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
- Metastasis remains the leading cause of cancer mortality, yet effective therapies for inhibiting and treating metastasis are limited. Therapeutic responses are influenced by organ-specific immune microenvironments, highlighting the need to develop strategies to pharmacologically modulate these niches. Here, using the clinical-stage inhibitor ABBV-CLS-484 (AC484) as a chemical probe, we demonstrated that systemic PTPN1/2 inhibition remodels the pulmonary myeloid landscape, specifically activating alveolar macrophages (AMs) toward a tumoricidal state. Integrated single-cell and spatial transcriptomics and functional assays revealed that AC484 promotes accumulation, IFNγ production and responsiveness, and tumor-killing activity of AMs within metastatic lesions. Depletion of AMs diminished the anti-metastatic efficacy of AC484. Mechanistically, inhibition of PTPN1/2 amplified IFNγ-STAT1 signaling in AMs, and disrupting this pathway impaired the tumor control capability of AC484. These findings delineate a distinct innate immune axis where PTPN1/2 acts as a molecular "brake" on AM activation, suggesting that pharmacologically unleashing tissue-resident macrophages offers a therapeutic strategy to overcome metastatic progression, particularly in microenvironments where adaptive immunity is insufficient. - Source: PubMed
Publication date: 2026/09/15
Liu YueSun Im-MengCreixell MarcBrown JordanKharbanda SamirLee James JShahryari VarahramHake KayleyO'Hara JacquelineFinn Kenneth JYang NianxinPenland LolitaWang JiaxiLi Ka ManBalibalos JohnStebbins Aaron WGodfrey Patrick MTai Po-HanMalahias EvangeliaKong WenjunFong NicoleHendrickson DavidGupta ShagunChan Leanne JgMcAllister Fiona EPatel Chirag HPaddock Marcia NNguyen Tuan AndrewHarding Fiona APowell Jonathan D - Immune checkpoint inhibitors (ICIs) have transformed cancer therapy but remain limited by primary and acquired resistance, highlighting the need for novel immunotherapeutic strategies beyond cell-surface receptors. Intracellular immune regulators integrate signaling downstream of immune receptors and therefore represent attractive therapeutic targets capable of simultaneously modulating multiple immunosuppressive pathways. In this review, we summarize recent advances in therapeutics targeting intracellular immunoregulatory proteins that entered or advanced in clinical development between 2022 and 2026, with emphasis on representative targets, biological rationale, clinical development, and emerging therapeutic opportunities. We discuss membrane-proximal signaling regulators, intracellular signaling hubs, and innate immune mediators, including HPK1, DGKα/ζ, SHP2, CBL-b, PTPN1/2, JAK1, PI3Kγ/δ, MALT1, STING, and RIPK2. Current evidence indicates that intracellular regulators downstream of immune receptors warrant particular investigation because they integrate convergent signaling from multiple immune checkpoints and co-stimulatory receptors. Among these targets, HPK1 inhibitors have demonstrated preliminary monotherapy activity in selected patients, whereas the strongest clinical signals for SHP2 inhibition have been observed in combination with KRAS-targeted therapy and may reflect both tumor-cell-intrinsic and immune-mediated effects. Across multiple programs, rational combination strategies, biomarker-guided patient selection, optimized pharmacokinetic properties, and treatment sequencing appear more important than monotherapy. We further discuss major challenges, including incomplete understanding of target biology, limited druggability of certain intracellular proteins, and the need for improved translational strategies. Collectively, intracellular immunomodulators substantially expand the therapeutic landscape beyond conventional ICIs and may contribute to next-generation precision cancer immunotherapy. - Source: PubMed
Publication date: 2026/09/13
Zhang ChunyanZhu JianweiZhou ZiqinLi XianlanSu Qin - Diabetes mellitus affects hundreds of millions of people worldwide and remains a leading cause of multi-organ morbidity. Eriodictyol (Eri), a natural flavonoid enriched in edible plants and other citrus fruits, exhibits antioxidant, anti-inflammatory, and glucose-lowering properties in vitro. However, its systemic efficacy against diabetic hyperglycemia and tissue injury in vivo has not been systematically examined. - Source: PubMed
Publication date: 2026/08/25
Deng XuZheng JiaojiaoXiao Chunxia - Although chlorogenic acid, suramin, ursolic acid, and the glycyrrhetinic acid derivative FC122 are individually known PTP1B inhibitors, no study has systematically characterized how mechanistic diversity determines the pharmacological outcome of their combinations. Here, we integrate experimental enzyme kinetics, molecular docking, molecular dynamics (MD), and membrane permeability simulations to address this question. Individual inhibitory potencies ranked SUR > FC122 > UA > CGA (IC: 1.82, 3.27, 6.12, and 252 µM, respectively). Fixed-ratio combination experiments showed two distinct profiles: additivity for the uncompetitive + mixed pair (FC122 + UA) and competitive + competitive pairs (SUR + CGA), and antagonism for the competitive + uncompetitive combination (SUR + FC122). Docking and MD provided the structural basis for these results and suggested that each combination imposes a distinct structural flexibility profile on the disordered C-terminal region of PTP1B (residues 300-400). For the first time, the MD-AMBER-Umbrella-COM protocol was applied to generate a comparative membrane permeability profile for mechanistically diverse PTP1B inhibitors, proposing a permeability order (SUR > FC122 > CGA ≈ UA). These results suggest that kinetic compatibility is a more reliable predictor of promising inhibitor combinations than binding-site geography alone, and they offer a rational framework for designing multisite PTP1B inhibition strategies in type 2 diabetes mellitus. - Source: PubMed
Trapala JonathanÁlvarez-Añorve Laura IVasquez-Martínez NathalyChavira-Suárez ErikaVásquez-Bochm LuzMatuz-Mares DeyamiraCortés-Benítez FranciscoGonzález-Andrade Martin - Protein tyrosine phosphatases (PTPs) are essential for regulating cell signaling pathways, and their dysregulation is linked to various human diseases, including cancer and diabetes, making them important therapeutic targets. However, developing PTP inhibitors remains challenging due to the conserved structure and charged active sites. In this study, a series of furo[3,2-b]pyrrole-benzimidazole derivatives was designed and synthesized as potential PTP inhibitors. Structure-activity relationship (SAR) studies showed that extending the aromatic system with the benzimidazole scaffold increased potency, and the carboxylic acid group was essential for inhibitory activity. Among the synthesized compounds, 5a was identified as the lead compound, exhibiting strong inhibitory activity against PTP1B (IC = 0.70 ± 0.04 μM) and the oncogenic SHP2-E76K mutant (IC = 0.36 ± 0.02 μM). Molecular docking studies suggest that the inhibitory activity of this series may depend on the compounds' ability to bind a putative allosteric site, thereby stabilizing the WPD loop in its inactive, open conformation; kinetic and biophysical validation of this mechanism is planned for future work. Antiproliferative cell tests demonstrated that although compound 5a exhibited superior enzymatic inhibition, smaller analogs, such as 2a, lacking the extended benzimidazole moiety, showed more potent, dose-dependent cytotoxicity in U2OS human osteosarcoma cells (IC = 16.25 μM vs. 157.24 μM for 5a), likely due to improved physicochemical properties and membrane permeability. These findings offer a promising scaffold for future development and optimization of potent, broad-drug-like PTP inhibitors with enhanced activity against the full-length SHP2-E76K construct relative to the isolated catalytic domains tested. - Source: PubMed
Publication date: 2026/08/16
Milaneh SliemanYe ZehaoGao Li-XingLi JiaZhou Yu-BoXu LeiWang Wen-Long