Human Furin ELISA kit (4×96T)
- Known as:
- Human Furin Enzyme-linked immunosorbent assay test reagent (4×96T)
- Catalog number:
- lf-ek50800
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Abfrontier
- Gene target:
- Human Furin ELISA kit (4×96T)
Related genes to: Human Furin ELISA kit (4×96T)
- Gene:
- FURIN NIH gene
- Name:
- furin, paired basic amino acid cleaving enzyme
- Previous symbol:
- PCSK3, FUR, PACE
- Synonyms:
- SPC1
- Chromosome:
- 15q26.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-08
- Date modifiied:
- 2016-02-22
Related products to: Human Furin ELISA kit (4×96T)
Related articles to: Human Furin ELISA kit (4×96T)
- The factor VIII (FVIII) B domain, a large and heavily glycosylated region, is crucial for FVIII secretion, although its structural and functional roles remain incompletely understood. Although the B domain is dispensable for cofactor activity, previous research hints at multiple, yet unverified, functional roles. Here, we used an integrative hybrid approach to generate detailed structural models of glycosylated and furin-cleaved full-length FVIII (Gly/FC-FL-FVIII) that include the B domain, using AlphaFold2 predictions. These models were further refined and validated with biophysical data from atomic force microscopy (AFM) and cryogenic electron microscopy of recombinant and plasma-derived FL-FVIII proteins. Additionally, we modeled a FL-FVIII-von Willebrand factor (VWF) complex with both the B domain and D'-D3 domains to investigate B-domain interactions during intracellular processing. Our results suggest that the B domain functions largely as an independent domain encircling the FVIII core. AFM studies revealed that VWF tails are associated with globular FVIII structures. Structural analysis indicated that B-domain glycosylation enhances stability, supports proper folding, and promotes efficient trafficking through the endoplasmic reticulum-Golgi pathway. We propose that, within the Golgi, the B domain may unfold around FVIII via furin cleavages, facilitating essential interactions with partners such as VWF. Our models also suggest that the B domain shields key FVIII epitopes, potentially reducing immune interference and inhibiting premature activation. This study presents a novel structural model of the FVIII B domain and FL-FVIII, offering critical insights into previously unexplored aspects of B-domain function and its essential role in FVIII biology. - Source: PubMed
Publication date: 2026/07/27
Ramaraje Urs Samhitha UrsPellequer Jean-LucTeulon Jean-MarieMa BoxueUgurlar DenizGasper SimonePepanian AnnaMüller JensImhof DianaSingh SnehaOldenburg JohannesBiswas Arijit - Schizophrenia (SCZ) and systemic lupus erythematosus (SLE) exhibit epidemiological overlap, suggesting shared genetic underpinnings. Using the largest SLE genome-wide association study (GWAS) to date, we identified a significant genetic correlation between SCZ and SLE (rg = 0.25, p = 9.0 × 10-4). Cross-trait analysis nominated multiple candidate shared loci outside the major histocompatibility complex (MHC), most with aligned effects. The strongest candidate shared association was found at the FURIN-FES locus, previously implicated in SCZ and newly associated with SLE. In addition to FURIN-FES, FCGR2A, DOT1L and an intergenic noncoding RNA locus on chromosome 2 showed additional evidence consistent with shared association. Functional annotation showed that this locus modulated the expression of FURIN, which encodes a proprotein convertase involved in diverse biological processes, and FES, which encodes a tyrosine kinase important in innate immune signalling. The shared risk allele was also associated with altered plasma levels of FURIN, FES, and their functional partners (GDF2, BMP10, NTF4, FER). Tissue- and cell-type-specific eQTL analysis revealed distinct regulatory effects: FURIN expression was perturbed in neuronal and immune cells, while FES expression was altered in immune cells. Mendelian randomisation supported a causal role for FES protein in both disorders. These findings highlight that pleiotropy at the FURIN-FES locus for SCZ and SLE is compatible with disease-specific mechanisms. This underscores that shared genetics across traits does not necessarily mean shared biology. - Source: PubMed
Gong ChenDand NickButler Amy WAmar AriellaLiu LuTriantafyllou Pinelopi MariaMorris David LVyse Timothy J - Factor VIII (FVIII) circulates as an inactive procofactor and is converted to its active form (FVIIIa) by proteolytic cleavage at Arg372, Arg740, and Arg1689. Although these cleavage events are well characterized, their individual contributions to FVIII activation and hemostatic function remain incompletely defined. To address this, we engineered a FVIII variant (FVIII-2RKR) in which the B-domain and acidic region 3 region were replaced with a PACE/furin processing site, generating a molecule that requires only cleavage at Arg372 for conversion to FVIIIa. FVIII-2RKR exhibited markedly increased apparent activity in plasma-based assays, shortened thrombin generation lag time, and enhanced factor Xa (FXa) generation compared with B-domain-deleted FVIII, whereas both proteins were functionally equivalent following thrombin activation. FVIII-2RKR was cleaved more rapidly at Arg372 by thrombin and FXa, demonstrating that processing at Arg740 and Arg1689 regulates the rate of Arg372 cleavage rather than directly contributing to cofactor activity. In hemophilia A mice, FVIII-2RKR consistently enhanced early hemostatic function across ferric chloride, laser injury, and tail bleeding models, achieving improved efficacy at lower doses. Despite reduced half-life due to impaired von Willebrand factor (vWF) binding, FVIII-2RKR remained effective in vWF-deficient mice, indicating that vWF is not required for local FVIII function at sites of vascular injury. Together, these findings define distinct roles for FVIII activation cleavage sites and demonstrate that processing at Arg740 and Arg1689 regulates activation through Arg372, linking the rate of FVIII activation to hemostatic efficacy in vivo. - Source: PubMed
Publication date: 2026/10/01
Ivanciu LacramioaraBos Mettine H AParthasarathy SudharsanToso RaffaellaCamire Rodney M - A recombinant vaccinia virus (vA4-HiBiT) was constructed with a short, split luciferase HiBiT tag at the C-terminus of the A4 core protein open reading frame. When HeLa or A549 cells stably expressing LgBiT were infected with vA4-HiBiT, the interaction of the split luciferase fragments reconstituted NanoLuc enzyme activity. Upon addition of a membrane-permeable luciferase substrate, a strong luminescence signal indicated core entry into the cytoplasm within 5 min after infection and was proportional to virus multiplicity within the range of 0.5-80 PFU/cell. This direct entry assay was dependent on a functional virus entry-fusion complex, was inhibited by a neutralizing antibody, and was unaffected by an inhibitor of protein synthesis. Entry was enhanced by brief pH 5 treatment of cell-bound virus relative to pH 7 and prevented by pH 3 treatment. Bafilomycin A1, an inhibitor of endosomal acidification, exhibited greater inhibition of entry in A549-LgBiT cells compared to HeLa-LgBiT cells, as did treatment with ammonium chloride, suggesting variations in entry pathways or cell metabolism. Inhibition of entry by latrunculin A and cytochalasin D indicated a role for actin polymerization in both cell lines. Despite the discovery of a conserved furin cleavage consensus sequence in the A16 subunit of the entry-fusion complex, a furin inhibitor did not reduce virus entry unlike results obtained with a human papillomavirus control. These data support the use of this NanoBiT assay for studies of vaccinia virus entry, with application to basic research, antivirals, and neutralizing antibodies. - Source: PubMed
Publication date: 2026/09/29
Zhang YunliangHolly JaroslavGibbs JamesYewdell Jonathan WMoss Bernard - : Host factors angiotensin-converting enzyme 2 (ACE2), transmembrane protease-serine 2 (TMPRSS2), furin paired basic amino acid cleaving enzyme (FURIN), and neuropilin-1 (NRP1) facilitate severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) entry, but it is unclear whether their upper-airway expression after recovery is associated with the severity of the preceding acute illness. We examined the association between post-acute expression of these genes and previous coronavirus disease 2019 (COVID-19) severity. : This multicenter cross-sectional study included 104 adults with polymerase chain reaction (PCR)-confirmed COVID-19 during the first two pandemic waves in Murcia, Spain. Nasal and/or oropharyngeal swabs were collected in the post-acute phase, at a median of 75 days after symptom onset, and transcript levels were quantified by quantitative real-time PCR. Severity was categorized using the World Health Organization (WHO) Clinical Progression Scale, and associations were evaluated using logistic regression adjusted for age, sex, and race/ethnicity. : In the primary analyses using continuous expression measures, none of the four genes was significantly associated with severity. In exploratory tertile-based analyses, the intermediate ACE2 tertile (odds ratio [OR] = 0.17, 95% confidence interval [CI] 0.05-0.61; = 0.007) and intermediate NRP1 tertile (OR = 0.29, 95% CI 0.10-0.88; = 0.030) were associated with lower odds of severe disease; no significant associations were observed for the high tertiles or for FURIN or TMPRSS2. : Primary adjusted analyses did not reveal statistically significant associations between post-acute nasal expression of ACE2, TMPRSS2, FURIN, or NRP1 and COVID-19 severity. Because expression was measured after clinical recovery, these associations cannot be interpreted as predictors of acute severity and may instead reflect persistent molecular remodeling after more severe disease; reverse causation cannot be excluded. Longitudinal studies with acute-phase and serial post-acute sampling and healthy controls are needed. - Source: PubMed
Publication date: 2026/09/09
Piqueras-Sánchez Ana MaríaLópez-Gil José FranciscoHellín-Meseguer DiegoCabezas-Herrera JuanBlesa-Llaona Ginés FranciscoMeseguer-Cabezas JoséBernal-Morell EnriqueMinguela-Puras AlfredoPiqueras-Pérez Francisco MateoDíaz-Manzano José Antonio