Ask about this productRelated genes to: CD117 antibody
- Gene:
- KIT NIH gene
- Name:
- KIT proto-oncogene, receptor tyrosine kinase
- Previous symbol:
- PBT
- Synonyms:
- CD117, SCFR, C-Kit
- Chromosome:
- 4q12
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: CD117 antibody
Related articles to: CD117 antibody
- Lung cancer poses severe therapeutic challenges due to its complex metabolic reprogramming and epigenetic abnormalities. This study aimed to explore the inhibitory effect of Carnosol (CA) on lung cancer and elucidate its underlying molecular mechanisms. Using multiple experimental approaches, including the Cell Counting Kit-8 assay, colony formation assay, flow cytometry, RNA sequencing, metabolite extraction followed by gas chromatography-mass spectrometry (GC-MS), and Western blot analysis, we systematically evaluated the in vitro effects of CA on lung cells. The anti-lung cancer efficacy of CA in vivo was validated using a tumor xenograft model. The results demonstrated that CA significantly inhibited the viability of lung cancer cells in a dose-dependent manner and induced G1 cell cycle arrest by downregulating the expression of Cyclin E1 and CDK2. Furthermore, CA altered cellular metabolism by modulating the glycolysis pathway, thereby suppressing histone H3 lactylation levels. Immunoprecipitation assays further confirmed that CA selectively reduced lactylation at the histone H3K18 site by influencing the expression of KAT2B, consequently regulating lung cancer cell proliferation. In conclusion, CA exhibits promising antitumor effects by targeting the KAT2B-H3K18la axis, suggesting its potential as a novel therapeutic agent for lung cancer treatment. - Source: PubMed
Publication date: 2026/06/12
Liu MinfuHou ShuwanDu QianqianYu HuimingWan LeyaoZha ShuaiChen LinLi AnzhengWu JiaqinGuo YaoFeng FanXu KangWang Chunli - This study evaluated an enzyme-linked immunosorbent assay (ELISA) for the detection of Coll2-1, a peptide fragment of type II collagen released during cartilage degradation in horses using a kit originally developed for dogs. - Source: PubMed
Publication date: 2026/06/12
Ramos SofiaLamy ElsaNunes TelmoRosa TeresaBettencourt ElisaMonteiro Susana - Extraction and purification of nucleic acids are essential for the detection of foodborne pathogens, yet conventional methods are often limited by operational complexity and reliance on specialized instrumentation, restricting their use in low-resource settings. Herein, we report a simple and efficient nucleic acid extraction platform based on a chitosan-derived sponge-like cryogel (CSC), enabling dynamic adsorption-elution-driven separation under mild conditions. The CSC exhibits high nucleic acid binding capacity (88 μg for DNA and 305 μg for RNA per 10 mg material) and rapid adsorption kinetics following a pseudo-second-order model. Isotherm analyses indicate that RNA and DNA binding follow the Langmuir and Freundlich models, respectively, suggesting a combined mechanism of electrostatic interaction and physical entanglement. Notably, the compressible and shape-recoverable structure enables dynamic extraction through simple aspiration-compression operations, eliminating the need for external equipment. For practical application, the CSC was integrated into a Pasteur pipette to construct a portable extraction device. This system allows rapid nucleic acid purification from Vibrio parahaemolyticus and Salmonella in bacterial cultures and milk samples, with direct compatibility for quantitative polymerase chain reaction (qPCR) and recombinase polymerase amplification (RPA)-clustered regularly interspaced short palindromic repeats (CRISPR)/Cas12a assay. The method achieved sensitive detection down to 10 CFU ·mL, outperforming a commercial kit. Importantly, the entire extraction process avoids chaotropic salts, organic solvents, and complex instrumentation, offering a simplified and environmentally friendly alternative. This work provides a practical and scalable strategy for nucleic acid purification with potential applications in point-of-care testing for food safety. - Source: PubMed
Publication date: 2026/06/06
Li WeixuanCao LiminSui JianxinLin HongWang KaiqingWang Xiudan - Stem cell-based dental pulp regeneration is a promising treatment for pulp necrosis, wherein vascularization is critical. Dental pulp cells (DPCs) are mechanosensitive; however, the mechanism by which compressive stress regulates their angiogenic activity remains unclear. This study investigated the underlying mechanotransductive mechanisms and optimal loading parameters. - Source: PubMed
Publication date: 2026/06/04
Zhang NingningHuang QianShen ShuhuiTu JingxuanYang WenjieHuang ChupengAn XiaoliSi Qingzong - Hypoxia is a key feature of the tumor microenvironment in colorectal cancer (CRC), but the mechanisms linking hypoxia to metastasis remain incompletely understood. To investigate this, bioinformatics analysis of The Cancer Genome Atlas (TCGA) and Clinical Proteomic Tumor Analysis Consortium (CPTAC) datasets assessed TAR DNA-binding protein 43 (TDP-43) expression and its correlation with hypoxia-inducible factor-1α (HIF1A). In vitro and in vivo functional assays, including Cell Counting Kit-8 (CCK-8), Transwell, chicken chorioallantoic membrane (CAM), and xenograft, were conducted to evaluate proliferation, migration, invasion, and angiogenesis. Mechanistic studies, including chromatin immunoprecipitation (ChIP), RNA immunoprecipitation (RIP), luciferase reporter, and actinomycin D assay, were conducted to elucidate HIF1-mediated transcriptional regulation of TARDBP and TDP-43-dependent stabilization of thyroid receptor-interacting protein 6 (TRIP6) mRNA. As a result, TDP-43 was upregulated in CRC tissues and correlated with HIF1A expression. Hypoxia induced TDP-43 expression through HIF1-dependent transcriptional activation via direct binding to hypoxia-response element (HRE) 3 site in the TARDBP promoter. TARDBP knockdown suppressed hypoxia-induced proliferation, migration, invasion, and vascular endothelial growth factor (VEGF) secretion, which were rescued by HIF1A overexpression. RIP-qPCR revealed TDP-43 binding to TRIP6 mRNA via its RNA recognition motifs (RRM domains), stabilizing TRIP6 transcripts and promoting its expression. TRIP6 reconstitution reversed the anti-tumor effects of TARDBP silencing. In vivo, TARDBP depletion inhibited tumor growth and downregulated metastasis-related factors in xenograft models. In conclusion, the HIF1-TARDBP-TRIP6 axis promotes CRC malignancy under hypoxia by integrating transcriptional activation and post-transcriptional mRNA stabilization, offering potential therapeutic targets for advanced CRC. - Source: PubMed
Publication date: 2026/06/12
Cheng KeLiu YonggangFeng WeiyuXu DongliHao Bin