PTP1B Recombinant Protein
- Known as:
- PTP1B Recombinant Protein
- Catalog number:
- ZR-53-301
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- PTP1B Recombinant Protein
Related genes to: PTP1B Recombinant Protein
- Gene:
- PTPN1 NIH gene
- Name:
- protein tyrosine phosphatase non-receptor type 1
- Previous symbol:
- PTP1B
- Synonyms:
- -
- Chromosome:
- 20q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1991-09-13
- Date modifiied:
- 2019-02-14
Related products to: PTP1B Recombinant Protein
Related articles to: PTP1B Recombinant Protein
- Protein tyrosine phosphatases (PTPs) are pivotal in cellular signal transduction. Recent studies have identified protein tyrosine phosphatase, non-receptor type 1 (PTPN1), as a novel immune checkpoint. However, its effects and underlying mechanisms in hepatocellular carcinoma (HCC) remain underexplored. This study aims to elucidate the impact of PTPN1 on the prognosis of HCC patients, the tumor microenvironment (TME), and the biological behavior of HCC cells, with the goal of assessing its clinical potential in HCC. - Source: PubMed
Publication date: 2026/06/23
Zhan ZhaoShi DingfangHuang RongDong DoudouZhou LiliRen ZichunChen ShihuaLin MingqiangXin ChenqiLin Yaobin - Metabolic diseases such as type 2 diabetes and obesity represent a rapidly escalating global health burden, while existing therapeutic strategies largely target isolated symptoms or single molecular pathways. To address this limitation, we developed an integrated computational pipeline leveraging a knowledge graph, pathway enrichment, and network pharmacology to elucidate multi-target mechanisms of Single Herbal Drugs (SHDs). SHDs associated with diabetes and obesity were curated from the Ayurvedic Pharmacopoeia of India, and their phytochemicals were identified using the IMPPAT database. Following drug-likeness and predicted bioavailability filtering, 11 SHDs and 188 phytochemicals were shortlisted. Molecular targets of these phytochemicals, along with disease-associated genes and therapeutic targets of FDA-approved drugs, were compiled through multi-database integration. Pathway enrichment analysis revealed significant overlap between SHD-associated and disease-associated pathways. All curated data were integrated into a Neo4j-based knowledge graph to enable SHD-disease intersection analysis, prioritizing key targets such as PTPN1, GLP1R, and DPP4. SHD-Target-Drug profiling demonstrated convergence with clinically validated drug combinations. Network pharmacology based on protein-protein interaction network analysis further identified PPARG as a central regulatory hub. We propose a quantitative framework to identify structurally dissimilar phytochemical pairs acting on complementary disease-associated targets, highlighting non-redundant network-level interactions and generating mechanistic hypotheses for potential synergy. Molecular docking of PPARG and DPP4 identified promising lead phytochemicals, including Chitraline, Isovitexin, and Pakistanine for DPP4, and Sulfurein, Sesamin, and Pterosupin for PPARG. Overall, this integrative approach provides a robust systems-level framework for mechanistically dissecting SHDs and bridging traditional herbal knowledge with modern biomedical research. - Source: PubMed
Publication date: 2026/06/17
Sil PriyotoshTiwari RahulGarisetti VasaviBaskaran Shanmuga PriyaDhanaseelan Fenita HephzibahSrivastava SmitaSamal Areejit - Diabetic retinopathy (DR) is the leading cause of vision loss in the working-age population, with public health economic implications worldwide. Systemic inflammation and leukocyte activation are early events in diabetes, whereas microglial activation, neuroinflammation, and retinal neurodegeneration are early events in DR. Protein tyrosine phosphatase 1B (PTP1B) plays a complex role in monocyte and macrophage activation, which may affect DR. We investigated the role of myeloid cell-specific PTP1B using LysMcre-PTP1B fl/fl (LysM-PTP1B) transgenic mice, as well as pharmacological inhibition with a PTP1B inhibitor, MSI-1436, in the early stages of DR. Mice were rendered diabetic for 6 weeks using anomer-equilibrated streptozotocin (STZ). Retinal changes were evaluated by histology and immunohistochemistry, and systemic leukocyte activation by flow cytometry. Mitochondrial function in high-glucose-concentration-challenged, cultured bone marrow-derived macrophages (BMDMs) from LysM-PTP1B- and MSI-I436-treated mice was determined in vitro. Both myeloid cell-specific depletion and pharmacological inhibition of PTP1B prevented STZ-induced retinal neurodegeneration, development of acellular retinal capillaries, as well as microglial and systemic leukocyte activation without altering the development of diabetes. In vitro, inhibition of PTP1B prevented high-glucose-level-induced mitochondrial dysfunction in BMDMs. We conclude that inhibition of PTP1B prevents DR by decreasing myeloid cell-driven inflammation, and PTP1B represents a therapeutic target for prevention DR. - Source: PubMed
Ali AyazBoyne MorganOthman AbrarKamli-Salino SarahKuffova LuciaForrester John VDelibegovic Mirela - Targeted degradation of PTPN2 is an attractive cancer immunotherapy strategy. However, unfavorable physicochemical properties limit the development of current PTPN2 degraders. In this study, using a ring-opening scaffold-hopping strategy, we identified a class of alkyne-containing PTPN2 ligands, which were subsequently employed for PROTAC design. Through optimizing linkers and CRBN ligands, we obtained featuring a rigid linker and a naphtholactam-based ligand. exhibits subnanomolar degradation potency (DC = 0.25 nM, 868-fold superior to the previously discovered ) and good subtype selectivity (PTPN2/PTPN1 selectivity >20-fold). Compared to previous PTPN2 degraders, it displays lower molecular weight, fewer hydrogen bond donors/acceptors, and a reduced cLogP. exhibited nanomolar antiproliferation potency in the IFN-γ stimulated HT-29 cell line, nearly 80-fold more potent than the clinical candidate . Moreover, it possessed excellent PTPN2 degradation potency and effectively suppressed tumor growth in mice. Collectively, is a promising lead compound worthy of further study. - Source: PubMed
Publication date: 2026/05/14
Hu LinghaoGuo LitingZhang MengxiWei JingxunHuang QiChen HaowenLiu YingXu XiaominXu LeiZhou YuboLi JiaWang Mingliang - The apoptotic pathway mediated by mitochondria depends on the activation of pro-apoptotic Bcl-2 proteins Bax and Bak. When they permeabilize the outer mitochondrial membrane (OMM), mitochondrial dysfunction occurs, leading to caspase activation. A recent study proposed that Bax accumulation on mitochondria increases apoptotic susceptibility, with adhesion-initiated signals regulating Bax. When adhesion signaling is inhibited, Bax translocates to the OMM, undergoes conformational change, and forms complexes that create pores. Although MOMP is well studied, mechanisms regulating Bax shuttling, non-canonical partners, and mitochondrial dynamics remain poorly understood. - Source: PubMed
Publication date: 2026/05/10
Tanisha Mehrin HaqueSiddique Md AymanAhmed ZubaierMustafa NashrahTasneem Fariha