c_Myc EMSA Probe Set
- Known as:
- c_Myc EMSA Probe Set
- Catalog number:
- AY1283P
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- c_Myc EMSA Probe Set
Related products to: c_Myc EMSA Probe Set
(+) Control probe (DNA), biotinylated(+) Control probe (RNA), biotinylated(-) Control probe (DNA), biotinylated(-) Control probe (RNA), biotinylated0.2 mm, 30 cm Spacer Set
0.2 mm, 30 cm Spacer Set0.35 mm, 30 cm Spacer Set
0.35 mm, 30 cm Spacer Set0.5 mm, 30 cm Spacer Set
0.5 mm, 30 cm Spacer Set0.75 mm Dual Gel Cast Set
0.75 mm Dual Gel Cast Set0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
0.75 mm Plate Set, RM
Related articles to: c_Myc EMSA Probe Set
- Non-small cell lung cancer (NSCLC) remains difficult to cure owing to therapy resistance and immune evasion that limits durable therapeutic responses. Here, we report a carrier-free nanoregulator (CE NPs) formed by co-assembling chlorin e6 (Ce6) with a covalent c-Myc inhibitor (EN4), enabling photo-immunotherapy that couples photodynamic therapy (PDT)-induced immunogenic cell death (ICD) with acetate-metabolism-driven immune reprogramming. Upon 660-nm light irradiation, CE NPs efficiently generate reactive oxygen species to trigger apoptosis and subsequent ICD. In parallel, EN4-mediated c-Myc suppression coordinately downregulates MCT1, Cyclin D1, LDHA, and PD-L1, thereby interrupting the MCT1/acetate/acetyl-CoA/c-Myc self-amplifying "closed-loop" circuit, restraining tumor proliferation and glycolysis, and alleviating PD-L1-associated immune escape. Consequently, CE NPs, along with 660-nm light illumination, achieve robust tumor growth inhibition without obvious systemic toxicity under the tested conditions, promotes systemic immune activation, suppresses distant tumors in a bilateral model, and establishes durable immune memory that resists tumor rechallenge. Collectively, this work establishes a "closed-loop regulatory circuit" strategy by integrating PDT-induced ICD with acetate-metabolism reprogramming to overcome immune evasion and improve NSCLC photo-immunotherapy. - Source: PubMed
Publication date: 2026/09/10
Zhu JianweiDong DanmingXu JiayueTang XiaopengGao YuanZhu JinbinZhuang YiniZhang PeiLv ZhuangChen XiaoyuanZou JianhuaShi Huaxia - How cancers regulate endoplasmic reticulum (ER) pH and minimize ER stress remains unclear. Here we show that in breast cancer, these processes are governed by the anion channel GPR89. While normally localized to the Golgi, we find GPR89 is also present in the ER of tumor cells, where it collaborates with vacuolar H⁺ ATPase to regulate pH, and reduces ER stress via IRE1α-HSP47-XBP1s, ATF6 and ATP2A2 pathways. This ER localization of GPR89 drives a tumor-specific dependency, rendering breast cancer cells, but not normal tissues, dependent on this anion channel. Structural modeling and mutagenesis identify five key amino acids essential for GPR89's ER pH regulatory function and tumor cell survival. Consistent with its cancer-specific functions, GPR89 cooperates with Myc to accelerate mammary tumorigenesis. These findings uncover how breast cancers adapt to oncogenic stress by co-opting Golgi mechanisms of pH regulation to support ER homeostasis and survival. - Source: PubMed
Publication date: 2026/08/24
Ferro RiccardoCarroll AlexandraMendes-Pereira Ana MReen VirinderVlachogiannis GeorgeUceda-Castro RebecaKrastev DragomirAmodeo ValeriaPettitt StephenD'Uonno NadjaMavrommati IoannaNavarro BlancaHitchen LukeTrendell JenniferStojiljkovic AnaPrince CynthiaJanghra NarinderRoxanis IoannisGazinska PatrycjaLarcombe-Young DanielMarlow RebeccaAnnunziato StefanoJonkers JosKanitkar Tejashree RajaramXu AmadeusPatel NirmeshLiv NalanAlexander JohnQuist JelmarPardo MercedesRoumeliotis Theodoros IChoudhary Jyoti SWeekes DanielMarra PierfrancescoLoizou Joanna INatrajan RachaelGrigoriadis AnitaMadhusudhan Mallur SrivatsanHaider SyedLord Christopher JTutt Andrew - Ischemic stroke is a leading cause of death and disability, with limited therapies for neurological recovery. Buyang Huanwu Decoction (BYHWD) is a traditional Chinese medicine formula used for stroke, but its effects on endogenous neurogenesis and the underlying mechanisms remain incompletely defined. - Source: PubMed
Publication date: 2026/09/22
Xu JiadongLiu ShuyanChen HaoweiSang TingtingZhang YaniSheng XuanYang YanFang YanXu LanxiChu Lisheng - /Aims: Hepatocellular carcinoma (HCC) is an aggressive disease with limited response to available therapies. Progress in therapeutic development has been hampered by the lack of preclinical models that recapitulate human HCC and support evaluation of multimodal therapies. Here, we employ CRISPR editing to identify alterations that drive hepatocyte transformation and to establish genetically defined HCC models. - Source: PubMed
Publication date: 2026/09/22
Elkhadragy LobnaDavid Olayinka GCastillo Caitlyn CRedlon Luke NJordan Luke RKhan NusratLiu HannahRosa Lopes Isadora AndreZhou YanqiongKanzaki HiroakiHoshida YujinSamuelson Jonathan PLujambio AmaiaSchook Lawrence BGuzman GraceSchachtschneider Kyle MGaba Ron C - Parafibromin/CDC73 is a multifunctional nuclear scaffold protein with context-dependent roles in tumorigenesis, functioning as both a tumor suppressor and an oncogenic driver. Originally identified as the product of the HRPT2 tumor suppressor gene, which is mutated in hyperparathyroidism-jaw tumor syndrome, Parafibromin represses the transcription of pro-mitogenic and oncogenic genes by interacting with SUV39H1. Parafibromin also associates with β-catenin, the central effector of the canonical Wnt (Wnt/β-catenin) pathway, a major morphogen signaling pathway frequently activated in cancer. The Parafibromin/β-catenin complex acts as a transcriptional co-activator, promoting pro-oncogenic Wnt targets such as c-Myc and Cyclin D1. This nuclear scaffold function of Parafibromin is regulated by its tyrosine phosphorylation status at Y290, Y293, and Y315: PTK6/BRK phosphorylates these tyrosine residues, whereas SHP2 dephosphorylates them. Dephosphorylated Parafibromin forms a stable complex with β-catenin, while phosphorylation prevents this interaction and abolishes Parafibromin-mediated Wnt activation. This mechanism may play a critical role in the development of hepatocellular carcinoma, in which SHP2-mediated tyrosine dephosphorylation of Parafibromin enhances Wnt signaling and promotes the dedifferentiation of hepatoma cells into cancer stem-like cells. In addition to β-catenin, Parafibromin acts as a multivalent scaffold that interacts with key transcriptional effectors in morphogen signaling pathways, such as Hedgehog and Notch signaling, as well as with YAP1 and TAZ in the mechanosensing Hippo signaling. Notably, these interactions of Parafibromin are also controlled by its phosphorylation status at Y290/Y293/Y315. Thus, deregulated Parafibromin tyrosine phosphorylation disrupts the coordinated intracellular signaling required for normal cell growth and differentiation, highlighting Parafibromin as a potential therapeutic target in cancer. - Source: PubMed
Publication date: 2026/09/17
Takahashi-Kanemitsu AtsushiKikuchi IppeiMurata-Kamiya NaokoHatakeyama Masanori