rHuman TFPI-2 Domain 1
- Known as:
- rHuman TFPI-2 Domain 1
- Catalog number:
- rf007-1
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Agrenvec
- Gene target:
- rHuman TFPI-2 Domain 1
Related genes to: rHuman TFPI-2 Domain 1
- Gene:
- TFPI2 NIH gene
- Name:
- tissue factor pathway inhibitor 2
- Previous symbol:
- -
- Synonyms:
- PP5, TFPI-2, REF1
- Chromosome:
- 7q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-07-14
- Date modifiied:
- 2016-10-05
Related products to: rHuman TFPI-2 Domain 1
*Please allow 3-5 days for delivery time.* In mammals, TIR domain adapters, including Myd88, TIRAP, TICAM-1 (also called TRIF), and TRAM, act in Toll-like receptor (TLR) signaling pathway. The last me*Please allow 3-5 days for delivery time.* RAIDD (RIP-associated ICH-1 homologous protein with a death domain) is an adaptor molecule that mediates the action of cysteine proteases involved in apoptos09C01,Efha1,EF-hand domain-containing family member A1,Rat,Rattus norvegicus,Smhs2100 kDa coactivator,Bos taurus,Bovine,p100 co-activator,SND1,Staphylococcal nuclease domain-containing protein 1100 kDa coactivator,EBNA2 coactivator p100,Homo sapiens,Human,p100 co-activator,SND1,Staphylococcal nuclease domain-containing protein 1,TDRD11,Tudor domain-containing protein 11100 kDa coactivator,Mouse,Mus musculus,p100 co-activator,Snd1,Staphylococcal nuclease domain-containing protein 1100 kDa coactivator,p100 co-activator,p105 coactivator,Rat,Rattus norvegicus,SND p102,Snd1,Staphylococcal nuclease domain-containing protein 1100 kDa protein,Dd5,E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,Edd,Edd1,Hyd,Hyperplastic discs protein homolog,Rat,Rattus norvegicus,Ubr5101F6,CYB561D2,Cytochrome b561 domain-containing protein 2,Homo sapiens,Human,LUCA12.2,Putative tumor suppressor protein 101F6101f6,Cyb561d2,Cytochrome b561 domain-containing protein 2,Mouse,Mus musculus,Putative tumor suppressor protein 101F6110 kDa protein,FYVE finger-containing Rab5 effector protein rabenosyn-5,Homo sapiens,Human,Rabenosyn-5,ZFYVE20,Zinc finger FYVE domain-containing protein 20116 kDa U5 small nuclear ribonucleoprotein component,Bos taurus,Bovine,EFTUD2,Elongation factor Tu GTP-binding domain protein 2,SNRP116,U5 snRNP-specific protein, 116 kDa,U5-116 kDa116 kDa U5 small nuclear ribonucleoprotein component,Chicken,EFTUD2,Elongation factor Tu GTP-binding domain protein 2,Gallus gallus,RCJMB04_4m11,SNRP116,U5 snRNP-specific protein, 116 kDa,U5-116 kDa116 kDa U5 small nuclear ribonucleoprotein component,EFTUD2,Elongation factor Tu GTP-binding domain-containing protein 2,Homo sapiens,hSNU114,Human,KIAA0031,SNRP116,SNU114 homolog,U5 snRNP-specific pr116 kDa U5 small nuclear ribonucleoprotein component,Eftud2,Elongation factor Tu GTP-binding domain-containing protein 2,Mouse,Mus musculus,Snrp116,U5 snRNP-specific protein, 116 kDa,U5-116 kDa Related articles to: rHuman TFPI-2 Domain 1
- Recurrent pregnancy loss (RPL) is a clinically heterogeneous reproductive disorder, and in many women the underlying mechanism remains unexplained by standard thrombophilia evaluation. Pregnancy is characterized by a tightly regulated hemostatic balance at the maternal-placental interface. Heparanase, tissue factor pathway inhibitor 2 (TFPI-2), and heparan sulfate (HS) are expressed in placental and hemostatic pathways and may contribute to coagulation-related pregnancy complications. We investigated whether the heparanase/TFPI-2/HS axis is altered in women with RPL. Blood samples were obtained from 69 women with RPL and 47 control women with at least two normal deliveries and no history of pregnancy-related vascular complications. Samples were collected at least three months after pregnancy and in the absence of hormonal therapy. Plasma and white blood cell samples were analyzed using an enzyme-linked immunosorbent assay, Western blotting, real-time polymerase chain reaction, co-immunoprecipitation, and Sanger sequencing. Mechanistic experiments using heparanase-derived peptide 16 and TFPI-2-derived peptide 6 were performed in MCF-7 and JAR cells. We found that women with RPL had increased plasma heparanase levels, heparanase procoagulant activity, HS levels, and heparanase mRNA expression compared with controls. TFPI-2 protein and mRNA expression were also elevated. The heparanase rs4693608 AA genotype was more frequent in women with RPL and, together with rs4364254 TT, was associated with increased heparanase expression and procoagulant activity. Although TFPI-2 levels were higher in RPL, co-immunoprecipitation showed reduced heparanase/TFPI-2 complex formation, suggesting impaired inhibitory regulation. HS modulated heparanase binding to TF and TFPI-2 in a concentration-dependent, bell-shaped manner. Heparanase-derived peptide 16 increased TFPI-2 expression, supporting a regulatory feedback loop. In conclusion, RPL is associated with dysregulation of the heparanase/TFPI-2/HS axis, including increased heparanase expression and activity, altered heparanase/TFPI-2 interaction, and heparanase-related genetic variation. These findings suggest a coagulation-related reproductive mechanism that may contribute to pregnancy loss and warrants validation in larger prospective studies. - Source: PubMed
Publication date: 2026/09/15
Yanovich ChenSabbah NadinAsayag KerenCrispel YonatanCohen HaimKeren-Politansky AnatNadir Yona - Endothelial cells and astrocytes are critical structural and functional components of the blood-brain barrier. In many neuroinflammatory diseases, endothelial cells are among the first to respond to inflammatory stimuli and release extracellular vesicles (EVs). However, whether inflammatory stimulation alters EV RNA cargo and subsequently regulates astrocyte function remains unclear. In this study, we performed integrated RNA sequencing and proteomic analyses to investigate the effects of TNFα-stimulated endothelial EVs on astrocytes. RNA profiling revealed significant alterations in EV cargo after TNFα stimulation, including 867 upregulated and 577 downregulated mRNAs, 317 upregulated and 15 downregulated lncRNAs, and 88 upregulated and 62 downregulated miRNAs. The results of functional enrichment analysis suggested that altered EV RNAs may primarily promote inflammatory responses, cell migration, and RNA splicing in astrocytes while reducing their regulatory effects on neuronal projection and calcium homeostasis. Further integrative analysis of EV RNAs and astrocytic proteomics revealed key overlapping targets, including upregulated expression of ICAM1, SOD2, TFPI2, and TNFAIP8, whereas NFKBIA expression was consistently decreased. Network analysis revealed NF-κB as the central regulatory node. Reduced levels of EV-derived NFKBIA mRNA were associated with decreased IκBα protein levels in astrocytes, which promoted NF-κB activation and inflammatory cytokine release. Finally, overexpression of IκBα in astrocytes significantly attenuated TNFα EV-induced IL-1β and IL-6 secretion. Collectively, these findings demonstrate that TNFα-stimulated endothelial EVs coordinately regulate astrocyte function through mRNA, lncRNA, and miRNA cargo and that the IκBα/NF-κB axis may be a key mechanism underlying endothelial EV-mediated inflammatory disruption of the blood-brain barrier. - Source: PubMed
Publication date: 2026/08/01
Wang LeLuo LiZhang ZhaoyangLi XueqinXu YiLuo HanLyu QiangShang Fei-Fei - Diabetic nephropathy (DN) represents the leading cause of end-stage renal disease; however, its molecular mechanisms remain incompletely understood. This study aims to elucidate the specific roles and regulatory mechanisms of Tissue factor pathway inhibitor 2 (TFPI2) and forkhead box O4 (FOXO4) in DN. - Source: PubMed
Publication date: 2026/08/20
Mu LiqinZhao YuLi YangGao WeiWang Jing - Tissue factor pathway inhibitor (TFPI) is a serine protease inhibitor existing in two isoforms, TFPI-1 and TFPI-2. Peptides derived from the TFPI C-terminus exhibit potent antimicrobial activity. In this study, a TFPI-1 homolog from Sebastes schlegelii (SsTFPI-1) was identified, and its sequence characteristics, immune response profile, and the antimicrobial activity of its C-terminal peptide TS20 were systematically characterized. The open reading frame of SsTFPI-1 is 867 bp in length, encoding 288 amino acids that comprise a signal peptide, three Kunitz domains, and a low-complexity region. SsTFPI-1 was ubiquitously expressed across all examined tissues, with the highest expression in blood, and its transcript levels were significantly upregulated in the spleen or head kidney following stimulation with Listonella anguillarum, Edwardsiella piscicida, or poly(I:C). Subcellular localization revealed that SsTFPI-1 predominantly localizes in the cytoplasm of EPC cells, and its C-terminus undergoes endogenous cleavage. Antimicrobial assays demonstrated that TS20 exerts pronounced antibacterial activity against Micrococcus luteus with favorable thermal stability. Mechanistically, TS20 disrupts the bacterial cell membrane, enters the cells, binds to DNA, and progressively degrades it. Furthermore, TS20 significantly inhibits SVCV infection in EPC cells by targeting both viral particles and host cells, thereby reducing viral adhesion and entry, while simultaneously downregulating the expression of type I interferon (IFN-I) related genes. In vivo experiments confirmed that TS20 significantly reduced viral loads of SVCV and RBIV-C1 in common carp and turbot, respectively. Collectively, these findings elucidate the immunological role of SsTFPI-1 in S. schlegelii and underscore the potential of TS20 as a promising antimicrobial agent. - Source: PubMed
Publication date: 2026/08/12
Zhu Zhi-ShuChen Zi-YueWang Guang-HuaJing HaoYang KaiSun NuoDu Yi-LinWang Zi-QiZhang Min - Type 1 diabetes (T1D) is an autoimmune disease characterized by progressive β-cell destruction, yet current risk stratification tools, which rely mainly on genetic susceptibility and autoantibody profiles, remain insufficient for accurately predicting disease progression. We aimed to characterize macrophage-related inflammatory transcriptional activity in T1D and to develop peripheral blood-based biomarkers for diagnosis and risk stratification. - Source: PubMed
Publication date: 2026/06/26
Chen YangZhou YiwenLi ShuangChen YuluLiu JingfeiYang ChunZhao HangSu ZhangyaoBian LinglingChen ShuangShen MinQin YaoChen HengXu XinyuShi YunZhang MeiYang TaoGu Yong