SIRT1 antibody - N-terminal region (ARP32386_P050)
- Known as:
- SIRT1 (anti-) - N-terminal region (ARP32386_P050)
- Catalog number:
- arp32386_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SIRT1 antibody - N-terminal region (ARP32386_P050)
Related genes to: SIRT1 antibody - N-terminal region (ARP32386_P050)
- Gene:
- SIRT1 NIH gene
- Name:
- sirtuin 1
- Previous symbol:
- -
- Synonyms:
- SIR2L1
- Chromosome:
- 10q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-20
- Date modifiied:
- 2016-10-05
Related products to: SIRT1 antibody - N-terminal region (ARP32386_P050)
Related articles to: SIRT1 antibody - N-terminal region (ARP32386_P050)
- Medulloblastoma (MB) is the most common malignant pediatric brain tumor with poor prognosis, high recurrence, and severe treatment-related toxicities. One-third of MB are driven by aberrant activation of the Sonic hedgehog (SHH) signaling pathway. In current study, through analysis of clinical patient cohorts and animal model database, and utilizing genetically engineered primary and xenograft mouse MB models, we investigated the role of Sirtuin1 (Sirt1), a class III histone deacetylase (HDAC), in SHH signaling and MB. We found that Sirt1 was highly expressed in both human and mouse SHH-type MB, and its expression positively correlated with SHH pathway activity and tumor proliferation. Knockdown of Sirt1 in primary MB cells significantly suppressed SHH signaling and MB proliferation in vitro, further impaired neoplastic progression and extended survival in orthotopic transplantation MB model. Mechanistically, we discovered that Sirt1 modulates SHH signaling at downstream by interacting with and deacetylating full-length Gli3 (Gli3FL), thereby inhibiting its proteolytic processing into the repressor form (Gli3R), which attenuates the negative feedback regulation of SHH signaling, sustaining pathway activation and promoting tumor progression. Importantly, pharmacological inhibition of Sirt1 demonstrated promising therapeutic efficacy in both subcutaneous transplantation and primary MB models. Our findings identify Sirt1 as a potential therapeutic target for SHH-driven MB and other cancers. - Source: PubMed
Publication date: 2026/04/18
Hu JianZheng ChaonanFeng YingyingLi YuhangPei PanpanYang ManQu YanghuiZheng Long-TaiZhang LiZhen Xue-ChuWang Yuan - Ferroptosis promotes the progression of Parkinson's disease (PD) through its unique regulatory pathways. Biochanin A (Bioch A) has long attracted the attention of researchers due to its neuroprotective effects. However, whether Bioch A can treat PD by inhibiting ferroptosis and the underlying mechanism remain unclear. This study aimed to investigate whether Bioch A exerts a neuroprotective effect on PD by activating the Sirt1/Nrf2/GPX4 signaling pathway to inhibit ferroptosis. Behavior was evaluated by the open field and grip force tests in mice. Immunofluorescence staining, lipid peroxidation assay, transmission electron microscopy (TEM), cell viability assay, and Western blot were used to detect pathological changes and the expression levels of ferroptosis-related proteins in mice and SH-SY5Y cells. The results of the study indicate that Bioch A exerts a neuroprotective effect by improving iron metabolism, and restoring the imbalance of the antioxidant system, and reducing the production of lipid peroxides, thereby inhibiting ferroptosis. In addition, mechanistic validation showed that under the intervention of ML385 and EX527, Bioch A still maintained the activation of the Sirt1/Nrf2/GPX4 signaling pathway, thereby significantly inhibiting ferroptosis in SH-SY5Y cells. Collectively, this study confirms Bioch A exerts neuroprotective effects against PD by inhibiting ferroptosis through targeting the Sirt1/Nrf2/GPX4 signaling pathway, providing a novel targeted strategy and potential intervention approach for PD treatment. - Source: PubMed
Publication date: 2026/04/16
Yang HanZhang KexianNiu MingguangQian QianTian ShuxiangJin XinyueXiao YangYin Yanyan - Myocardial ischemia/reperfusion (I/R) injury is a major contributor to coronary heart disease. Fasting has emerged as a cardioprotective intervention, yet the underlying mechanisms are unclear. Ferroptosis, an iron-dependent form of regulated cell death, has been implicated in I/R injury, but its interplay with fasting in the myocardial context has yet to be determined. - Source: PubMed
Publication date: 2026/04/16
Han RuijuanXie JiananZhou ShanshanZhang XiaopingSun Kai - Cyclophosphamide (CP) is an alkylating agent that has been widely used in cancer therapy and in the treatment protocols of autoimmune disorders. However, the increased incidence of CP-induced testicular dysfunction represents a major limitation of its therapeutic use. The contributing factors to these deleterious effects include interference with the antioxidant defenses, potentiation of the inflammatory events, and abrogation of autophagy in the testicular tissues. Till now, there is no single agent that can completely overcome this health problem. This work tried to explore the possible role of chicoric acid in the alleviation of CP-induced testicular toxicity in a rat model. Fifty adult male Wistar rats were randomly assigned into control group, CP alone group, and 3 CP groups that were treated with three different doses of chicoric acid (25, 50, and 100 mg/kg/day). The harvested seminal fluid, blood, and tissue specimens were processed and evaluated at both the biochemical and pathological levels. Chicoric acid dose-dependently restored the weight and functions of the testis to approximate the normal values, abrogated the changes in the hormonal profile induced by CP, augmented the antioxidant defense mechanisms, and modulated autophagy in the testicular tissues when compared to animals treated with CP alone. These changes were dose-dependently reflected in the histopathological and electron microscopic picture of the testicular tissues. In conclusion, the antioxidant, anti-inflammatory, autophagy-inducing, and antiapoptotic properties of chicoric acid may make it a promising candidate for the mitigation of CP-induced gonadal dysfunction in male Wistar rats. - Source: PubMed
Publication date: 2026/04/17
Alghubayshi AliAlmuntashiri SultanAtia Hanan AbdelmawgoudEmam Marwa NagyKabel Ahmed M - Sirtuin1 (SIRT1) is a histone deacetylase that plays a critical role in insulin sensitivity. Vildagliptin (Vilda) is dipeptidyl peptidase-4 inhibitor approved as oral antidiabetic agent. Docosahexaenoic (DHA) could attenuate hyperglycemia and insulin resistance. The current study was conducted to evaluate the effect of DHA versus Vilda on insulin resistance and hyperglycemia in type 2 diabetes (T2D) rat model via SIRT1/Akt/PI3K. Eighty male Wistar rats were divided into five groups: normal control, diabetes control (the diabetic rats fed high carbohydrate-high fat diet for four weeks, followed by a single intraperitoneal injection of 35 mg/kg streptozotocin, Vilda + diabetic (diabetic rats received 6 mg/kg vildagliptin), DHA + diabetic (diabetic rats received 300 mg/kg DHA), and DHA only group (normal non-diabetic rats received 300 mg/kg DHA). All treatments were given orally for 4 weeks. Each of Vilda and DHA significantly (p < 0.001) decreased blood glucose (131.40. ± 6.10 mg/L and 137.10 ± 7.37, respectively vs. 449.9 ±46.28 1.84 mg/L), increased insulin levels (7.77 ±0.26 µIU/mL and 7.56 ± 0.42, respectively vs. 3.86 ± 0.37 ), decreased HOMA-IR (2.52 ± 0.09 and 2.55 ± 0.091, respectively vs. 4.26 ± 0.34), decreased pancreatic malondialdehyde (MDA) (3.84 ± 0.29 nmol/mg protein and 3.18 ± 0.21, respectively vs. 6.65 ± 0.71), increased gluthathione (2.18±0.11μmol/mg protein and 2.51±0.09, respectively vs. 1.00±0.29), catalase (104.50±6.74 nmol/mg protein and 122.30±6.20, respectively vs. 70.30±13.98), increased glutathione peroxidase activity (GPx) (0.76±0.19 U/mg protein and 0.99±0.16, respectively vs. 0.47± 0.14) and increased superoxide dismutase activity (SOD) (6.43±1.15 U/mg protein and 8.13±1.16, respectively vs. 3.98±1.4) compared with diabetic group. DHA & Vilda significantly (p < 0.001) improved lipid profile (total cholesterol, triglycerides, LDL-C & HDL-C). DHA was superior to Vilda in increasing levels of glutathione (2.51 ± 0.09 µmol/mg protein vs. 2.18 ± 0.11), catalase activity (122.30 ± 6.20 nmol/mg protein vs. 104.50 ± 6.74 ), SOD activity (8.13±1.16 U/mg vs. 6.43±1.15) and GPx activity (0.99±0.16 U/mg protein vs. 0.76±0.19). Moreover, both Vilda and DHA significantly increase gene expression of SIRT1, Akt, and PI3K and markedly restored normal pancreatic tissue architecture compared with diabetic control group. DHA was comparable to Vilda as insulinotropic and anti-hyperglycemic agent in T2D rats via activation of SIRT1/Akt/PI3K pathway & reducing oxidative stress. - Source: PubMed
Publication date: 2026/04/17
Abo-Saif Mariam AWerida Rehab HMohamed Salma AshrafKhedr Naglaa F