TACE Antibody
- Known as:
- TACE Antibody
- Catalog number:
- 1131
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- TACE Antibody
Related genes to: TACE Antibody
- 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: TACE Antibody
Related articles to: TACE Antibody
- 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 - NOD-like receptors (NLRs) are cytosolic pattern-recognition receptors that detect pathogen-associated and damage-associated molecular patterns and mediate innate immune signaling in vertebrates. However, the genomic repertoire, evolutionary diversification, and infection-associated expression of NLR genes remain poorly defined in non-model amphibians. In this study, 66 NLR genes were identified from the Chinese spiny frog (Quasipaa spinosa) genome and designated as QsNLR1-QsNLR66. These genes were unevenly distributed across chromosomes and were classified into three phylogenetic groups, with most members exhibiting conserved motif architectures. Gene duplication analysis indicated that dispersed duplication was the main contributor to QsNLR expansion. Synteny analysis detected five conserved orthologous gene pairs between Q. spinosa and Pelophylax nigromaculatus, suggesting partial conservation of NLR genomic organization between the two amphibians. K/K analysis showed that several duplicated gene pairs, including NLRC3-like/QsNLR36 and NLRC3-like/QsNLR50, exhibited K/K ratios greater than one, suggesting potential sequence divergence after duplication. Spleen RNA sequencing (RNA-seq) after Aeromonas hydrophila challenge revealed enrichment of immune-related Gene Ontology (GO) terms and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways. Weighted gene co-expression network analysis linked several QsNLRs to infection-associated modules, among which QsNLR57 was co-expressed with CYBB, ADAM17, SPI1, and HK2. RT-qPCR using time-matched phosphate-buffered saline (PBS) controls showed distinct temporal patterns, with stronger induction of QsNLR29, QsNLR57, and QsNLR66 and weaker or delayed responses of QsNLR50 and QsNLR56. These results characterize the NLR repertoire of Q. spinosa and identify infection-associated QsNLR candidates for future studies of antibacterial immunity in amphibians. - Source: PubMed
Publication date: 2026/08/26
Wang Zhi-GangXiao BoMo Xi-ChengZhang Ning