SIRT2 Antibody
- Known as:
- SIRT2 Antibody
- Catalog number:
- 32057
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- SIRT2 Antibody
Related genes to: SIRT2 Antibody
- Gene:
- SIRT2 NIH gene
- Name:
- sirtuin 2
- Previous symbol:
- SIR2L
- Synonyms:
- -
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-14
- Date modifiied:
- 2016-10-05
Related products to: SIRT2 Antibody
Related articles to: SIRT2 Antibody
- Serine/arginine-protein kinase 1 (SRPK1) is a central regulator of alternative splicing whose overexpression drives oncogenic reprogramming in multiple cancers. To understand the phosphorylation dynamics of SRPK1 activity, we performed a systematic integrative phosphoproteomic meta-analysis of 798 profiling and 232 differential human datasets. We identified S51, S309, and S311 as the three predominant Class I phosphosites on SRPK1. High-confidence co-phosphoregulated proteins (Fisher's Exact Test < 0.05, ≥3 independent studies, ≥3 experimental conditions) revealed an extensive network of splicing factors (SRRM1, SRRM2, GPATCH8) and noncanonical RS-domain proteins (LBR) that function as both substrates and binary interactors, preferentially linked to S309 and S311. Proteogenomic interrogation via cProSite demonstrated significant upregulation of phosphorylation at these sites in breast, ovarian cancer and lung adenocarcinoma cohorts. Downstream substrates and co-regulated proteins further intersected with apoptosis regulators like SIRT2, BAD, FOXO3, and PI3K/Akt pathway components, mechanistically hinting at SRPK1 phosphorylation in apoptosis suppression and uncontrolled proliferation. These co-phosphorylation signatures therefore position SRPK1 as a potential orchestrator of splicing condensates that rewire oncogenic pathways, offering a phosphosite-specific blueprint for targeted splicing modulators and combination immunotherapies in splicing-related malignancies. - Source: PubMed
Publication date: 2026/09/24
Vijayan JishnaSubair SuhailGopalakrishnan Athira PerunellySambreena AlimathRaju RajeshRajeev Athira C - A series of pyrazolyl-thioureas was designed and synthesized as novel sirtuin 1 (SIRT1) and sirtuin 2 (SIRT2) inhibitors. Compounds were prepared through a multistep, divergent procedure starting from amino pyrazole intermediates. Biological evaluation revealed that several derivatives exhibited significant SIRT2 inhibitory activity, with compounds 6a and 7f emerging as the most promising inhibitors, showing IC values of 2.2 and 13.6 µM, respectively. Selected compounds displayed selective antiproliferative activity against HepG2 hepatocellular carcinoma cells, while showing limited cytotoxicity toward normal fibroblasts. The biological properties of 6a and 7f were further investigated by analyzing SIRT1 activity and correlating antiproliferative activity with tubulin acetylation. Docking simulations identified the molecular basis of SIRT1 and SIRT2 inhibition. Overall, these results identify pyrazolyl thioureas as a promising scaffold for novel SIRT1 and SIRT2 inhibitors with potential anticancer applications. - Source: PubMed
Lusardi MatteoAstigiano CeciliaBellitto DeianiraRaineri MatteoGuccione GiorgiaSalis AnnalisaCichero ElenaBrullo ChiaraPonassi MarcoBruzzone SantinaSpallarossa Andrea - To evaluate morphologic and quantitative MRI features associated with seromucinous and mucinous ovarian tumors of benign and borderline histology, with emphasis on their complementary role within structured preoperative imaging assessment. - Source: PubMed
Publication date: 2026/09/18
Özyılmaz SafaKulalı Fatma - Metabolic dysfunction-associated steatotic liver disease (MASLD) is a leading cause of hepatocellular carcinoma (HCC), but how metabolic zonation drives regional transformation remains unclear. We identify sirtuin 2 (SIRT2) as a zonated cholesterol sensor that initiates reprogramming to drive MASLD-HCC. Lineage tracing establishes zone 1 hepatocytes as the cellular origin of tumors. SIRT2 overexpression in zone 1 triggers HCC, whereas its deletion prevents carcinogenesis by restoring cholesterol and bile acid metabolism and CD8 T cell recruitment. Mechanistically, cholesterol binds and activates SIRT2, which deacetylates sterol carrier protein 2 (SCP2) at Lys546, thereby blocking peroxisome proliferator-activated receptor α (PPARα) recruitment to the Cyp7b1 promoter, suppressing alternative bile acid synthesis, and permitting 27-hydroxycholesterol accumulation. SIRT2 inhibition reverses this cascade in mice and human hepatic organoids. Patient specimens confirm zonal SIRT2 and cytochrome P450 7B1 (CYP7B1) dysregulation. Our findings establish spatially compartmentalized cholesterol sensing as a new regulatory layer and identify SIRT2 as a druggable target in liver cancer. - Source: PubMed
Publication date: 2026/09/17
Zhang YingtingLong XidaiFu YinkunTang XinxinLuo HaoZou ZhihuiHe WeiHan LongchuanLi YueLuo JingTian LihongLu YuhengChen YiPan RimingBao XinyuLuo YuruiHuang ZonglinZhang ZhenwuLiu YonghuiFeng LiHuang YingLin Chao-PoZhang JianChen GuoqiangHe Ming - Aspirin, as the most widely used drug in the world, has been reported to exert antiplatelet, anti-inflammatory, and anti-tumor effects. However, apart from the hydrolyzed acetyl group acetylating proteins, and salicylic acid functioning as a classic COX enzyme inhibitor, it is unknown whether the salicylic group of aspirin could participate in the salicylation of histone lysine. Herein, we discover and characterize lysine salicylation (Ksa) in histone and 39 Ksa sites of histone were mapped in 3 cell lines. Ksa could be stimulated by aspirin via direct action and conversion to salicyl-CoA, and regulated by CBP and SIRT2 in vivo. Multi-omics analyses reveal associations between histone Ksa enrichment and transcriptional changes in physiologically relevant genes. Moreover, immunohistochemistry of Ksa levels in bladder cancer tissues are associated with aspirin exposure and show a preliminary correlation with recurrence-related outcomes. Collectively, we discover a new histone mark with potential physiological relevance and may reveal a previously unrecognized mechanism underlying the non-canonical functions of aspirin. - Source: PubMed
Publication date: 2026/09/16
Zhang FacaiZhou ChuanzanHe JiaoyanHuang PengpengZhang RongHu HuanJiao MengHu LinyiLiu FengQi XiaolongHe XiangYang YunkaiChinn Y EugeneFeng DechaoZhang DahongZhang Qi