ZAP_70
- Known as:
- ZAP_70
- Catalog number:
- 000341A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ZAP_70
Related genes to: ZAP_70
- Gene:
- ZAP70 NIH gene
- Name:
- zeta chain of T cell receptor associated protein kinase 70
- Previous symbol:
- SRK
- Synonyms:
- ZAP-70, STD
- Chromosome:
- 2q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-16
- Date modifiied:
- 2019-04-23
Related products to: ZAP_70
70 kDa zeta-associated protein,Homo sapiens,Human,SRK,Syk-related tyrosine kinase,Tyrosine-protein kinase ZAP-70,ZAP7070 kDa zeta-associated protein,Mouse,Mus musculus,Srk,Syk-related tyrosine kinase,Tyrosine-protein kinase ZAP-70,Zap70,Zap-70Anti- Zap-70 (Ab-319) AntibodyAnti- Zap-70 (Ab-319) AntibodyAnti- Zap-70 (Ab-493) AntibodyAnti- Zap-70 (Ab-493) AntibodyAnti- Zap-70 (Phospho-Tyr319) AntibodyAnti- Zap-70 (Phospho-Tyr319) AntibodyAnti- Zap-70 (Phospho-Tyr493) AntibodyAnti- Zap-70 (Phospho-Tyr493) AntibodyAnti-Human_Mouse ZAP-70 APC 100 testsAnti-Human_Mouse ZAP-70 APC 25 testsAnti-Human_Mouse ZAP-70 Biotin 100 ugAnti-Human_Mouse ZAP-70 Biotin 25 ugAnti-Human_Mouse ZAP-70 FITC 100 ug Related articles to: ZAP_70
- Bladder cancer (BC) is a highly prevalent malignant tumor. The traditional Chinese medicine formula Guo Lou Qu Mai Wan (GLQMW), when used in conjunction with chemotherapy, has been shown to reduce adverse reactions and prolong survival time, although its specific mechanisms remain unclear. This study aims to investigate whether GLQMW exerts its therapeutic effects on bladder cancer by modulating the tumor immune microenvironment. - Source: PubMed
Publication date: 2026/04/15
Teng QiliangCheng ShuminChen JiaZhu HongyaHu KaiSun LinglingZhao JinYuan ZhenboWang WenjingZhang LiLiu TaoliFeng Jiahao - Ionic imbalance in the tumor microenvironment alters the function of tumor-infiltrating T lymphocytes. High extracellular K suppresses T cell function by negatively regulating T cell receptor (TCR) signaling. The mechanism of how monovalent cations regulate T lymphocyte function is unknown. Here, we present a mechanism that explains how cellular potassium dynamics regulate TCR function. At rest, high intracellular K uncouples allosteric recruitment of ZAP-70, a key signaling module, to the TCR complex. Elevated K concentration imparts a higher thermodynamic penalty on the binding of the ZAP-70 regulatory module to the phosphotyrosine residues in the ITAM motifs of the CD3 chain. Our data suggest that K functions as a key allosteric modulator, stabilizing the autoinhibited conformation of ZAP-70. Thus, it prevents spontaneous TCR activation in the resting state. Formation of the antigen-TCR complex induces K efflux, leading to spontaneous recruitment of ZAP-70 to the TCR. Increasing extracellular K concentration perturbs K efflux and slows ZAP-70 recruitment to the TCR complex, even upon antigen binding. Impaired ZAP-70 activation partially dampens TCR signaling, thereby altering downstream signaling. In contrast, the regulatory module in the paralogous kinase Syk, which is expressed in B cells, is insensitive to potassium concentration. At elevated K concentration, the interaction between the Syk regulatory module and phosphorylated ITAM motifs remains unaltered. We conclude that K dynamics are integral to T cell ligand discrimination and fundamental to turning off the signaling during T cell quiescence. - Source: PubMed
Publication date: 2026/04/27
Roy SwarnenduSenGupta SoumeeGangopadhyay KaustavMajumder SudiptaDas JibiteshSinha AnushkaDas Prosad KumarSinha BidishaDas Rahul - Colon cancer (CC) ranks as the third most common cancer and the second leading cause of cancer-related death worldwide. Despite significant advances in treatment and early intervention, the precise mechanisms of action for many targeted therapies remain to be fully elucidated. This study aimed to investigate the potential off-target effects of the AURKA inhibitor Alisertib in colon cancer. Transcriptomic analysis revealed a striking divergence between AURKA silencing and Alisertib treatment: AURKA knockdown predominantly affected cell cycle-related pathways, whereas Alisertib significantly modulated immune-related pathways. This functional heterogeneity at the transcriptomic level suggests that Alisertib's mechanism of action is not solely dependent on AURKA inhibition. Through bioinformatics prediction and experimental validation, we further identified ZAP70 as a leading candidate mediator of Alisertib's effects. Crucially, a series of in vitro and in vivo experiments demonstrated that Alisertib's ability to suppress malignant phenotypes and tumor growth in colon cancer cells was maintained irrespective of AURKA overexpression, confirming its AURKA-independent activity. Collectively, our findings systematically reveal that Alisertib exerts significant AURKA-independent antitumor effects in colon cancer, likely mediated through alternative mechanisms such as the regulation of ZAP70 and associated immune pathways. This study provides a novel perspective on the pharmacological action of Alisertib and its clinical application. - Source: PubMed
Publication date: 2026/04/29
Gao QiZhang XingyuHui KaiyuanZou XunLi LuyaoYu ZienFeng YiwenShen XiaozhuJiang XiaodongLiu Bin - Pulmonary fibrosis (PF) is a life-threatening interstitial lung disease characterized by scarring and inflammation in lung tissues. Aberrant activation of the JAK/STAT and NF-κB signaling pathways is critical in initiating and sustaining the inflammatory processes that drive fibrotic progression. In this study, we identify a novel small-molecule compound, T4015, a 4-indolyl-2-phenylaminopyrimidine derivative, as a dual-pathway inhibitor targeting both JAK/STAT and NF-κB signaling. Dual-luciferase reporter assays demonstrate the potent inhibitory activity of T4015 against these pathways. T4015 effectively suppresses the phosphorylation of STAT3, JAK1, and TYK2 induced by IL-6 and IFN-β, while suppressing LPS-induced NF-κB activation in macrophages. Transcriptome sequencing and pathway enrichment analyses further confirm that T4015 downregulates multiple inflammation-related signaling cascades, including the JAK/STAT, NF-κB, TNF, IL-17, and Toll-like receptor pathways. In a mouse model of bleomycin-induced PF, T4015 treatment significantly improves survival, attenuates collagen deposition, and reduces the expression of pro-inflammatory and profibrotic markers such as IL-6, CCL2, and COL1. Molecular docking and target prediction analyses suggest that T4015 exhibits strong binding affinity for multiple kinases within the JAK/STAT and NF-κB networks, including JAK1, TYK2, JAK2, JAK3, RIPK1, IRAK1/4, TAB1, and ZAP70. Collectively, these results highlight T4015 as a promising therapeutic candidate for PF through its simultaneous inhibition of the JAK/STAT and NF-κB signaling pathways. - Source: PubMed
Publication date: 2026/04/25
Zhang MinghuiXu HangLiu ShanXu XiaohanYin JiayiZhang XinxinZhang XiaonanYang XiaopingLiu XiaochunYin BinZhou MingmingWang LeweiZhang MengLiu HuiyingJiang WenqingSong QiaolingYang Jinbo - Actin-rich protrusions densely cover the surface of T cells and are well characterised for their role in migration. Recent studies have uncovered their contribution to antigen surveillance and immune signalling. To further explore how protrusions initiate signalling pathways mediating T-cell activation, we performed live-cell imaging of endogenously tagged proteins in HER2-specific chimeric antigen receptor (CAR) T cells targeting HER2⁺ breast-cancer cells. Quantitative STED microscopy allowed us to monitor protein rearrangement and to correlate it with membrane topology over time. Before activation, key signalling proteins (including Lck, CD45, LAT, and the CAR) were not enriched in protrusions. Upon contact with target cells, rapid protein reorganisation occurred preferentially within protrusions, initiating signalling. HER2-CAR clustering, accompanied by ZAP-70 and LAT recruitment, was enhanced in protrusions. While Lck distribution remained unchanged, exclusion of the phosphatase CD45 was enhanced at protrusion-cell contacts, independently of the CAR signalling domain. Overall, signalling machinery rearranged faster and more effectively at protrusive contacts than at main plasma membrane regions. Together, our data re-frame protrusions as sites of enhanced receptor activation by exclusion and clustering dynamics rather than by pre-enrichment of the signalling machinery. - Source: PubMed
Publication date: 2026/04/21
Rodilla-Ramirez CarmenCarai GiorgiaFox EleanorZehtabian AminAdam HelenDallio KatjaLazki-Hagenbach PiaEwers HelgeSu XiaoleiBottanelli Francesca