VEGFR2 (Phospho_Tyr951) Antibody
- Known as:
- VEGFR2 (Phospho_Tyr951) Antibody
- Catalog number:
- E011086-2
- Product Quantity:
- 100ug
- Category:
- Antibodies
- Supplier:
- EnoGene
- Gene target:
- VEGFR2 (Phospho_Tyr951) Antibody
Related genes to: VEGFR2 (Phospho_Tyr951) Antibody
- Gene:
- KDR NIH gene
- Name:
- kinase insert domain receptor
- Previous symbol:
- -
- Synonyms:
- FLK1, VEGFR, VEGFR2, CD309
- Chromosome:
- 4q12
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-10
- Date modifiied:
- 2019-04-23
Related products to: VEGFR2 (Phospho_Tyr951) Antibody
Related articles to: VEGFR2 (Phospho_Tyr951) Antibody
- Inhibition of the VEGF/VEGFR-2 pathway is a validated strategy to suppress tumor angiogenesis and progression; however, long-term use of several VEGFR-2 tyrosine kinase inhibitors is limited by resistance and systemic toxicity. Here, a series of novel indolinone-matrine hybrids were designed and synthesized via a molecular hybridization strategy. The antiproliferative activities were evaluated against human hepatocellular carcinoma (HCC) cell lines (HepG-2, HuH7, and MHCC97H). Among them, J9 showed the most potent activity with IC values of 5.81, 2.14, and 3.03 μM, respectively, and relatively low cytotoxicity toward HEK-293 cells (IC = 27.90 μM) and HL7702 cells (IC50 = 52.23 μM). In HuH7 cells, J9 significantly inhibited colony formation and migration, induced G1-phase arrest, and promoted apoptosis in a dose-dependent manner. Western blot analysis indicated that J9 treatment was associated with downregulation of VEGFR-2 and activation of caspase-dependent apoptosis (increased cleaved caspase-3 and cleaved PARP). Moreover, J9 inhibited VEGFR-2 kinase in vitro (IC = 253.51 ± 1.21 nM), and docking/MD simulations suggested stable binding within the VEGFR-2 ATP-binding pocket. Collectively, J9 represents a promising matrine-derived antitumor candidate with potential VEGFR-2-targeting activity. - Source: PubMed
Wang ZiyiWei YongquanXing ZexuJiang LiheWang Lisheng - The peach-potato aphid, Myzus persicae Sulzer (Hemiptera: Aphididae), is among the most destructive and adaptable agricultural pests worldwide, known for its ability to colonize hundreds of host plants and transmit numerous plant viruses. Moreover, it has evolved resistance to more insecticide classes and active ingredients than any other known arthropod pest, making it a key model for studying the evolution of resistance. This review synthesizes the biochemical, genetic, and ecological mechanisms underpinning this adaptability. We trace the historical and contemporary development of resistance to organophosphates, carbamates, pyrethroids, neonicotinoids, sulfoximines, ketoenols, and other insecticides, highlighting how metabolic detoxification by cytochrome P450 monooxygenases, carboxylesterases, glutathione S-transferases (GSTs), and uridine diphosphate-glycosyltransferases (UDPGTs) interacts with target-site mutations such as modified acetylcholinesterase (MACE), knockdown resistance (kdr), super-kdr, R81T, and acetyl-CoA carboxylase (ACC) substitutions. We also examine the regulation of these pathways through gene amplification, transcriptional plasticity, and inducible responses, while emphasizing fitness trade-offs that shape resistance dynamics in the field. By integrating these diverse perspectives, this review goes beyond cataloguing mechanisms to provide a comprehensive framework that explains how multi-resistant clones of M. persicae emerge and persist. We further discuss the implications of composite genotypes for resistance monitoring and management, and outline future directions including molecular diagnostics, synergists targeting detoxification enzymes, and integrated pest management strategies. Together, these insights underscore the urgent need for sustainable, informed approaches that account for genetic and biochemical dimensions of resistance to preserve the efficacy of current and future insecticides against this globally significant pest. - Source: PubMed
Publication date: 2026/03/03
Ali JaminTonğa AdilKhan Khalid AliOberemok VolYusuf Abdullahi AhmedChen Rizhao - Pain is the primary symptom of Achilles tendinopathy, with neovascularisation implicated in symptom development despite unclear mechanisms. Neovascularisation and pain are regulated by vascular endothelial growth factor A (VEGFA) and its receptor, KDR. Since VEGFA polymorphisms have previously been associated with Achilles tendinopathy, this study aimed to determine whether VEGFA (rs699947 C>A, rs2010963 G>C) and/or KDR (rs2071559 C>T, rs1870377 A>T) polymorphisms are associated with exercise-related pain at injury onset, multiple and/or bilateral injuries, as well as self-reported pain using multidimensional pain scales. - Source: PubMed
Publication date: 2026/04/13
Brazier Christina DMkumbuzi Nonhlanhla SLaguette Mary-Jessica NSeptember Alison VCollins Malcolm - Merkel cell carcinoma (MCC) is a neuroendocrine carcinoma of the skin characterized by poor prognosis. This study aimed to explore the relationship between genetic alterations, tumor mutational burden (TMB), and MCC-specific survival (MCC-SS) in patients who underwent genomic profiling of tumors with OncoPanel. Univariate and multivariable analysis were used to assess the impact of genetic alterations on MCC-SS. Of the 188 identified patients, 164 were included in the analysis. The cohort had a mean age of 72.4 years (SD = 11.03), including 61.6% male. The median TMB was 5.32 (IQR = 3.04-25.53). Kaplan-Meier curves by high versus low TMB were significantly different (log-rank test, P = 0.017). PIK3CA (adjusted P = 0.003), SETBP1 (adjusted P = 0.002), KDR (adjusted P = 0.028), and RET (adjusted P = 0.033) were selected for multivariable analysis. In the multivariable regressions, only PIK3CA (HR = 2.07 [95% CI, 1.10-3.88]; P = 0.024) remained significant. PIK3CA remained significant across prespecified sensitivity analyses. In this study, high TMB and PIK3CA alterations were associated with poor MCC-SS. Identifying a higher-risk subgroup may inform risk stratification and motivate further evaluation of PI3K pathway targeting in future studies. - Source: PubMed
Publication date: 2026/04/22
Lobo MatheusBahar FurkanSchnabel Julia LNeto Joao P DupratShetty AniketKhaddour KaramThakuria ManishaSilk Ann WDeCaprio James A - - Source: PubMed
Publication date: 2026/04/22
Ladha Feria AAvillach PaulOpotowsky Alexander RNael AldweibBrueckner MartinaChung Wendy KCnota James FGelb Bruce DLewis MatthewLiu CongRoberts Amy ESeidman Christine ESeidman J GTristani-Firouzi MartinWagner MichaelNewburger Jane WKim YuriMorton Sarah U