ADA17_HUMAN TACE ELISA tesk kit
- Known as:
- ADA17_HUMAN TACE Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen16978
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- ADA17_HUMAN TACE ELISA tesk kit
Related genes to: ADA17_HUMAN TACE ELISA tesk kit
- Gene:
- ADAM17 NIH gene
- Name:
- ADAM metallopeptidase domain 17
- Previous symbol:
- TACE
- Synonyms:
- cSVP, CD156B
- Chromosome:
- 2p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-10
- Date modifiied:
- 2019-04-23
Related products to: ADA17_HUMAN TACE ELISA tesk kit
Related articles to: ADA17_HUMAN TACE ELISA tesk kit
- Plasmacytoid dendritic cells (PDCs) represent a crucial bridge between innate and adaptive immunity as they can recognise viruses and viral-infected cells, secrete type I interferon and prime naive T-cell responses. Like naive T cells, PDCs express CD62L, an essential molecule involved in the trans-endothelial migration process, and are supposed to travel directly from blood to lymph nodes to prime naive T cells. We developed a therapeutic PDC line model (PDC*line) derived from a patient with blastic PDC neoplasm, and showing high antigen-presentation capacities. PDC*line-based vaccine was tested in clinical trials in melanoma and lung cancer. Efficient specific T lymphocyte priming was observed suggesting the efficient migration of injected PDC*line-based vaccine to lymph nodes. Here, we investigated the mechanisms involved in this migration and its regulation. In humanised mice, our results demonstrated the efficient migration of the PDC-based vaccine from blood to lymph nodes and its capacity to prime naive T cells. The expression of CD62L was evaluated following irradiation, which was mandatory in the vaccine manufacturing step and possibly important for its efficacy. CD62L was rapidly shed after irradiation of PDC*line cells and primary PDCs but not of NK-T cells, demonstrating the cell specificity of the mechanism. Our results show that p38 MAP kinase, known to be activated in response to irradiation and ADAM17 metalloprotease are involved in the rapid CD62L shedding. This new pathway could participate to the regulation PDC transmigration through High Endothelial Venules and homing to secondary lymphoid organs in cellular stress conditions. - Source: PubMed
Publication date: 2026/09/02
Leplus EstelleKacher JamilaHannani DalilVayssiere GuillaumeMolens Jean-PaulLaulanier KarineGeorgess DanJosserand VéroniqueSaas PhilippePlanel SéverineChaperot LaurencePlumas Joel - Autoimmune diseases affect 5-10% of the global population, with a prevalence of 13% in women and 7% in men. Despite advances in immunology, the molecular basis of immune dysregulation remains limited. Nardilysin (NRD convertase, NRDc), a zinc-dependent metalloendopeptidase, has been identified as an enzyme involved in this dysregulation. Recent studies have identified NRDc dysregulation as a shared feature across type 1 diabetes (T1D), rheumatoid Arthritis (RA), and vitiligo, though the specific mechanism implicated differs by the disease involved. Reported roles for NRDc include modulating the release of the immune checkpoint protein VTCN1 (B7-H4), modulation of pro-inflammatory cytokines, and activation of ADAM17-mediated release of TNF-α and its receptors. While NRDc is recognized for its role in immune signaling, gene transcription, cell differentiation, proliferation, homeostasis, thermogenesis, and metabolism, a unified framework connecting NRDc's multifaceted enzymatic activity to autoimmunity is currently lacking. We review current literature to construct such a framework, positioning it as hypothesis-generating by outlining specific, testable predictions to guide future investigation. Based on the literature, we propose that NRDc functions as a crucial molecular indicator and a therapeutic interface, rather than just a bystander enzyme. - Source: PubMed
Publication date: 2026/08/07
Choudhary YashikaMoutughimou Ben AliUpadhye Vijay JagdishJadeja Shahnawaz DVaishnav Jayvadan - Platelet concentrates stored at room temperature have a shelf life of 5 to 7 days. During storage, platelets undergo glycoprotein cleavage by metalloproteases, notably cleavage of glycoprotein Ibα (GPIbα) by a disintegrin and metalloprotease 17 (ADAM17), which leads to decreased posttransfusion reactivity and recovery. To investigate the putative roles of nascent synthesis of ADAM17 in GPIbα shedding and platelet function during room temperature platelet storage. Human platelets maintained in autologous plasma were treated with naked endonuclease-resistant ADAM17 or control short inhibitory RNA (siRNA) and monitored for molecular and cellular effects during storage. Platelet-specific Adam17-deleted mice were generated, and the dynamics of GPIbα cleavage were assessed. Platelets translated nascent ADAM17 during storage, coinciding with progressive GPIbα ectodomain cleavage. siRNA treatment suppressed ADAM17 translation and rescued total but not surface levels of full-length GPIbα in resting platelets during storage. Flow cytometry and confocal microscopy in permeabilized platelets indicated an internal pool of GPIbα protected from agonist-induced cleavage by cell-permeable ADAM17 pharmacological blockade but not by non-cell-permeable blocking antibodies. ADAM17 siRNA did not alter stimulation-mediated decrease in surface GPIbα across 5 days in storage. Deletion of murine platelet Adam17 resulted in increased basal GpIbα in an inverse gene-dose-dependent manner, and protection from stimulation-mediated cleavage. Hemostasis was normal in platelet-specific Adam17-deleted mice. ADAM17 synthesis contributes to GPIbα cleavage in stored platelets, but extant siRNA-resistant ADAM17 is sufficient to cleave GPIbα upon platelet stimulation. An internal pool of GPIbα is exposed upon platelet stimulation but subject to rapid cleavage by ADAM17. - Source: PubMed
Publication date: 2026/07/02
Askari ShayanGhansah HarrietMansi Christopher DStalker Timothy JGoldfinger Lawrence E - Prediabetes associates with increased production of triglyceride-rich lipoproteins (TRLs), cardiovascular disease (CVD), and hepatic steatosis, which is linked to increased plasma levels of soluble TREM2 (sTREM2), the shed domain of TREM2 (triggering receptor expressed on myeloid cells 2). Whether and how TREM2 shedding contributes to elevated TRLs is unknown. By complementary analyses of individuals with prediabetes and hepatic steatosis and preclinical models, we show that plasma sTREM2 levels correlate positively with plasma apolipoprotein C3 (APOC3), an apolipoprotein that slows TRL catabolism and predicts CVD risk. Individuals with prediabetes and hepatic steatosis had higher plasma concentrations of APOC3-rich TRLs 35 to 60 nm in diameter than healthy controls. Mouse models of prediabetes with hepatic steatosis revealed that the increased plasma concentrations of sTREM2, APOC3, and TRLs were due to activation of macrophage ADAM17, a TREM2 sheddase. Preserving macrophage full-length TREM2 protected against the elevated plasma APOC3, sTREM2, dyslipidemia, and atherosclerosis, while TREM2-deficiency increased APOC3, TRLs, and atherosclerosis. Mechanistically, full-length TREM2 mediates macrophage TRL uptake, preventing excessive hepatic APOC3-rich TRL release and atherosclerosis. Our findings identify macrophage TREM2 shedding as an upstream contributor to the elevated TRLs in hepatic steatosis, providing a mechanistic link between hepatic steatosis and CVD risk in prediabetes. - Source: PubMed
Publication date: 2026/08/27
Tang JingjingKanter JennyShao BaohaiShimizu-Albergine MasamiKramer FarahKhang Ah ReumLuo JasonZheng HuaqingTran AlanCervantes JocelynFrey Jeremy MDorfman Mauricio DHsu Cheng-Chiehden Hartigh Laura JVaisar TomasDavies Brandon SjMullick Adam EIoannou GeorgeSmith Gordon IKlein SamuelDavidson Nicholas OBornfeldt Karin E - The role of adamalysins (ADAMs) has been widely described in many processes related to carcinogenesis, angiogenesis, inflammation, metastasis, and metabolic disorders. Despite numerous studies, their role in colorectal cancer (CRC) remains unclear. The aim of this study was to evaluate the expression of selected ADAM genes in colorectal cancer tissue and corresponding surgical margins. In addition, for a subgroup of patients, the expression of selected proteins from the ADAM family was assessed. The final study group consisted of 67 patients who underwent elective surgery for colorectal cancer. The relative expression of the , , , and genes was expressed as relative quantification (RQ) and determined by real-time quantitative PCR (RT-qPCR) in tumor tissue and surgical margins. In addition, for a subgroup of 45 patients, the expression of ADAM10, 12, and 17 proteins was assessed by ELISA. Associations between ADAM expression and clinicopathological parameters were analyzed statistically. gene expression was significantly higher in tumor than in margin tissue (median RQ: 0.995 vs. 0.251; = 0.003), whereas RQ was significantly higher in the margin (median RQ: 0.400 vs. 0.204; = 0.021). No significant differences were observed in the expression of the , , , or genes based on tumor stage, sex, substance use, BMI, or age, except for nominally higher gene expression in patients over 65 years of age ( = 0.033). Among patients under 65 years of age with cardiovascular disease (CVD), RQ in tumor tissue was significantly higher than in those without CVD ( < 0.05). In obese patients with CVD, a markedly increased expression of in tumor tissue was observed, regardless of age (1.469 vs. 0.132; < 0.005). Significant positive correlations were observed between the and RQ, and between the and RQ, in both tumor and marginal tissues (all adjusted < 0.01). No significant correlations were found between gene expression and corresponding protein levels for ADAM10, ADAM12, or ADAM17. , , , and are poor biomarkers for colorectal cancer, but their significance may increase in patients with comorbid metabolic disorders. The lack of correlation between protein expression and gene expression suggests the contribution of post-transcriptional and post-translational regulatory mechanisms, which justifies further research. - Source: PubMed
Publication date: 2026/08/20
Kalita AgnieszkaSikora-Skrabaka MagdalenaGołąbek KarolinaDąbrowska MariaStrzelczyk Joanna KatarzynaWaniczek DariuszWitkoś AndrzejNowakowska-Zajdel Ewa