HTRA2 Antibody
- Known as:
- HTRA2 Antibody
- Catalog number:
- csb-pa010902esr2hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- HTRA2 Antibody
Related genes to: HTRA2 Antibody
- Gene:
- HTRA2 NIH gene
- Name:
- HtrA serine peptidase 2
- Previous symbol:
- PRSS25
- Synonyms:
- OMI, PARK13
- Chromosome:
- 2p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-26
- Date modifiied:
- 2014-11-18
Related products to: HTRA2 Antibody
Related articles to: HTRA2 Antibody
- Epilepsy affects more than 50 million individuals globally and has a substantial genetic component that remains to be completely understood. Traditional studies have focused on severe, early onset cases enrolled through clinical or research settings. Recent biobank-based approaches, leveraging large-scale population datasets, offer opportunities to explore genetic associations in broader epilepsy phenotypes, including milder, later onset forms. We analyzed data from more than 750 000 individuals across the UK Biobank, All of Us, and Massachusetts General Brigham Biobank, including 20 026 individuals with epilepsy. Rare coding variant burden testing revealed a significant association with LGI1, a known epilepsy gene. Among the other top 10 associated genes, seven had prior evidence linking them to epilepsy (GABRG2, ATP1A3), neurological disorders with comorbid seizures (HTRA2, KRIT1, STAG1), possible involvement in seizure phenotypes (ADAM23), or roles in neuronal function (PDCD4). Thus, we provide the first statistical evidence for ADAM23 as a candidate gene for epilepsy, based on the suggestive association signal combined with prior biological evidence from both animal (canine and murine) and one recent human epilepsy case study, potentially contributing to human epilepsy through its direct interaction with LGI1. Phenome-wide analyses highlighted the pleiotropic effects of epilepsy genes, with LGI1 and ADAM23 predominantly associated with epilepsy, whereas other genes such as KRIT1, TSC1, and TSC2 exhibited broader systemic involvement. Our study shows the potential of population-scale genomic data and suggests that integrating these datasets with deep phenotyping will uncover more novel insights into epilepsy genetics in the future. - Source: PubMed
Publication date: 2026/05/30
Lal Jessica CastrillonLeu CostinBoßelmann Christian MIvaniuk AlinaPérez-Palma EduardoLal Dennis - Alternative splicing quantification is critical for understanding disease mechanisms and developing precision medicine approaches. Conventional gel-based methods suffer from poor resolution and limited quantitative precision, especially for similar-sized exons. Here, we present multiplex alternative splicing quantification (MASQ), a dual TaqMan probe qPCR platform enabling precise quantification of alternative splicing events. MASQ employs FAM-labeled probes targeting the alternative exon and HEX-labeled probes for constitutive exon normalization, providing internal controls and eliminating variability. Using exon 27 as a model system, where inclusion promotes immune checkpoint resistance through enhanced PBAF complex recruitment to the promoter, we demonstrate superior analytical performance. MASQ exhibits exceptional linearity ( > 0.98), high precision (intra-assay CV < 9%), and femtogram-level sensitivity (LOD 195 fg). CRISPR-engineered cellular validation confirmed probe specificity, while analysis of uterine corpus endometrial carcinoma specimens revealed significantly elevated exon27 inclusion in cancer tissues (61.2% ± 14.5%) compared to normal endometrium (12.7% ± 4.0%, < 0.01). Platform generalizability was demonstrated through adaptation to exon 7 quantification and monitoring splice-switching oligonucleotide effects (44.6% reduction at 24 h, < 0.0001). MASQ represents a broadly applicable platform for alternative splicing analysis, enabling applications including biomarker discovery, diagnostic development, and monitoring. - Source: PubMed
Publication date: 2026/04/01
Jeong HyejeongCho NamjoonPark Jong-IlYoo Heon JongKim Kee K - Inflammatory bowel disease (IBD) is a debilitating condition driven by the dual pathologies of chronic inflammation and impaired intestinal barrier function. A significant clinical need exists for therapies that can effectively target both issues simultaneously. In this study, we investigated the therapeutic potential and mechanism of 5-hydroxy-N,N,N-trimethyltryptamine (5-OH-TMT), a quaternary ammonium salt derivative of bufotenine. We demonstrate that oral administration of 5-OH-TMT significantly ameliorates disease in two distinct murine models of experimental colitis (dextran sulfate sodium-induced and 2,4,6-trinitrobenzene sulfonic acid-induced colitis). The 5-OH-TMT treatment markedly improved clinical symptoms, potently suppressed pro-inflammatory cytokine production, and promoted a vital restoration of intestinal barrier integrity. Further exploration of the molecular basis of action of 5-OH-TMT using an unbiased proteomic screen revealed that 5-OH-TMT directly binds to and inhibits the mitochondrial serine protease high-temperature requirement A2 (HTRA2) protein. Additional mechanistic studies demonstrated that this inhibition of HTRA2 activates the Dectin-1/CARD9 signaling pathway, a key axis in mucosal defense. Subsequent work confirmed that siRNA-mediated silencing of HTRA2 could phenocopy the drug's effects, including the suppression of pro-inflammatory NF-κB phosphorylation. In conclusion, our findings establish that 5-OH-TMT mitigates colitis through a newly identified mechanism involving direct HTRA2 inhibition. This inhibition unleashes a protective Dectin-1-dependent program that both suppresses inflammation and restores barrier function. This work identifies the HTRA2-Dectin-1 axis as a promising new therapeutic target for IBD. 5-OH-TMT mitigates colitis through HTRA2 binding-mediated activation of the Dectin-1 signaling pathway. This figure is created with biorender.com. - Source: PubMed
Publication date: 2026/04/02
Xiao Chun-XiuWu Wen-YuanLi Shi-CongDong Mei-LingBian Yu-HangYu MengLv XiangChen Wei-GuoHong MinZhou JingSun YangMa Hong-YueZhu Yu-Yu - Halophilic proteases are valuable in industrial applications due to their resistance to harsh conditions. HtrA2 serine protease is widely distributed and conserved among eukaryotes and prokaryotes. However, HtrA2 proteases from archaea have been poorly characterized. In this study, from haloarcheon sp. TG1 was cloned and corresponding nucleotide and amino acid sequences were analyzed. Recombinant HtrA2 was produced in , and biochemical properties of purified HtrA2 were characterized. HtrA2 was immobilized for the first time using polyhydroxybutyrate (PHB) nanoparticles. Additionally, potential of HtrA2 as a detergent additive was evaluated by its bloodstain removal activity. Recombinant HtrA2 showed its optimum activity at 50 °C, pH 7.0, and 3.0 M NaCl. HtrA2 activity was highly retained over wide temperature (40 to 60 °C) and pH ranges (pH 5.0 to 11.0). Moreover, various organic solvents, inhibitors and metal ions were well tolerated by the enzyme. Acetone and Fe significantly increased HtrA2 activity, while it was not inhibited by phenylmethylsulfonyl fluoride and sodium dodecyl sulfate. Also, immobilization of HtrA2 onto PHB nanoparticles improved its reusability. Furthermore, HtrA2 successfully removed the bloodstain from cotton fabric. This comprehensive characterization of HtrA2 demonstrates that recombinant HtrA2 obtained from sp. TG1 is promising for industrial applications. - Source: PubMed
Publication date: 2026/03/13
Kurt-Kızıldoğan AslıhanKonuksever ÖmerYavuz ÖzlemOtur ÇiğdemAbanoz-Seçgin BüşraOkay Sezer - Essential tremor (ET) is the most common adult-onset movement disorder, yet its genetic basis remains incompletely understood. Although familial aggregation is well recognized, ET shows marked genetic heterogeneity, with many rare and family-specific variants reported. - Source: PubMed
Publication date: 2026/02/25
Aghayev AgharzaErdoğdu MeldaAydemir DuyguBagirova GulendamAslanger Ayca DilrubaCankay Tugba UyarAkcakaya Nihan HandeUyguner Zehra Oya