. - Source: PubMed
Publication date: 2026/07/06
Tian YongyangZhu HaiyuanWang JinhuiWang LilinLiu LiGui Xiao