VEGF165, Rat (CHO-expressed) Protein
- Known as:
- VEGF165, Rat (CHO-expressed) Protein
- Catalog number:
- z03006-1
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Genscript
- Gene target:
- VEGF165 Rat (CHO-expressed) Protein
Related genes to: VEGF165, Rat (CHO-expressed) Protein
- Gene:
- NRP1 NIH gene
- Name:
- neuropilin 1
- Previous symbol:
- -
- Synonyms:
- NRP, VEGF165R, CD304
- Chromosome:
- 10p11.22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-23
- Date modifiied:
- 2016-10-05
- Gene:
- NRP2 NIH gene
- Name:
- neuropilin 2
- Previous symbol:
- -
- Synonyms:
- VEGF165R2
- Chromosome:
- 2q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-23
- Date modifiied:
- 2015-09-01
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- Glioblastoma (GBM) is the most aggressive and malignant primary brain tumor in adults, characterized by rapid growth, diffuse invasion, marked intratumoral heterogeneity, and resistance to conventional therapies. Semaphorin-Plexin signaling, originally identified as a key regulator of axonal guidance during nervous system development, has subsequently emerged as a critical pathway involved in multiple aspects of cancer biology, including tumor proliferation, invasion, angiogenesis, immune modulation, and therapeutic resistance. - Source: PubMed
Publication date: 2026/08/06
Prajapati ShatrudhanSingh Ajay PalTripathi VashnaviYadav Shikha - Vascular endothelial growth factor (VEGF) and its receptor VEGFR are master regulators of vasculogenesis and angiogenesis. VEGF activates VEGFR by inducing its dimerization and trans-autophosphorylation. The coreceptor neuropilin (Nrp1 and Nrp2) and heparan sulfate proteoglycan (HSPG) modulate VEGF-VEGFR signaling, but the underlying mechanisms remain incompletely understood. Here we report a cryo-EM structure of the dimeric mouse VEGF-VEGFR2-Nrp1 ectodomain complex with a 2:2:2 stoichiometry, revealing direct Nrp1-VEGFR2 interactions that stabilize the VEGFR2 dimer. We also determined two cryo-EM structures of the VEGF-VEGFR2-Nrp1 complex in the presence of short- or long-chain heparin, which bridges all three proteins and promotes the formation of two distinct tetrameric complexes. Long-chain heparin induces a cis tetrameric complex consistent with receptor clustering on the same cell surface, whereas short-chain heparin promotes a trans tetrameric assembly which might be formed by two dimeric complexes from opposing cells. Our structure-based mutational analyses support the model that both the Nrp1-VEGFR2 interface and the heparin-mediated clustering enhance VEGFR2 signaling. - Source: PubMed
Publication date: 2026/07/15
Chen LianqiSun ZhichenQiao JianBai Xiao-ChenZhang Xuewu - Pancreatic ductal adenocarcinoma (PDAC) is a highly lethal malignancy in which liver metastasis represents the principal determinant of poor prognosis. Although metastatic dissemination is thought to be driven by highly plastic tumor cells, the transcriptional features of liver metastasis-related initial cell (LMIC) and its spatial crosstalk with the metastatic microenvironment during PDAC progression remain incompletely defined. - Source: PubMed
Publication date: 2026/06/16
Li YangLiu Ya-DieJiang Zhi-YingLu Hong-Xiang - Neuropilins (NRPs), particularly NRP-1, are multifunctional co-receptors involved in neuroinflammatory and neuroprotective processes. Altered NRP expression has been observed in multiple sclerosis (MS) lesions and peripheral circulation, suggesting early involvement in disease progression. This review addresses the dual role of NRPs in MS and experimental autoimmune encephalomyelitis (EAE), emphasizing expression patterns, signaling pathways, and therapeutic interventions. NRP-1 is expressed by endothelial cells, microglia, and macrophages, while Sema3A, a key ligand, is produced by reactive astrocytes and contributes to a non-regenerative microenvironment. NRP-1 is involved in regulating blood-brain barrier (BBB) integrity, contributes to leukocyte trafficking, and modulates inflammatory signaling via the IFN-γ-STAT1-CXCL10 axis. In EAE, endothelial-specific NRP-1 deletion reduces disease severity, demyelination, and immune infiltration. Immunologically, NRP-1 governs interactions among T cells, dendritic cells, and macrophages, facilitating regulatory T cell (Treg) function and peripheral tolerance. Trogocytosis-mediated NRP-1 transfer from dendritic cells to T cells and polysialylated NRP-2 on dendritic cells further influence immune modulation. Tuftsin, a tetrapeptide targeting NRP-1, promotes anti-inflammatory microglial polarization and Treg activation, improving EAE outcomes. Therapeutic interventions, such as Bu-Shen-Yi-Sui Capsule (BSYSC), FTX-101 (a Sema3A-NRP-1 inhibitor), and tuftsin restore BBB function, reduce inflammation, enhance remyelination, and improve clinical scores. NRP-1 signaling thus exhibits context-dependent dual roles: promoting inflammatory cascades while enabling neuroprotection through regulatory immune networks and oligodendrocyte precursor cell support, highlighting NRP-1 as a therapeutic target in MS. - Source: PubMed
Publication date: 2026/05/28
Goleij PouyaBabamohamadi MehreganHeidari Mohammad MahdiKhazeei Tabari Mohammad AminAbolfazli SajadMohammadi SoroushMajma Sanaye PanteaArefnezhad RezaAschner MichaelKhan HaroonRezaei Tavirani MostafaMovafagh Abolfazl - H2A.Z is a conserved histone variant that plays essential roles in various DNA-templated processes. Although both histone H3 acetylation and H2A.Z enrichment levels are important epigenetic marks that regulate gene expression, their functional interplay remains incompletely understood. This study integrates genetic, molecular, and genomic approaches to investigate how GCN5 - a conserved histone acetyltransferase - couples H3 acetylation with H2A.Z dynamics in Arabidopsis, and how this interplay shapes gene expression and plant development. We found that the increase in H2A.Z levels observed in the nrp1-1 nrp2-2 double mutant (defective in NAP1-RELATED PROTEIN 1 and 2) suppresses the morphological and molecular phenotypes of gcn5-7. Conversely, H2A.Z-depleted mutants aggravate these phenotypes of gcn5-7/c1. Notably, the reduction in H3 acetylation caused by GCN5 loss promotes the decrease in H2A.Z level, and this requires the function of NRPs. The integrated analysis of ChIP-Seq and RNA-Seq data revealed that the differential gene expression in the GCN5 deletion mutant is correlated with H2A.Z distribution and enrichment levels. Moreover, H2A.Z overaccumulation at genes in the nrp1-1 nrp2-2 mutant promotes increased H3 acetylation in a GCN5-dependent manner. In conclusion, our findings support a model in which GCN5-mediated H3 acetylation shapes H2A.Z occupancy, linking chromatin dynamics to precise gene expression control and proper plant development. - Source: PubMed
Publication date: 2026/04/26
Su YingpeiHu QinLiu MinQian WeiyeXu ChaoXu JunjieAusin IsraelWang Yafei