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
- 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 - The interaction between mammalian enabled protein (Mena), an actin regulatory protein, and protein tyrosine phosphatase 1B (PTP1B) is critical for maintaining epidermal growth factor receptor (EGFR) signaling homeostasis and regulating cellular motility. Mena recruits PTP1B to activated EGFR in vivo, facilitating receptor dephosphorylation and limiting invasive signaling. However, overexpression of wild-type Mena or the invasive isoform, MenaINV, perturbs this regulatory mechanism by altering PTP1B localization and EGFR signaling dynamics. Here, we report the solution NMR structure of the unliganded Mena EVH1 domain, which contains a conserved aromatic triad (Y16, W23, F77) that forms the canonical polyproline-binding cleft. Building on prior evidence that the PTP1B polyproline region serves as an EVH1 ligand, we investigated the structural basis of the interaction between EVH1 and wild-type PTP1B. NMR chemical shift perturbation analyses using multiple PTP1B variants, including full-length and truncated constructs, revealed that binding affects not only the canonical EVH1 hydrophobic cleft but also residues on the opposite surface, suggesting an expanded interaction interface. Diffusion-ordered spectroscopy (DOSY) and size-exclusion chromatography further indicate that PTP1B variants containing the disordered C-terminal tail form more compact complexes with EVH1, consistent with a disorder-to-order transition. Complementary perturbation studies using [2H,15N] PTP1B demonstrate that EVH1 binding induces changes not only in the polyproline region but also across the phosphatase core, α7 helix, and C-terminal tail. Despite these structural perturbations, enzymatic assays show that EVH1 binding does not affect the catalytic activity of PTP1B, supporting a model in which Mena functions as a scaffold to spatially organize PTP1B within EGFR signaling complexes. - Source: PubMed
LaComb LanetteCahill Sean MBonanno Jeffrey BCowburn DavidAlmo Steven CGhosh Agnidipta - To evaluate clinical outcomes (performance-based tests and patient-reported outcome measures [PROMs]) and biomechanical measures of movement smoothness, and explore their associations with molecular markers in individuals with knee osteoarthritis (KOA). - Source: PubMed
Publication date: 2026/07/30
Gawelowicz KarolSimonsen Morten BildeHedström MargaretaBroström EvaAulin CeciliaNaili Josefine E