SIRT2 antibody - C-terminal region (ARP32385_P050)
- Known as:
- SIRT2 (anti-) - C-terminal region (ARP32385_P050)
- Catalog number:
- arp32385_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SIRT2 antibody - C-terminal region (ARP32385_P050)
Related genes to: SIRT2 antibody - C-terminal region (ARP32385_P050)
- 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 - C-terminal region (ARP32385_P050)
Related articles to: SIRT2 antibody - C-terminal region (ARP32385_P050)
- Peripheral arterial disease (PAD) is characterized by impaired angiogenesis, yet the molecular mechanisms linking metabolic dysregulation to epigenetic reprogramming in endothelial cells (ECs) remain poorly understood. Here, we identify hexokinase 2 (HK2) as a critical regulator of angiogenesis through histone lactylation in PAD. In clinical specimens and murine hindlimb ischemia (HLI) models, HK2 expression was significantly downregulated. Functional assays in hypoxia-serum starved (HSS) human umbilical vein ECs (HUVECs) demonstrated that HK2 overexpression rescued angiogenesis by enhancing proliferation, migration, tube formation, and pro-angiogenic protein expression (VEGFA), while HK2 knockdown suppressed these phenotypes. Mechanistically, HK2 deficiency selectively reduced histone H3 lysine 18 lactylation (H3K18la) among eight tested histone lactylation sites, and HK2 restoration under HSS restored H3K18la level. Exogenous lactate reversed angiogenic defects in HK2-knockdown HUVECs by elevating H3K18la, which directly activated VEGFA transcription, as shown by Chromatin Immunoprecipitation coupled with quantitative Polymerase Chain Reaction (ChIP-qPCR). Furthermore, Sirtuin 2 (SIRT2), as a de-lactylase, inhibition in HK2-knockdown HUVECs restored H3K18la, angiogenesis, and pro-angiogenic protein expression. In HLI mice, SIRT2 inhibitor treatment improved blood flow recovery, increased EC density, and upregulated H3K18la. Our findings establish HK2 as a metabolic-epigenetic nexus driving angiogenesis via lactate-dependent H3K18la modification and propose SIRT2 inhibition as a novel therapeutic strategy to bypass HK2 deficiency in PAD. - Source: PubMed
Publication date: 2026/05/28
Chen JingWang YueWang XuanLi JinLiu YuZhou JipengLi ChuanchangWu WanzhouBai Yongping - This study aimed to examine the protective effects of kaempferol on the in vitro maturation (IVM) of bovine oocytes and their subsequent embryonic development, and to investigate the underlying mechanisms. Bovine oocytes were cultured with kaempferol at concentrations of 0, 0.01, 0.1, and 1 μM. Of the tested concentrations, the 0.1 μM kaempferol group consistently yielded the highest numerical rates of first polar body extrusion, cleavage, and blastocyst formation, although no statistically significant differences were detected among groups. Based on these preliminary screening experiments, only the optimal concentration (0.1 μM) was used in subsequent mechanistic assays. Further analyses demonstrated that 0.1 μM kaempferol significantly reduced oocyte apoptosis and intracellular reactive oxygen species levels. Meanwhile, it increased the glutathione content, adenosine triphosphate levels, and mitochondrial membrane potential of oocytes (P < 0.05). Gene expression analysis confirmed that 0.1 μM kaempferol upregulated antioxidant-related genes (SOD3, SIRT2), mitochondrial dynamics-associated genes (DNM1, MFN2), and the anti-apoptotic gene BCL-2, while downregulating the pro-apoptotic gene BAX (P < 0.05). Collectively, these results indicate that 0.1 μM kaempferol effectively alleviates oxidative stress and improves mitochondrial function in bovine oocytes, thereby showing potential to enhance oocyte quality. Although the improvements in developmental rates did not reach statistical significance under the current experimental conditions, the consistent numerical superiority of the 0.1 μM treatment, together with the robust molecular evidence, supports its further investigation as a promising supplement in oocyte IVM systems. - Source: PubMed
Publication date: 2026/05/25
Wang HongtaoWang WeixiaLi YongxinChen XiaoxinLiu JianqiangLiu YiLuan HuLv JunweiMa HairuiZhang PengjuLi XintaoZhang Lichun - Sirtuin 2, a NAD+-dependent deacetylase of the sirtuin family, has emerged as a pivotal regulator of brain physiology and pathology. Highly expressed in the central nervous system, sirtuin 2 exerts diverse and cell-type-specific functions in neurons, oligodendrocytes, astrocytes, and microglia. This review provides a comprehensive synthesis of current knowledge on sirtuin 2 within the central nervous system, emphasizing its multifaceted roles across different brain cell types and its potential as a therapeutic target in neurological disorders. In neurons, sirtuin 2 modulates axonal dynamics, mitochondrial function, and synaptic plasticity, displaying both neuroprotective and detrimental effects depending on context. In oligodendrocytes, sirtuin 2 is essential for differentiation, myelination, and axonal metabolic support via exosomal transfer, while its dysregulation contributes to hypomyelination and age-related myelin decline. In astrocytes, sirtuin 2 influences metabolism, senescence, and reactive gliosis, exerting protective effects under physiological conditions but potentially aggravating pathology after injury or in Alzheimer's disease. In microglia, sirtuin 2 modulates inflammatory responses, acting as either a suppressor or amplifier of neuroinflammation depending on the stimulus and disease context. The dual, sometimes opposing, functions of sirtuin 2 across central nervous system cell types underscore the complexity of its regulation and the need for context-dependent therapeutic approaches. By integrating evidence from genetic and pharmacological studies, this review delineates the cell-specific mechanisms through which sirtuin 2 influences central nervous system physiology and pathology. Understanding these heterogeneous and context-dependent actions is essential to harness the therapeutic potential of sirtuin 2 modulation in neurodegenerative, inflammatory, and demyelinating diseases. - Source: PubMed
Publication date: 2026/05/14
Garmendia-Berges MaiderPuerta Elena - -mediated clonal hematopoiesis of indeterminate potential (CHIP) is a known cardiovascular risk factor, but its role in cardiac aging and potential for pharmacological intervention remain unclear. Herein, Mendelian randomization using large-scale genome-wide association studies (GWAS) data assessed CHIP's causal impact on aging and cardiovascular disease that revealed significant causal associations between -CHIP, CVD, and aging biomarkers. Transcriptome-guided screening identified oridonin as a candidate compound reversing CHIP- and aging-associated gene signatures. Multi-tiered target prediction combining chemical structure-based algorithms and transcriptomic correlation identified KDM5C as a key target, validated by enzymatic inhibition and surface plasmon resonance assays. and administration of oridonin significantly ameliorated cardiac dysfunction and pathological remodeling in the CHIP model. Epigenetic regulation was profiled ChIP-seq and RNA-seq, focusing on H3K4me3-mediated transcription. BMT mice exhibited age-progressive myocardial fibrosis, inflammation, senescence, and functional decline. Mechanistically, oridonin inhibited KDM5C histone demethylase, restored H3K4me3 levels, and activated the SIRT2 anti-aging pathway. Rescue experiments using gene overexpression and recombinant protein supplementation confirmed the functional role of the KDM5C-H3K4me3-SIRT2-S100A8 axis in mediating oridonin's effects. Overall, -driven CHIP promotes cardiac aging, as evidenced by human genetic analyses and long-term BMT models. Oridonin, by inhibiting KDM5C and restoring H3K4me3-dependent SIRT2 signaling, mitigates CHIP-induced myocardial aging. - Source: PubMed
Publication date: 2026/02/10
Chen XinglingZhao QiangqiangChen LinhuangLin ShengrongMai BinHe XinglingZhang XiaojiaoChen JiahuiLi SijingLi ZiruZhang HuaZhou YuehuiLi XiaofangLiao HuiliYe TaochunSun ShuningYang ZhongqiNi ShihaoLu Lu - The effect of NAD in enhancing mitochondrial function and energy metabolism in human cells is closely linked to NAD-dependent sirtuins (i.e. SIRT1 and SIRT3). SIRT2 primarily functions in the cytoplasm, where it can serve as a key deacetylase for tubulin and modulates stability of microtubules. Microtubule plays a pivotal role in regulating mitochondrial dynamics, including mitochondrial movement, fission/fusion, repair, and mitophagy-dependent clearance. However, the potential role of NAD in modulating SIRT2-related microtubule stability, and the potential involvement of the NAD-SIRT2-microtubule axis in regulating mitochondrial and mitophagy functions remains unexplored. In this study, we demonstrate that senescent muscle cells exhibit microtubule hyper-stabilization and reduced dynamics, concomitant with SIRT2 inactivation and tubulin hyperacetylation. These alterations impair microtubule-dependent mitochondrial repair and mitophagy function, resulting in mtDNA leakage, CGAS-STING1 activation and subsequently accelerated senescence. Notably, treatment with nicotinamide mononucleotide (NMN) effectively reactivates SIRT2, restores microtubule dynamics, and enhances mitochondrial quality control by promoting repair and mitophagy. Consequently, NMN mitigates CGAS-STING1-driven senescence. Our findings reveal a novel mechanism by which NMN preserves mitochondrial health in senescent cells via a SIRT2-microtubule axis, highlighting its protective role beyond canonical NAD-sirtuin pathways, and suggesting microtubule dynamics as a promising therapeutic target for improving cellular defects associated with mitochondrial and mitophagy dysfunctions.: D-gal: D-galactose; EdU: 5-ethynyl-20-deoxyuridine; HDAC6: histone deacetylase 6; LAMP1: lysosome associated membrane protein 1; MSCs: mesenchymal stem/stromal cells; mtDNA: mitochondrial DNA; NAD: nicotinamide adenine dinucleotide; NMN: nicotinamide mononucleotide; PBS: phosphate-buffered saline; SA-GLB1/β-gal: senescence-associated galactosidase beta 1; SIRT2: sirtuin 2. - Source: PubMed
Publication date: 2026/05/24
Cui JieRen ShifengWang BingjieZhang NanZhu ShanshanZhang YajunQi XiangqingMeng WeixueShao LiweiGao ShanXing LijieLi ZengjunMu Xiaodong