polyclonal PEN2 | gamma-secretase subunit PEN-2
- Known as:
- pab PEN2 | g-secretase active sequence peptide PEN-2
- Catalog number:
- as06154
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Agrisera
- Gene target:
- polyclonal PEN2 | gamma-secretase subunit PEN-2
Related genes to: polyclonal PEN2 | gamma-secretase subunit PEN-2
- Gene:
- PSENEN NIH gene
- Name:
- presenilin enhancer, gamma-secretase subunit
- Previous symbol:
- -
- Synonyms:
- PEN2
- Chromosome:
- 19q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-08
- Date modifiied:
- 2019-04-23
Related products to: polyclonal PEN2 | gamma-secretase subunit PEN-2
Related articles to: polyclonal PEN2 | gamma-secretase subunit PEN-2
- DNA methylation is an epigenetic modification that regulates gene expression in response to environmental exposures. We measured differential DNA methylation levels in blood before after general anesthesia and surgery in participants with and without postoperative delirium (POD) and postoperative neurocognitive disorder (PNCD). - Source: PubMed
Publication date: 2026/06/15
Hogan Kirk JBerger MilesKolstad Sydney PMadrid AndyHsia BethanyWright Mary CDevinney MichaelSmith Melody RAlisch Reid S - Mutations in KRT5, POFUT1, POGLUT1, and PSENEN define four genetic subtypes of Dowling-Degos disease (DDD), with varied clinical and histologic expression including those previously reported as Galli-Galli disease. We report a case of DDD3 associated with a novel early nonsense variant in POGLUT1 (c.12G>A; p.Trp4*), representing, to the best of our knowledge, the first documented case in Spain. A 55-year-old man presented with recurrent pruritic erythematous scaly papules on the trunk and hyperkeratotic brown papules on the cervical and thoracic regions. Direct microscopic examination of scales from erythematous lesions revealed yeast cells and short hyphae compatible with Malassezia sp. Initial histopathologic evaluation of a pigmented papule was interpreted as simple lentigo. Subsequent biopsy demonstrated elongated rete ridges and focal suprabasal acantholysis without dyskeratosis, raising suspicion for DDD. Whole-exome sequencing identified a heterozygous nonsense variant in POGLUT1, confirming the diagnosis of DDD3. Previous studies have shown that diffuse cytokeratin 5 (CK5) expression throughout all epidermal layers may support the diagnosis of DDD3. This case highlights diagnostic pitfalls related to subtle and focal acantholysis, emphasizes the importance of clinicopathologic correlation and serial sectioning. - Source: PubMed
Publication date: 2026/05/27
González Fernández JoséGarcía García MarLarrosa Martínez DiegoAra Martín Marianode la Fuente Meira SoniaPrieto Torres Lucía - The γ-secretase complex is a membrane-embedded protease essential for intramembrane cleavage of substrates such as Notch receptors and the amyloid precursor protein (APP), processes central to cancer progression and Alzheimer's disease (AD) pathology. However, catalytic inhibition of γ-secretase disrupts multiple signaling pathways, resulting in dose-limiting toxicities. In this study, we report a structure-guided approach to generate peptides with binding and stability profiles that disrupt the assembly of γ-secretase by targeting the interactions of Presenilin-1 and Nicastrin with APH1. First, molecular docking was performed for 36 248 peptides of varying lengths to assess their affinity scores to the PS1 and NCT interaction regions of APH1. Peptides filtered based on their affinity scores and physicochemical properties were then subjected to global molecular docking. 50-nanosecond molecular dynamics simulations and MM/PBSA analyses were performed on the top 10 potential candidates, identifying those with high dynamic interaction potential. Thus, seven γ-secretase inhibitor candidates with favorable affinity scores capable of providing stable interactions and thereby having the potential to disrupt the APH1:PS1 assembly were identified. This approach, which overcomes the challenges of targeting the transmembrane catalytic domain, is based on the inhibition of subunit assembly and presents promising candidates for future experimental studies. - Source: PubMed
Publication date: 2026/04/02
Yuka Selcen ArıTelli KübraYılmaz Alper - The identification of reliable biomarkers for prostate cancer remains a pressing need in clinical oncology. Inflammatory and regulatory molecules such as NF-κB p65, apolipoprotein E (ApoE), angiopoietin-1 (Ang-1), forkhead box protein A2 (FOXA2), presenilin enhancer-2 (PEN-2) and β-amyloid precursor protein (β-APP) have been implicated in tumour biology. However, their roles in prostate cancer progression and invasion require further elucidation. - Source: PubMed
Albaz Ali CanKosova FundaTemeltaş GökhanÜçer OktayMüezzinoğlu Talha - Lung cancer remains a leading cause of cancer-related mortality worldwide. Chemotherapy, including cisplatin, plays a pivotal role in its treatment; however, the development of cisplatin resistance presents a major clinical challenge. The PSENEN gene, which encodes a regulatory protein, is overexpressed in numerous malignancies. This study explores the role of PSENEN in mediating cisplatin resistance in non-small cell lung cancer (NSCLC). RNA sequencing revealed significant upregulation of PSENEN in cisplatin-resistant A549/DDP cells. Functionally, PSENEN inhibition reversed cisplatin resistance, inhibited cell proliferation and metastasis, and enhanced programmed cell death in A549/DDP cells. Single-cell RNA sequencing indicated that PSENEN was expressed in both cancer and stromal cells. Further functional studies suggested that PSENEN regulates chemoresistance through interactions within the stromal microenvironment. Differentially expressed protein analysis (DIA) of stromal cell supernatants, coupled with functional assays, identified PPIB as a key mediator of PSENEN's effect on lung cancer cell drug resistance via stromal signaling. In vivo, pharmacological inhibition of PSENEN significantly suppressed subcutaneous tumor growth. Additionally, analysis of the immune microenvironment revealed a strong correlation between PSENEN expression and the infiltration of multiple immune cell types. Multiple immunofluorescence and immunohistochemistry validation confirmed that PSENEN is positively correlated with CD56 and PD-1, suggesting its potential application value in immunotherapy. - Source: PubMed
Publication date: 2025/12/16
Cao ZhenyuZhu JiaqiQin ZheChen ZhijianWu TongLin WenxiGao BoGu HaoyiJiang YunChen Jianle