CD95 _ FAS
- Known as:
- CD95 _ Fas Cell Surface Death Receptor
- Catalog number:
- GTX82928
- Product Quantity:
- 200 µg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- CD95 _ FAS
Related genes to: CD95 _ FAS
- Gene:
- FAS NIH gene
- Name:
- Fas cell surface death receptor
- Previous symbol:
- FAS1, APT1, TNFRSF6
- Synonyms:
- CD95, APO-1
- Chromosome:
- 10q23.31
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-25
- Date modifiied:
- 2019-04-23
Related products to: CD95 _ FAS
Related articles to: CD95 _ FAS
- Soluble Fas (sFas) plays multiple roles in tumorigenesis and cancer dissemination by avoiding apoptosis via connection to Fas ligand. We assessed associations of serum sFas levels with the incidence of extrahepatic biliary tract cancer (eBTC) in a prospective case-control study nested in the Japan Collaborative Cohort study. - Source: PubMed
Publication date: 2026/09/04
Adachi YasushiNojima MasanoriLin YingsongMasaki YoshiharuMurota AyakoSasaki YasushiNakase HiroshiWakai KenjiMori MitsuruTamakoshi Akiko - Following the publication of the above article, a concerned reader drew the Editor's attention to the fact that, regarding the EdU assay experiments shown in Fig. 6 on p. 657, discrete areas of the cells appeared to overlap in different data panels, which were intended to show differently performed experiments in two distinct cell lines (the SW1990 and Panc‑1 cell lines), albeit the areas were inverted in the case of the 'LV‑RNAi' data panels. Moreover, within these areas of overlapping cells, certain of the cells were uniquely found to be coloured differently in the associated data panels. In addition, in Fig. 9 on p. 658, the bands shown for the caspase‑3 and caspase‑3 experiments with the SW1990 cell line looked remarkably similar, suggesting that the data in this figure may also have been assembled incorrectly. After having conducted an internal investigation of the data in this paper, the Editor of has decided that this article should be retracted from the publication on the grounds of an overall lack of confidence in the presented data. The authors were asked for an explanation to account for these concerns, but the Editorial Office did not receive a reply. The Editor sincerely apologizes to the readership for any incovenience caused, and we thank the reader for drawing this matter to our attention. [International Journal of Molecular Medicine 32: 653‑660, 2013; DOI: 10.3892/ijmm.2013.1437]. - Source: PubMed
Publication date: 2026/09/04
Zhou JianSong ShiduoHe SongbinWang ZhenxinZhang BingLi DechunZhu Dongming - Bronchial asthma associated with acute or chronic lung injury has emerged as a significant public health concern due to environmental chemical pollution, particularly following the widespread application of sodium hypochlorite (NaClO) disinfectant during the COVID-19 pandemic. Captopril, an antihypertensive agent, has been shown to alleviate symptoms; understanding the mechanism of captopril-mediated protection could facilitate the development of more effective therapeutic strategies. BEAS-2B is a line of immortalized human bronchial epithelial cells, widely used as an model to investigate pulmonary toxicology. This study investigated the mechanism by which captopril protects the lung and BEAS-2B cells against NaClO-induced lung injury. - Source: PubMed
Publication date: 2026/09/04
Li JiaweiShi MinjieHe GaihuaYu WeihuaFan ZhenpengWang ChangyanLiu RuiKong DeqinLi WenjunLiu JiangzhengLi Wenli - KasA is an essential enzyme of Mycobacterium tuberculosis (Mtb). It plays a critical role in synthesizing long-chain mycolic acids, the major components of the bacterial cell wall, by regulating the FAS-I and FAS-II fatty acid synthesis pathways. Inhibiting KasA offers a promising strategy for treating tuberculosis (TB). This study used fragment-based drug design (FBDD) to design novel small molecules targeting KasA. Fragments from known KasA inhibitors were generated with the MacFrag tool and then combined with Fragmenstein to create potential hit compounds. A multi-tiered molecular docking approach was used to evaluate their binding affinity and interactions with KasA. Selected candidates underwent pharmacokinetic analysis and molecular dynamics (MD) simulations. Five promising molecules, namely KasA_FB1, KasA_FB2, KasA_FB3, KasA_FB4 and KasA_FB5, were identified. Their molecular docking binding energies were - 7.80, - 8.30, - 9.00, - 7.80, and - 9.00 kcal/mol, respectively, all superior to the reference co-crystal ligand TLM (- 7.20 kcal/mol). MD simulations showed that their dynamic stability was comparable to or better than TLM. MM-GBSA and free energy perturbation (FEP) analyses further confirmed their superior binding affinity for KasA. These compounds represent promising candidates for the development of new anti-TB drugs targeting KasA and warrant experimental validation. - Source: PubMed
Publication date: 2026/09/03
Islam Md AtaulAli Mohammad AjmalChikhale RupeshIslam Md LutfulFarah Mohammad Abul - CAR T cell therapy has revolutionized the treatment of hematological malignancies by effectively eliminating tumor cells. In the field of kidney transplantation, comparable cellular therapies are being explored to facilitate transplantation and prevent graft rejection. Chimeric HLA antibody receptor (CHAR) T cells are a promising therapy for eliminating HLA-specific B cells in sensitized patients and potentially ameliorating antibody-mediated rejection. We previously demonstrated that HLA class I CHAR T cells selectively eliminated HLA class I-specific B cells with high specificity. Since HLA sensitization is most often directed against HLA-DQ of the allograft, we developed HLA-DQ2 and HLA-DQ7 CHAR T cells to target B cells with corresponding HLA specificity. - Source: PubMed
Publication date: 2026/09/03
Arana CaroltGille IlseHagedoorn RenateGarcía-Busquets AinhoaSchenk Hannah C MBetriu SergiRemst Dennis F Gvan der Meer-Prins Ellen M WVaal Yvonne J H deVoogt-Bakker Kim HBuchli Ricode Vries Aiko P JJuan ManelKramer Cynthia S MPalou EduardRoelen Dave LDiekmann FritzHeemskerk Mirjam H MRovira JordiHeidt Sebastiaan