Mouse Monoclonal to Rat PAI1 1mg
- Known as:
- Mouse Monoclonal Rat PAI1 1mg
- Catalog number:
- IMA-32K3-1mg
- Product Quantity:
- 1mg
- Category:
- -
- Supplier:
- Innovative
- Gene target:
- Mouse Monoclonal Rat PAI1 1mg
Related genes to: Mouse Monoclonal to Rat PAI1 1mg
- Gene:
- SERPINE1 NIH gene
- Name:
- serpin family E member 1
- Previous symbol:
- PLANH1, PAI1
- Synonyms:
- PAI
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: Mouse Monoclonal to Rat PAI1 1mg
Related articles to: Mouse Monoclonal to Rat PAI1 1mg
- To reconnoitre the mechanism of Abietic acid (AA) in diabetes by and experiments. Using GeneCards, diabetes gene targets were obtained. The protein-protein interaction and network topology analysis were performed using the String platform and Cytoscape 3.7.2. The enrichment analysis was done by Shiny GO. The docking was by Autodeck. Diabetes was induced by injecting STZ (55 mg/kg, i.p once) in Sprague-Dawley rats. The parameters included glucose, lipids, blood pressure, ECG, OGTT, kidney and cardiac markers, liver enzymes, AMPK, Nrf2, PPAR-γ, TLR-4, oxidative markers, LVF tests, and histopathology. AA interacts with 15 important targets (PIK3CD, MAPK1, NF-κB, mTOR, STAT3, GRIN1, ITGB3, ACACA, HSP90AB1, SERPINE1, ADRB1, ULK1, TLR4, CTSD, CDK5). The signalling pathways, like insulin, MAPK1, TLR, AMPK, JAK-STAT, are associated with these proteins. In docking, the highest affinity of AA was observed for ITGB3 (- 8.1), TLR4 (- 7.8), and ACACA (- 7.3). In rats, AA(40 and 80 mg/kg) decrease hyperglycaemia and hyperinsulinemia, improves glucose tolerance, normalize blood pressure, combat dyslipidaemia (decrease triglyceride, total cholesterol, LDL, increase HDL), preserves myocytes and ventricular function (decrease troponin-I, LDH, CK-MB, LVEDP, normal ECG), hepatoprotective (decrease AST, ALT), reno-protective (decrease creatinine, urea, uric acid) and combat oxidative stress (decrease MDA, increase SOD, catalase). Nrf2, AMPK, and PPAR γ levels were increased while TLR-4 levels were decreased after AA treatment. The study is supported by the preserved histopathological architecture of pancreatic, renal, hepatic, and cardiac cells. The present study preliminarily clarifies that AA exhibits therapeutic potential in preclinical models through multitargets and multi-pathways (Nrf/TLR4/PPAR γ), which points out a new direction for further research and clinical application. - Source: PubMed
Publication date: 2026/09/24
Mishra AkashShah Hital - Gangrenous mastitis is a severe form of mastitis in dairy goats that causes extensive tissue damage and has a poor prognosis, thereby substantially affecting the dairy goat industry; however, its molecular pathogenesis remains unclear. In this study, was used to establish a model of gangrenous mastitis in dairy goats. Mammary gland tissues were collected at 72 h post-inoculation for transcriptomic and proteomic sequencing, followed by integrated multi-omics analyses to systematically identify key regulatory pathways and candidate molecules associated with -induced gangrenous mastitis. The results showed that clinical mastitis was characterized mainly by activation of pathways related to the acute inflammatory response, pathogen recognition, neutrophil chemotaxis, and phagocytic defense. In contrast, gangrenous mastitis involved broader molecular reprogramming, with significant enrichment of the TNF, IL-17, and NF-κB signaling pathways, complement and coagulation cascades, platelet activation, and extracellular matrix (ECM) remodeling. Protein-protein interaction (PPI) analysis, gene set enrichment analysis (GSEA), and validation of key molecules indicated that IL6, S100A8, THBS1, SERPINE1, and MMP9 may represent important nodes in disease progression. Collectively, these findings indicate that gangrenous mastitis is a complex infectious tissue-injury process driven by inflammatory amplification, aberrant immune-cell activation, complement-coagulation dysregulation, and tissue structural disruption. The identified molecules and pathways may facilitate the development of biomarker panels for early diagnosis and risk stratification and inform preventive and adjunctive therapeutic strategies targeting excessive inflammation, microcirculatory dysfunction, and ECM damage in dairy goats. - Source: PubMed
Publication date: 2026/09/12
Fu MingzheTan XuewenLiu YingqiuZhang WeiminZhuang ShenAn XiaopengFan Yunpeng - Plasminogen activator inhibitor 1 (PAI-1) is a key regulator of fibrinolysis, and its deficiency causes bleeding symptoms. PAI-1 deficiency is rare, and pathogenic variants are only sporadically reported. - Source: PubMed
Publication date: 2026/08/27
Haisma BaukeNieuwenstein ThomasRijpma Sanna RSimons AnnetBlijlevens Nicole M Avan Heerde Waander LSchols Saskia E M - Coronary artery disease (CAD) may progress to ischemic cardiomyopathy (ICM) and heart failure through maladaptive cardiomyocyte remodeling and myocardial fibrosis. This study aimed to identify key molecular mediators linking inflammatory and fibrotic signaling during this pathological transition. - Source: PubMed
Publication date: 2026/09/11
Chen KexinHe XingyuNing XiangmingWang YaoLi NaHu TengMa ZeyuanYang FengruiZhang YinleiMa JunShi Zheng - Cellular senescence is a complex biological process characterized by irreversible cell-cycle arrest and acquisition of the senescence-associated secretory phenotype (SASP). Beyond biochemical stress, increasing evidence indicates that mechanical cues from the extracellular microenvironment contribute to the regulation of senescence; however, the molecular mechanisms linking mechanotransduction to senescent phenotypes remain incompletely understood. SERPINE1 (plasminogen activator inhibitor-1, PAI-1) has emerged as a key mechanosensitive effector induced downstream of mechanotransduction signaling pathways. In this review, we discuss SERPINE1 as both a hallmark of cellular senescence and a functional mediator linking mechanotransduction to senescence-associated processes. Once induced, SERPINE1 contributes to cell-cycle arrest and extracellular matrix (ECM) remodeling by inhibiting plasmin-dependent proteolysis. The resulting ECM accumulation and matrix stiffening further enhance integrin-dependent mechanotransduction, promoting further SERPINE1 expression and establishing a self-reinforcing mechanobiological feedback loop. SERPINE1 also contributes to senescence-associated inflammatory signaling, which may further support the maintenance of the senescent phenotype. Together, these findings identify SERPINE1 as a mechanistic link between mechanotransduction, ECM remodeling, and cellular senescence. Pharmacological studies using PAI-1 inhibitors further support the biological importance of this pathway and suggest that SERPINE1 may represent a potential therapeutic target for senescence-associated fibrotic diseases. - Source: PubMed
Nisa Intan ChairunChantachotikul PirawanTakahata KeiAnsori Arif Nur MuhammadDeguchi Shinji