PTP1B Antibody
- Known as:
- PTP1B Antibody
- Catalog number:
- 3171-100
- Product Quantity:
- 100 µg
- Category:
- Antibodies
- Supplier:
- Biovis
- Gene target:
- PTP1B Antibody
Related genes to: PTP1B Antibody
- 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 Antibody
Related articles to: PTP1B Antibody
- Immune evasion by cancer cells remains a major barrier to the success of immune checkpoint blockade (ICB). In recent years, Protein tyrosine phosphatase non-receptor type 2 (PTPN2) has emerged as a promising and druggable target for cancer immunotherapy. Small-molecule agents currently in clinical development to inhibit PTPN2 also exhibit substantial activity against the closely related phosphatase PTPN1. However, the relative contribution of each phosphatase and its direct effect in cancer cells remains unclear. Here, we identify the phosphatases PTPN1 and PTPN2 as cooperative regulators of tumor immune resistance. Dual genetic ablation of PTPN1/2 in cancer cells enhances Type I and II interferon signaling, MHC-I and CXCL9 expression, and sensitizes tumor cells to cytotoxic T lymphocyte-mediated killing. Mechanistically, loss of PTPN1/2 augments STAT1/3/5 signaling, lowering the activation threshold for interferon-driven inflammatory cell death and increasing antigen availability for immune recognition. However, by amplifying STAT1/3 signaling, PTPN1/2 ablation or inhibition concomitantly increases PD-L1 expression in tumor cells, thereby revealing the PD-1/PD-L1 axis as a therapeutic bottleneck during PTPN1/2 inhibition. Consistent with this model, PTPN1/2 inhibition sensitized immune checkpoint blockade-refractory tumors to PD-1 blockade in a tumor-intrinsic manner. These findings identify PTPN1/2 as cooperative mediators of cancer immune evasion and support PTPN1/2 inhibition as a strategy to enhance the responsiveness of solid tumors to checkpoint blockade. - Source: PubMed
Publication date: 2026/08/11
Poirier Alexandre JFeng Chu-HanWalback ErikaSu RuiHincapie Ana MariaAubry IsabelleWu ChenyueSt-Laurent ElisabethUttam SonaliColalillo BiancaHardy SergeDoré SamuelThéberge Jean-FrançoisTremblay Michel L - Mesenchymal stem cells (MSCs) are a promising cell source for osteoarthritis and intervertebral disc degeneration, but their application is limited by inefficient and unstable chondrogenic differentiation. Here, nine Phorbazole D analogues were synthesized and evaluated for promoting chondrogenesis in human umbilical cord mesenchymal stem cells (hUC-MSCs) under TGF-β/dexamethasone based induction conditions. Among the tested analogues, IO-5a was selected for further evaluation based on its comparatively higher pro-chondrogenic activity and no detectable cytotoxicity. Image-based Alcian blue analysis showed that the positive staining area increased from approximately 17% in the control group to approximately 45% after IO-5a treatment. RT-qPCR further showed that 10 µM IO-5a upregulated COL2A1, SOX9, ACAN, and COMP by approximately 2.6-fold, 1.1-fold, 1.35-fold, and 1.4-fold, respectively. Immunofluorescence, western blotting, and 3D pellet culture analyses supported increased cartilage associated marker expression and cartilage like matrix deposition. Preliminary structure-activity relationship analysis suggested that retention of the A-ring phenolic hydroxyl group and favorable A-/C-ring substituent matching may contribute to activity. In silico target prediction and molecular docking nominated PTPN1 (PTP1B) as a potential candidate protein, although this predicted interaction requires further experimental validation. Collectively, IO-5a represents a bioactive Phorbazole D analogue with chondrogenesis promoting activity in hUC-MSCs. - Source: PubMed
Publication date: 2026/07/30
Wang Ai-ZhuLiu Xiao-MeiZhang Li-MingFu Lu-LuLi PingZhang Jie-PingHan Hua - Diabetes mellitus, particularly type 2 diabetes mellitus (T2DM), represents a major global health challenge, driven by the increasing prevalence of obesity and sedentary lifestyles. T2DM is characterized by insulin resistance and progressive β-cell dysfunction, leading to chronic hyperglycemia and multiple complications. Among the molecular targets investigated for therapeutic intervention, protein tyrosine phosphatase 1B (PTP1B) has emerged as a key negative regulator of insulin signaling. By dephosphorylating the insulin receptor and its downstream substrates, PTP1B attenuates insulin action and contributes to metabolic dysfunction. In addition to its role in glucose homeostasis, PTP1B is implicated in obesity, diabetic complications, neurodegenerative disorders, and cancer, highlighting its relevance as a multifunctional therapeutic target. However, the development of PTP1B inhibitors remains challenging due to the highly conserved and polar nature of its catalytic site, which limits selectivity and cell permeability. Recent research has focused on alternative strategies, including allosteric modulation and multi-site inhibition, to overcome these limitations. This review provides a comprehensive overview of PTP1B inhibitors from both synthetic (2019-2025) and natural sources, with particular emphasis on natural products reported from 2022 onwards, while including selected earlier studies to provide historical context and illustrate representative structural classes and inhibition mechanisms. Although PTP1B remains an attractive therapeutic target, its clinical validation for diabetes treatment has yet to be achieved. Continued advances in medicinal chemistry and allosteric modulation may help overcome the current translational barriers. - Source: PubMed
Publication date: 2026/07/19
Braconi LauraMattolini LorenzoRomanelli Maria NovellaTeodori ElisabettaManetti Dina - Chemically induced proximity is a powerful modality for manipulating protein function. Most of the effort in this field has focused on targeted protein degradation, but recruitment of other types of post-translational modification enzymes to a target protein is also of interest. To construct such reagents, one would ideally like to have ligands that engage the enzyme without inhibiting its activity. In this study, we describe a screening platform for the discovery of noninhibitory macrocyclic ligands for a protein tyrosine phosphatase, using PTP1B as an exemplary model target. This workflow involves sequential screens of small libraries of bead-displayed macrocycles in which only one position of the macrocycle is varied in each round of screening while the others are held as invariant placeholders. The beads co-display a high KM substrate for the phosphatase, allowing ligand-dependent recruitment of the enzyme to the bead surface to be coupled to dephosphorylation of the co-displayed substrate. This is detected by staining with a labeled anti-phosphotyrosine antibody. Finally, we demonstrate that the same general approach can be applied to proteins lacking enzymatic activity by screening against biotin ligase-target protein fusions and employing a proximity labeling-like assay to register screening hits. - Source: PubMed
Dong JiajunLi BoFu Chung-WeiKodadek Thomas - This study aimed to identify and validate potential endoplasmic reticulum stress-related biomarkers of focal segmental glomerulosclerosis(FSGS). - Source: PubMed
Publication date: 2026/07/05
Wang HongyuZou JunLi HongbinJiang Gengru