Ovine Islet amyloid polypeptide,IAPP ELISA Kit
- Known as:
- Ovine Islet amyloid multipeptide,IAPP Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- E0009OV
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- Sunlog
- Gene target:
- Ovine Islet amyloid polypeptide IAPP ELISA Kit
Related genes to: Ovine Islet amyloid polypeptide,IAPP ELISA Kit
- Gene:
- IAPP NIH gene
- Name:
- islet amyloid polypeptide
- Previous symbol:
- -
- Synonyms:
- AMYLIN, DAP, IAP
- Chromosome:
- 12p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-24
- Date modifiied:
- 2014-11-19
Related products to: Ovine Islet amyloid polypeptide,IAPP ELISA Kit
Related articles to: Ovine Islet amyloid polypeptide,IAPP ELISA Kit
- The role of neuroinflammation in the pathophysiology of migraine is becoming increasingly important. The aim of this study was to evaluate serum netrin-1 and amylin levels in patients with episodic migraine. - Source: PubMed
Publication date: 2026/09/03
Kocoğlu Aysenur InceAltas MustafaAkdag TuranBugrul AhmetUyar Mehmet - Misfolded proteins, including islet amyloid polypeptide (hIAPP), serum amyloid A (SAA), and amyloid-betas (Aβs) such as Aβ1-40 and Aβ1-42 oligomers, collectively referred to in our work as amyloid oligomers, have been implicated in the development of both metabolic and cardiovascular diseases. However, their potential role as early biomarkers of myocardial damage remains insufficiently explored. We conducted a systematic review following PRISMA guidelines and epistemic meta-analysis to investigate the association between misfolded protein oligomers and early myocardial injury. All English- and Spanish-language articles with titles, abstracts, or keywords relevant to the research topic and indexed in at least one of the following databases-PubMed, BIREME, or Web of Science-were included. A comprehensive search across major databases identified 30 eligible studies. Thirty studies met inclusion criteria, in humans and animals, and in vitro. Amyloid oligomers were consistently elevated in patients with acute myocardial infarction, type 2 diabetes, or coronary artery disease compared with controls. In specific individual cohorts, a higher SAA concentration correlated with major adverse cardiovascular events, where it acted as an independent predictor of mortality in reperfused AMI (RR 5.8; 95% CI: 1.3-27.7) and cardiac rupture (OR 8.8; 95% CI: 1.7-25.6). Our findings support the hypothesis that protein misfolding contributes to early myocardial injury and highlight its potential as a novel source of cardiometabolic biomarkers. - Source: PubMed
Publication date: 2026/09/07
Chable-Guerrero Florencio AlejandroRomero-Zertuche DianaRevilla-Monsalve CristinaCastrejón-Delgado LizettAltamirano-Bustamante Nelly FAltamirano-Bustamante Myriam Marlenne - Achieving very-high (VHF) and ultra-high frequency (UHF) operation in organic field-effect transistors (OFETs) would expand their field of application to wireless communication. Such vision remains a major challenge, with OFETs mostly limited to High-Frequency bandwidth (3 - 30 MHz) due to intrinsic limitations, such as contact resistance and charge mobility, and fabrication-related parasitism, especially when adopting solution-based approaches. Here, we report on p-type OFETs exhibiting a frequency of transition (f) up to 135 MHz at V = V = -22 V, improving the voltage normalized f (f/V) for VHF organic transistors with f > 100 MHz to 0.28 MHz V. The devices were realized through a combination of direct-writing and solution-processing techniques employing an air-stable high-mobility semiconductor blend based on 2,7-dioctyl[1] benzothieno[3,2-b][1]benzothiophene (C-BTBT) and poly(indaceno-dithiophene-co-benzothiadiazole) (CIDT-BT). Femtosecond-laser sintering enabled submicron gate overlaps (∼ 0.4 µm), minimizing width-normalized parasitic gate capacitances (C/W ≈ 2.5 pF cm). DC and AC device characteristics can be approximated using compact models, and theoretical simulations indicate that these OFETs could be potentially used to fabricate rectifiers with a -3 dB cut-off frequency of 200 MHz. These results represent a significant step toward high-speed organic electronics, establishing a pathway for wireless systems fabricated through scalable solution-based processes. - Source: PubMed
Publication date: 2026/09/13
Losi Tommasovan Oosterhout KyleCambiaggio MartinoHeeney MartinHe QiaoKleemann HansLuzio AlessandroCantatore EugenioCaironi Mario - In humans, hypersecretion of amyloidogenic amylin (islet amyloid polypeptide, IAPP) in the setting of insulin resistance and type 2 diabetes (T2D) promotes systemic oligomerization and tissue deposition, with deposits identified in failing human hearts and the cerebrovasculature of patients with Alzheimer's Disease. In the renal vasculature, amylin aggregation disrupts microvascular integrity, activating hypoxia signaling pathways and contributing to maladaptive erythropoietic responses, including excess erythrocytosis. We hypothesized that amyloid-forming amylin would activate hypoxia-inducible factor (HIF) signaling, leading to metabolic alterations in liver and heart during T2D pathogenesis. To investigate this, we used the HIP rat, which expresses human amylin specifically in pancreatic β-cells, comparing tissues from 14 to 16-month-old rats with those from age-matched wild-type, hyperglycemic UCD and amylin-knockout (AKO) rats. We found greater accumulation of HIF-1α and HIF-2α in HIP rat livers compared with those in other groups, alongside increased expression of HIF-1 target genes. Mitochondrial ETS capacity was elevated in HIP rat livers, in conjunction with the formation of mitochondrial supercomplexes. Amylin aggregates formed in the hearts of HIP rats, alongside HIF-1α and HIF-2α accumulation. This was associated with suppression of ETS capacity, and increased p-AMPK/AMPK, indicating possible cardiac energetic impairment. Pancreatic secretion of amyloidogenic amylin is thus associated with HIF activation in key metabolic organs beyond the renal vasculature, and occurs alongside mitochondrial alterations in liver and heart that are consistent with sustained hypoxic stress. Our results, alongside previous work, suggest that amylin dysregulation is an overlooked, human-relevant aspect of diabetes pathogenesis, and as such, a potential therapeutic target. - Source: PubMed
Publication date: 2026/09/04
Knapton Alice EVerma NirmalKotiya DeepakSowton Alice PThackray Benjamin DHolzner Lorenz M WDarwin Paula MDespa SandaDespa FlorinMurray Andrew J - Amylin is a pancreatic neuroendocrine peptide that links peripheral metabolic regulation with central homeostatic and neurodegenerative pathways. However, its relevance to the inflammatory and demyelinating processes underlying multiple sclerosis (MS) remains unclear. To date, the role of amylin in MS has not been investigated. This study investigated serum amylin levels in patients with MS and their association with disease status. This cross-sectional case-control study included 62 patients meeting the 2017 McDonald criteria for MS and 63 control participants without MS or associated risk factors. Serum amylin levels were measured using enzyme-linked immunosorbent assay (ELISA). Between-group and phenotype-specific differences were examined. Multivariable logistic regression and receiver operating characteristic (ROC) curve analyses were performed to assess the association between serum amylin and MS status, and the discriminatory performance of serum amylin, respectively. Serum amylin levels were determined in both groups and reported as mean values. Mean serum amylin levels were significantly lower in patients with MS than in controls (234.01 ± 94.84 vs 284.04 ± 110.02 ng/L; P = .003). The groups were comparable across the principal anthropometric, metabolic, and biochemical variables assessed. No significant differences were observed among the relapsing-remitting, secondary progressive, and primary progressive MS (PPMS) phenotypes; however, pairwise analysis demonstrated a significant difference between the relapsing-remitting MS (RRMS) subgroup and controls (P = .017). In multivariable analysis, higher serum amylin levels remained independently associated with lower odds of MS after adjustment for aspartate aminotransferase (AST) activity (P = .02). Despite the significant between-group difference, serum amylin demonstrated only modest discriminatory performance (P = .003). Lower circulating amylin levels were associated with MS status, although their modest discriminatory performance does not support the use of serum amylin as a standalone diagnostic marker, based on the present data. The phenotype-specific difference observed in RRMS warrants further investigation in larger, longitudinal, and clinically characterized cohorts. These findings may deepen insights into MS development and support future biomarker research. - Source: PubMed
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