MAP2K2 Antibody
- Known as:
- MAP2K2 Antibody
- Catalog number:
- 32045
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- MAP2K2 Antibody
Related genes to: MAP2K2 Antibody
- Gene:
- MAP2K2 NIH gene
- Name:
- mitogen-activated protein kinase kinase 2
- Previous symbol:
- PRKMK2
- Synonyms:
- MEK2
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-05
- Date modifiied:
- 2019-04-23
Related products to: MAP2K2 Antibody
Related articles to: MAP2K2 Antibody
- Hearing loss affects over 1.5 billion people worldwide and has substantial social, educational, and economic consequences. Although genetic studies have identified numerous hearing-loss-associated genes, the molecular changes accompanying noise-induced hearing loss (NIHL) remain incompletely understood. We characterized the adult mouse cochlear proteome following damaging noise exposure using nano-LC-MS/MS and an integrative bioinformatics workflow. Comparative profiling of normal-hearing and NIHL cochleae identified 1742 proteins and an 80-protein NIHL-associated signature comprising 49 quantitatively defined differentially abundant proteins and 31 condition-specific proteins. These proteins were organized into five functional groups encompassing metabolic and mitochondrial function, protein synthesis and ribonucleoprotein complexes, structural and synaptic organization, cell polarity and cytoskeletal remodeling, and regulatory and stress-responsive functions. Representative alterations included reduced HSPA9, a mitochondrial chaperone involved in protein homeostasis; changes in the RNA-associated proteins PRMT1 and CIRBP; reduced HAPLN1, associated with extracellular matrix organization; and altered MAP2K2, a signaling protein related to cell polarity; and increased SYNJ2. Comparison with an independent cochlear proteomic data set identified 39 of the 80 proteins as dysregulated, with 22 showing concordant directional changes. Single-cell transcriptomic mapping provided cellular context for 74 of the 80 protein-associated genes, while human genetic and disease annotations supported the prioritization of selected proteins associated with hearing or ear phenotypes. Together, these findings define a proteomic landscape of the noise-exposed cochlea and identify molecular candidates and cellular processes for further investigation of NIHL. - Source: PubMed
Batissoco Ana CarlaAlencar-Coutinho DanilloFerreira-Scatone Ana CarolinaDiogo-Cavassana StellaOiticica JeanneLezirovitz KarinaBento Ricardo Ferreira - This paper introduces an approach for inferring the gene regulatory networks in vortioxetine-induced glioblastoma cells to investigate vortioxetine's systemic effects. The approach uses an ordinary differential equation (ODE)-based inverse problem to evaluate the drug-induced gene interactions within the GLIOMA and ERBB pathways, which are deeply intertwined in cancers, by using time-series datasets. Time-series datasets were generated in triplicate at 0, 3, 6, 9, 12, and 24 h. The results of the ERBB pathway confirmed that was commonly activated, while , as a proto-oncogene in glioblastoma, was inhibited by genes across all three datasets. In particular, was commonly activated by in all three datasets. The results of the GLIOMA pathway confirmed that was commonly activated, while and , which are mostly overexpressed in human cancers, were inhibited across all three datasets. Additionally, an analysis of the independent datasets generated at 6 and 22 h after the vortioxetine injection identified the most distinct variable genes between the two time points: (1.96) and (-3.02) for the ERBB signaling pathway, and (1.30) and (-1.92) for the GLIOMA pathway. We conclude that vortioxetine, an antidepressant, decreases , a proto-oncogene involved in the ERBB signaling pathway, and , another proto-oncogene involved in the GLIOMA pathway, over time in glioblastoma cells. - Source: PubMed
Publication date: 2026/07/06
Kim Shinuk - Selective inhibition of MEK isoforms remains a central challenge in MAPK-targeted drug discovery, largely due to the structural similarity between MEK1 and MEK2. While MEK1 has been extensively characterized, the structural basis of MEK2-specific ligand recognition is not fully understood. Here, we present crystal structures of human MEK2 in complex with the noncompetitive inhibitor U0126 and the allosteric inhibitor refametinib at resolutions of 3.15 Å and 3.30 Å, respectively. Despite a conserved kinase fold, MEK2 exhibits isoform-specific features within the N-lobe β-sheet. Additional differences are observed in the relative orientation of the helix C and activation segment, and the helix F-supported regulatory spine. Structural differences are reflected in micromolar binding affinities for U0126 ( = 9.8 μM) and refametinib ( = 7.4 μM). Notably, a single N-lobe substitution (Thr87 in MEK2 versus Phe83 in MEK1) selectively enhanced U0126 binding. The MEK2 T87F mutant exhibited an approximately twofold increase in affinity, while refametinib binding remained largely unchanged. SEC-MALS analysis demonstrated that MEK2 predominantly exists as a monomer in solution, contrasting with the reported homodimeric behavior of MEK1. Molecular dynamics simulations supported these findings by revealing isoform-specific differences in oligomeric state-dependent flexibility and inhibitor-induced dynamics. Collectively, our findings define the structural basis underlying the differential inhibitor recognition of MEK2 and MEK1, providing mechanistic insight into isoform-selective MEK-targeted drug design. - Source: PubMed
Publication date: 2026/07/03
Cheon Sang WonHwang EunmiLee Gi BaekHeo YoonyoungKim Hyoun SookHan Byung Woo - The identification of cuproptosis offers novel insights into therapeutic strategies for neoplastic diseases. We explore whether cuproptosis and cuproptosis-related genes (CRGs) could provide novel perspectives for the prognosis and treatment of gastric cancer patients. - Source: PubMed
Publication date: 2026/06/25
Chen LinhuiWang ZiGuo YanjunLi ChenyangZhang Guoxin - Diabetic nephropathy (DN) is a leading cause of chronic kidney disease. Salvianolic acid A (SAA) has shown promising therapeutic potential against DN, yet its underlying mechanisms and precise molecular targets remain incompletely elucidated. Potential targets of SAA were predicted using SwissTargetPrediction and SuperPred, with its drug-like properties evaluated by ADMET analysis. Diabetic nephropathy (DN)-related targets were collected from GEO, CTD, and GeneCards databases. Shared targets underwent GO and KEGG enrichment analyses. Core targets were identified through topological analysis in Cytoscape, machine learning, and Mendelian randomization validation. Molecular docking and dynamics simulations assessed the binding affinity and stability between SAA and core targets. Single-cell RNA sequencing data revealed their cell type-specific expression in kidney tissues. Experimental validation was performed using an in vitro high glucose-induced podocyte injury model analyzed by RT-qPCR. The intersection of 212 drug targets with 5,097 disease targets yielded 134 potential therapeutic targets for salvianolic acid A in DN. Machine learning and Mendelian randomization further identified eight targets with causal relationships to DN. Molecular docking demonstrated strong binding affinities of salvianolic acid A to the domains of FYN, AKR1B1, TNF, GALK1, HMGCR, MAP2K2, SCN4A, and ITGA5. Single-cell analysis revealed distinct expression patterns across different renal cell types. In vitro experiments demonstrated that SAA effectively protected podocytes from HG-induced injury. SAA alleviates diabetic nephropathy through multi-target mechanisms, influencing key genes involved in disease progression. This study provides a systematic elucidation of the therapeutic basis for SAA and supports its further clinical development. - Source: PubMed
Publication date: 2026/06/24
Fu TongfeiXiong ZhiliTao HongwuZhan Yongli