SIRT2 antibody - N-terminal region (ARP32384_T100)
- Known as:
- SIRT2 (anti-) - N-terminal region (ARP32384_T100)
- Catalog number:
- arp32384_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SIRT2 antibody - N-terminal region (ARP32384_T100)
Related genes to: SIRT2 antibody - N-terminal region (ARP32384_T100)
- 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 - N-terminal region (ARP32384_T100)
Related articles to: SIRT2 antibody - N-terminal region (ARP32384_T100)
- Ferroptosis is a non-apoptotic form of cell death characterized by cellular accumulation of iron-dependent lipid peroxidation. In recent years, a series of studies have proved that ferroptosis participate in the progression of chronic kidney disease (CKD). Notably, cognitive dysfunction is commonly found in CKD patients and it has been recognized as one of CKD pathological features. However, the character of ferroptosis in CKD related cognitive dysfunction remains unclear. This study aims to verify if ferroptosis participates in the CKD related cognitive dysfunction and the underlying mechanism. Then we use Fer-1 and Erastin to explore the effects of ferroptosis on cognition changes in CKD rat. RNA-seq analysis identified ferroptosis related lipid metabolism was significantly changed in CKD rats and the DEGs played an important role in oligodendrocyte differentiation, which were correlated with cognition ability. Fer-1 ameliorated the ultrastructure of hippocampal CA1 region and rescued the myelin sheath injury in CKD rats. Specifically, Fer-1 increased the density of myelinated axons and upregulated the levels of MBP and SOX10 in hippocampus of CKD rats. Notably, Fer-1 decreased the expression of Sirt2 and the AAV-Sirt2 abrogated the beneficial effects of Fer-1 on ferroptosis and myelin sheath in the hippocampus of CKD rats. This study provides a new strategy for improving cognitive dysfunction in CKD. - Source: PubMed
Publication date: 2026/08/15
Yu HuanZhang Chao-YangCai YanLiu YingWu NingWang Wen-JuanCai Guang-YanWang Yuan-Cheng - Age-related metabolic dysregulation, chronic inflammation, and impaired vascularization severely compromise critical-sized bone healing. Building upon G-PLA nanocomposites previously established for bioelectronic encapsulation, we herein investigate their potential as a bio-instructive interface for guided bone regeneration. Fabricated via in situ graphite exfoliation, G-PLA provides enhanced hydrophilicity, mechanical robustness, and bioactivity while preserving excellent 3D-printability. In rat cranial defects, G-PLA significantly accelerated regeneration, as demonstrated by micro-CT, histological, and immunohistochemical analyses. Comparative evaluations in young and aged animals revealed that G-PLA effectively mitigates age-dependent declines in reparative capacity. Proteomic profiling indicated that G-PLA orchestrates a pro-regenerative microenvironment by inducing glycolytic reprogramming to meet the elevated energy demands of regeneration. In aged defects, G-PLA upregulated glycolytic enzymes (e.g., ALDOA and HK2), enhanced angiogenesis (CD31/CD34), and suppressed inflammation- and senescence-associated markers (e.g., P21 and SIRT2). In vitro studies validated that G-PLA augments glycolytic flux in endothelial cells, enhances osteogenic differentiation of mesenchymal stem cells, and promotes macrophage polarization toward an anti-inflammatory M2 phenotype. Therefore, G-PLA nanocomposites transcend passive structural support to act as a bio-instructive interface that revitalizes the aging-associated vascular-bone coupling, offering a versatile framework for next-generation multifunctional implantable hybrid systems. - Source: PubMed
Publication date: 2026/08/13
Wang MengjiaZhang YanghengPan HaiyangXu ShuoyangZou YantingPeng ZhiweiJiang HaichangZhu ZhenYang WenrongLi YanfenSun LitaoHong HuaYan Fuhua - Sirtuins (SIRTs) are NAD-dependent enzymes implicated in cancer and other diseases, but the high conservation of their catalytic sites complicates the development of isoform-selective inhibitors. BZD9L1 is a benzimidazole-based sirtuin inhibitor with previously reported activity against SIRT1 and SIRT2. However, its potential interactions with other human sirtuin isoforms remain incompletely characterized. Here, we applied a comparative structure-based modelling framework integrating homology modelling, molecular docking, and targeted experimental assessment to investigate plausible binding modes of BZD9L1 across human SIRT1-7. Docking predicted that BZD9L1 could occupy the ADP-ribose cofactor-binding region of all seven isoforms, with broadly conserved orientations but differences in the predicted interaction networks. Hydrogen-bonding and π-mediated contacts predominated in the selected SIRT1-3 poses, whereas hydrophobic contacts were more apparent in several selected SIRT4-7 poses. The modest differences in docking scores were interpreted qualitatively and do not establish differential binding affinities or isoform selectivity. In colorectal cancer cells, BZD9L1 treatment altered acetyl-SOD2 levels, consistent with altered SIRT3-associated deacetylation in a cellular context. In a separate cell-free enzymatic assay, no measurable SIRT5 inhibition was detected under the conditions tested. These complementary assays provided distinct, independently interpreted readouts of SIRT3-associated cellular activity and SIRT5 enzymatic activity. Collectively, this study provides testable structural hypotheses regarding BZD9L1 recognition by human sirtuins and identifies interaction features that may guide subsequent biochemical and structure-based investigations. - Source: PubMed
Publication date: 2026/07/30
Tan Yi JerLee Yeuan TingOon Chern EinMancera Ricardo L - Myocardial ischemia-reperfusion injury (MIRI) is an inevitable pathological complication following reperfusion therapy for acute myocardial infarction. Massive reactive oxygen species burst, mitochondrial dysfunction, inflammatory cascade activation and multiple programmed cell death jointly aggravate irreversible cardiomyocyte loss, expanding infarct size and increasing the risk of progressive heart failure. As conserved NAD⁺-dependent deacetylases, the seven-member sirtuin (SIRT1-SIRT7) family exert widespread cardioprotective effects against MIRI, yet the subtype-specific molecular mechanisms, coordinated regulatory networks and translational bottlenecks lack systematic collation in existing reviews. This review aims to systematically summarize the regulatory pathways of all SIRT isoforms governing oxidative stress, mitochondrial homeostasis, inflammatory response and programmed cell death under MIRI, compare divergent biological functions among subtypes, sort out available SIRT-targeted pharmacological intervention strategies, and further clarify major obstacles restricting clinical translation, as well as prospective therapeutic targets for subsequent research. Distinguished by subcellular localization, nuclear, cytoplasmic and mitochondrial SIRT members participate in multi-layered myocardial defense. Nuclear SIRT1 coordinates AMPK-FOXO3-Nrf2 signaling to upregulate antioxidant enzymes and maintain mitophagic balance; mitochondrial SIRT3 dominates PINK1/Parkin-dependent mitophagy and deacetylates SOD2 to eliminate mitochondrial reactive oxygen species; cytoplasmic SIRT2 alleviates endoplasmic reticulum stress and restrains NLRP3 inflammasome activation; mitochondrial SIRT4 and SIRT5 stabilize mitochondrial fusion dynamics and eliminate lipid peroxidation via lysine desuccinylation, respectively; nuclear SIRT6 and SIRT7 relieve reperfusion inflammation, repair oxidative DNA damage and block late myocardial fibrosis. Collectively, the whole SIRT family forms an integrated endogenous protective network targeting all core pathological links of MIRI. In conclusion, SIRT1, SIRT3 and SIRT6 act as core cardioprotective subtypes: they synergistically activate the AMPK/Nrf2 antioxidant axis to block reperfusion oxidative injury. SIRT2, SIRT4, SIRT5 and SIRT7 serve auxiliary regulatory roles by balancing cardiac energy metabolism and maintaining genomic integrity. Current SIRT small-molecule agonists face prominent translational limitations including low oral bioavailability and poor myocardial tissue selectivity. Mitochondria or cardiomyocyte-targeted nano-delivery systems provide a feasible strategy to overcome such defects. Large animal MIRI models and prospective human clinical trials are urgently required to validate the long-term safety and therapeutic efficacy of SIRT-targeted interventions before clinical transformation. - Source: PubMed
Publication date: 2026/08/12
Xue TingtingWang ShuZhu XinyuLuo JialiZhu RuixiangLi HuihuiJu RuotongZhang PuhuaCui XiangrongJing Xuan - Impaired oligodendrocyte precursor cell (OPC) differentiation limits myelin renewal in aging and contributes to multiple sclerosis (MS) progression. How aging drives OPC deficits remains incompletely understood. We find dysregulation of genes associated with the circadian clock, including Bmal1, and metabolism in aged compared with young OPCs. Targeted loss of Bmal1 in OPCs drives metabolic dysfunction, leading to cellular senescence and impaired dynamics. OPC proliferation and differentiation occur at different rates throughout the day in young adult mice and become disrupted with aging. Chronotherapeutic targeting of BMAL1-controlled sirtuin signaling restores Bmal1-disrupted OPC dynamics after demyelination via sirtuin 2 (Sirt2)-dependent mechanisms. Induced pluripotent stem cell (iPSC)-derived OPCs from MS patients and MS lesion oligodendroglia recapitulate BMAL1 and SIRT2 disruptions. These findings establish BMAL1 as a key regulator of OPC energy metabolism, sirtuin homeostasis, and senescence. We anticipate that this work will provide a foundation for future studies investigating the interconnected roles of aging, circadian disruption, and myelin biology. - Source: PubMed
Publication date: 2026/08/07
Dierckx TessWilson Sarah EBuchanan RebeccaTsarouchas Themistoklis MCheng YuhsiangNunez Maria SacconiStrickland KellyKumsa DenaAuguste Yohan S SVanherle SamBouwman SanderRojo DanielaDal Cengio LouisaLerma-Martin CeliaMohammed YasseneSchirmer LucasBogie Jeroen F JEggen Bart J LGibson Erin M