SERTAD1 _ SEI1 antibody Host rabbit
- Known as:
- SERTAD1 _ SEI1 (anti-) Host host: rabbit
- Catalog number:
- 'ARP34310_P050
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- SERTAD1 _ SEI1 antibody Host rabbit
Related genes to: SERTAD1 _ SEI1 antibody Host rabbit
- Gene:
- SERTAD1 NIH gene
- Name:
- SERTA domain containing 1
- Previous symbol:
- -
- Synonyms:
- SEI1, TRIP-Br1
- Chromosome:
- 19q13.1-q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-16
- Date modifiied:
- 2014-11-19
Related products to: SERTAD1 _ SEI1 antibody Host rabbit
Related articles to: SERTAD1 _ SEI1 antibody Host rabbit
- Pterygium is a common ocular surface disorder, with its prevalence strongly correlated to ultraviolet (UV) exposure in geographic regions. Epidemiological investigations reveal significant demographic variations, with higher incidences observed in areas with intense UV radiation and within specific populations, notably rural individuals. Despite surgical interventions being the standard treatment, recurrent cases underline the necessity for understanding the underlying biological mechanisms contributing to pterygium pathogenesis. Recent advancements in cellular death mechanisms point to cuproptosis, a copper-dependent programmed cell death pathway, as a potential regulatory factor in ocular diseases, including pterygium. This study aims to systematically investigate the immunological significance of cuproptosis-related genes (CuRGs) in pterygium's pathogenesis using an integrative bioinformatics framework. We performed transcriptomic profiling on pterygium tissues and employed machine learning algorithms to identify pivotal biomarkers for pterygium risk stratification. Comprehensive immune profiling and functional enrichment analyses were conducted to elucidate the interplay between identified CuRGs and the immune microenvironment in pterygium. Our analysis highlighted 19 CuRGs, with eight genes displaying significant dysregulation in pterygium tissues (p < 0.05). We established robust associations between CuRG expression and prominent immune cell infiltrates, notably regulatory T cells and macrophages. Furthermore, three core biomarkers (SERTAD1, JMJD1C, CSRNP1) were identified through machine learning and validated by QPCR, with the support vector machine model demonstrating exceptional predictive performance (AUC = 0.84). Empirical validation corroborated significant downregulation of selected biomarkers in pterygium tissue samples compared to normal conjunctiva. Our findings underscore the vital role of CuRGs in modulating pterygium development through immune and metabolic interactions, establishing their potential as novel therapeutic targets. Nevertheless, our study has limitations, as these findings are hypothesis-generating and require validation in larger patient cohorts. - Source: PubMed
Publication date: 2026/05/16
Yang JiLiang Bo-YuFang Chen-YanLi Jia-JieZhang PengXiang PingZhang Li-WeiLiu Hai - - Source: PubMed
Publication date: 2026/03/07
Hu ChangyanMiao JuanjuanZhao QihongChen Lijian - Aberrant activation of autophagy contributes to neuronal cell death and plays a pivotal role in the pathogenesis of Alzheimer's disease (AD). To study this further, we assessed autophagy-related (ATG) proteins in 5xFAD mice at different ages and found a progressive inappropriate elevation of autophagic proteins in these mice. We identified a transcriptional coregulator, Sertad1 (SERTA domain-containing protein 1), which plays a necessary role in neuron death, as a key regulator of aberrant autophagy in AD. We found a progressive elevation in Sertad1 levels in 5xFAD mice with age compared with WT mice. Sertad1 knockdown in 5xFAD mice brains lowered levels of ATG proteins and lysosomal proteins, suggesting its role in the regulation of the autophagy-lysosomal pathway. We found that Sertad1 knockdown restored Akt activity, which is inhibited in AD, and blocked the activation of its target, FoxO3a, which is translocated to the nucleus in the absence of active Akt and mediates neuron death by apoptosis and autophagy. Furthermore, we showed that lentivirus-mediated RNAi targeting of Sertad1 in 5xFAD mice led to better performance in behavioral experiments compared with 5xFAD mice treated with nontargeting shRNA, accompanied by significant restoration of synaptic integrity. Overall, our results demonstrated that autophagy is robustly induced with disease progression, but ATG proteins accumulate in the brain because of their impaired clearance; Sertad1 knockdown restored synaptic failure and improved cognition in 5xFAD mice by enhancing clearance of ATG proteins and neuronal survival. Hence, Sertad1 could be an excellent target for therapeutic intervention to combat the multifaceted pathologies of AD. - Source: PubMed
Publication date: 2025/10/29
Ambareen NaqiyaGharami KusumikaMondal AnanyaSarkar Uday AdityaBiswas Subhas C - Cell division cycle-associated protein 4 (CDCA4) has the potential to indicate lung adenocarcinoma (LUAD) development, but its regulatory role in mitophagy remains unclear. This study aimed to elucidate the mitophagy regulation and therapeutic implications of CDCA4 in LUAD. CDCA4 expression was significantly elevated in LUAD clinical specimens versus paracancerous tissues and inversely correlated with mitophagy activity. Lentiviral vectors were employed to manipulate established LUAD cells, followed by treatment with chloroquine (CQ; lysosomal inhibitor) and rapamycin (autophagy inducer) in CDCA4-silenced cells. CDCA4 knockdown elevated total and mitochondrial superoxide levels, disrupted mitochondrial membrane potential, activated the PINK1/Parkin pathway, enhanced LC3-II conversion, and degraded mitochondrial membrane proteins, collectively promoting mitophagy. Silencing CDCA4 suppressed malignant phenotypes (proliferation/migration), effects reversed by CQ but exacerbated by rapamycin. Mechanistically, CDCA4 interacted with SERTAD1 and E2F1 and stabilized these proteins. The promotion of mitophagy by CDCA4 silencing was impaired by the overexpression of SERTAD1 and E2F1. LUAD cells silencing CDCA4 were injected into immunodeficient mice for in vivo verification. CDCA4-silenced xenografts exhibited suppressed tumor growth, increased apoptosis, and elevated mitophagy-related markers. This study identifies the CDCA4/SERTAD1/E2F1 complex as a pivotal mitophagy-inhibitory hub in LUAD, proposing this axis as a novel predictive and therapeutic target. - Source: PubMed
Tan JianlongWang JufenZhang WeidongZhang Cuihua - The activity of protein phosphatase 2A containing the B55 regulatory subunit (PP2A:B55) is tightly controlled by various positive and negative modulators. IER family proteins function as adapters by simultaneously binding the B55 subunit and specific substrates, thereby promoting their dephosphorylation by PP2A:B55. Here, we report that the B55-binding domain of IER proteins shares significant amino acid homology with the SERTA domain of the SERTAD family. All SERTAD family members-SERTAD1, SERTAD2, SERTAD3, SERTAD4, and CDCA4-bind to B55-containing PP2A complexes. Among these, SERTAD1 induces dephosphorylation of heat shock factor HSF1 at Ser320, leading to suppression of HSF1 transcriptional activity. This regulatory function of SERTAD1 requires its nuclear localization and interaction with both HSF1 and the B55 subunit. In contrast, the PP2A:B55 adapter IER5 promotes dephosphorylation of HSF1 at Ser303, Ser307, and Ser320, resulting in enhanced HSF1 activity. The differential dephosphorylation patterns mediated by SERTAD1 and IER5 are attributed to structural differences in helix 1 of their respective B55-binding domains. These findings identify SERTAD1 as a novel PP2A:B55 adapter and highlight the role of the B55-binding domain in governing site-specific substrate dephosphorylation. - Source: PubMed
Publication date: 2025/09/24
Sugiyama HarukaNakada TaiseiYano KoyoSakurai Hiroshi