Human Apolipoprotein C4 ELISA , APOC4
- Known as:
- Human Apolipoprotein C4 Enzyme-linked immunosorbent assay test , APOC4
- Catalog number:
- E01A0517
- Product Quantity:
- 96 Tests/kit
- Category:
- -
- Supplier:
- BGene
- Gene target:
- Human Apolipoprotein C4 ELISA APOC4
Related genes to: Human Apolipoprotein C4 ELISA , APOC4
- Gene:
- APOC4 NIH gene
- Name:
- apolipoprotein C4
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-08
- Date modifiied:
- 2016-10-05
Related products to: Human Apolipoprotein C4 ELISA , APOC4
Related articles to: Human Apolipoprotein C4 ELISA , APOC4
- Septic shock represents the most severe form of infection-driven systemic inflammation, whereas acute pancreatitis induces a sterile inflammatory response. Although clinically similar, their molecular profiles may reveal distinct mechanisms underlying infectious and non-infectious inflammation. We performed plasma proteomic profiling using LC-MS/MS in patients with septic shock (n = 13), acute pancreatitis (n = 8), and healthy controls (n = 8). Among 663 quantified proteins, 231 were differentially expressed in septic shock versus controls, 83 in pancreatitis versus controls, and 29 in septic shock versus pancreatitis. Septic shock was characterized by higher plasma concentrations of MARCKS, HSP90AA1, PSAP, CD163, and GANAB, whereas pancreatitis showed higher levels of CPA1, APOC4, APOC3, BPGM, and APOC2. Cluster analysis demonstrated separation between groups, with overlapping proteomic patterns in sepsis and pancreatitis. Gene Ontology and KEGG analyses revealed shared inflammatory signatures, including upregulation of acute-phase responses and downregulation of coagulation pathways. However, septic shock exhibited more extensive proteomic alterations, with distinct activation of PI3K-Akt signaling and suppression of lipid metabolism. In conclusion, septic shock and pancreatitis share common inflammatory pathways, while proteomic differences highlight divergent regulation of coagulation, lipid metabolism, and anti-inflammatory signaling, offering potential biomarkers to distinguish infectious from sterile systemic inflammation. - Source: PubMed
Publication date: 2026/09/06
Wallner JonMazubane Asandavan der Heijden JaapVorontsov EgorSallisalmi MarkoMarks-Hultström MichaelTenhunen JyrkiTenhunen Annelie Barrueta - Post-COVID-19 condition (PCC) with secondary adrenal insufficiency (SAI) involves multiorgan dysfunction, potentially linked to renin-angiotensin-aldosterone system dysregulation. The molecular basis of renin-associated pathology remains unclear. Here, PCC+SAI patients were stratified by upright renin into low- (<38.8 pg/mL) and high-renin (≥38.8 pg/mL) groups. Clinical, endocrine, and proteomic analyses were performed. We found that high-renin patients showed increased BMI, lipids, renin, and aldosterone, but reduced aldosterone-to-renin ratio. Proteomic annalysis identified 20 differentially expressed proteins (DEPs), including 17 upregulated and 3 downregulated proteins in Ren-H patients. Functional annotation revealed that 15 DEPs were immune-related (e.g., APOC4, APOE, C4BPA, CFAH, CFHR3, PF4V, PLF4), while FLNA and COF1 represented cytoskeletal proteins. These DEPs were primarily involved in immune response, complement and coagulation cascades, and MAPK signaling pathways. Correlation analyses indicated that upright renin was positively correlated with complement-related proteins and platelet-derived immune factors, while cytoskeletal proteins (FLNA, COF1) showed positive associations with serum Na+ levels. Additionally, white blood cell and platelet counts were positively correlated with the majority of DEPs. In conclusion, exploratory proteomic analyses suggest that elevated upright renin in PCC+SAI may be associated with immune dysregulation, complement activation, and cytoskeletal remodeling, offering novel insights into the endocrine-immune interactions driving postviral sequelae. - Source: PubMed
Bai GuirongXie XiaominJi WenruiHe YantingZhang LiLi HuanYang YazhiWu YawenPei SiqiLi LingPing Rui - The gene encodes a lipid transport protein central to Alzheimer's disease (AD) pathogenesis. Three common alleles-ε2 (rs7412(C > T)), ε3 (reference), and ε4 (rs429358(T > C))-arise from two coding variants in exon 4 and confer distinct AD risk profiles, with ε4 increasing risk and ε2 being protective. The ε3-linked variant rs769455[T] has also been associated with increased AD risk among individuals of African ancestry who also carry the ε4 allele. Determining how genetic variation influences CpG methylation requires methQTL-type analyses, but conventional bisulfite and array-based approaches offer limited resolution for distinguishing allele-specific effects. Here, we use high-accuracy long-read sequencing to generate haplotype-resolved methylation profiles across the locus in 332 postmortem brain tissue samples from ancestrally diverse cohorts, including 201 samples from individuals of European ancestry and 131 samples from individuals of African and African admixed ancestry. Treating each haplotype as an independent observation, OLS regression identified 18 novel differentially methylated CpG sites associated with ε2, ε4, and rs769455[T] across the locus (, and - genes). These findings reveal distinct allele-specific methylation signatures and demonstrate the utility of long-read sequencing for resolving epigenetic variation relevant to AD risk. - Source: PubMed
Publication date: 2026/06/19
Genner Rylee MMeredith MelissaDaida KensukeMoller AbrahamWeller CoryAyuketah AlexisJerez Pilar AlvarezAkeson StuartMalik LakshBaker BreeanaKouam CedricPaquette KimberlyCatching AdamBromberek SarahHu FangleReed XylenaMarenco StefanoAuluck PavanMandal AjeetPaten BenedictGibbs J RaphaelJain MitenCookson Mark RSingleton Andrew BNalls MikeBlauwendraat CornelisBillingsley Kimberley J - Elevated cholesterol levels are associated with the risk of the most socially significant cardiovascular diseases, such as atherosclerosis, ischemic heart disease, and myocardial infarction. - Source: PubMed
Publication date: 2026/06/02
Mamchur AleksandraBruttan MariaDaniel VeronikaKashtanova DariaZelenova ElenaDzhumaniiazova IrinaIvanov MikhailMatkava LorenaBlinova OlgaMitrofanov SergeyGolubnikova LiliyaKumar NaianaMaralova EkaterinaShingaliev AndreyEzhov MaratMeshkov AlekseyChubykina UlianaPogorelova OlgaTripoten MariiaBalahonova TatyanaViskova AlexandraKomarova MadinaGurtsiev TimurGomyranova NataliaVorobeva YuliaHotuleva AnastasiaKolyaskina MariaYudin VladimirMakarov ValentinKeskinov AntonKuzmina LyudmilaBoytsov SergeyYudin SergeySkvortsova Veronika - Ultracentrifugation (UC) has long been considered the "gold standard" for extracellular vesicle (EV) isolation. However, due to its drawbacks such as high cost of an ultracentrifuge and rotors, time-consuming and labor-intensive protocol, low yield considering initial biofluid volume and low throughput, development of new EV isolation approaches is still ongoing. Here we compare three methods for isolating the most studied EV subtype, small extracellular vesicles (sEVs), from human plasma: ultracentrifugation (UC), express asymmetric depth filtration (ExADFi), and anti-CD9 immunoaffinity capture (AS-CD9) with focus on their Raman and proteomic profiles. For all three methods, purity and quality of the sEV isolation were assessed based on the level of contamination of the sEV fraction with major plasma proteins such as albumin and apolipoproteins (APOA1, APOH, APOA4, APOC2, APOC1, and APOC4). UC showed the highest ratio of protein to nanoparticle concentration. AS-CD9 and ExADFi provided comparable to UC purity and levels of non-vesicular contaminants with AS-CD9 requiring minimal time and labor. ExADFi showed characteristics including purity of the sEV samples, yield, and isolation time that is between the UC and AS-CD9 methods. Raman spectroscopy provided more details about characteristics of the isolated sEVs and confirmed differences observed in the proteomic profiles. The findings demonstrate that the AS-CD9 and ExADFi methods could be appropriate substitutes of the classical UC-based isolation method and be chosen depending on the final requirements and use of the purified sEVs such as further functional and biomarker studies. - Source: PubMed
Chernyshev Vasiliy SStarodubtseva Natalia LRimskaya Elena NBugrova Anna EKononikhin Alexey SSilachev Denis NTokareva Alisa OEvtushenko Ekaterina AYakovlev Alexander AYurin Alexander MKepsha Maria AMezhevitinova Elena ANikolaev Eugene NFrankevich Vladimir ENazarova Niso MPrilepskaya Vera NSukhikh Gennadiy T