OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
- Known as:
- OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
- Catalog number:
- 001-66
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- Phoenix Peptide
- Gene target:
- OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
Related genes to: OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
- Gene:
- NPFFR1 NIH gene
- Name:
- neuropeptide FF receptor 1
- Previous symbol:
- GPR147
- Synonyms:
- OT7T022, NPFF1R1
- Chromosome:
- 10q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-05-27
- Date modifiied:
- 2016-10-05
Related products to: OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
"Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP ""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP ""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP ""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP ""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP""Recombinant Human Interleukin-18 receptor accessory protein_IL18RAP"α - Calcitonin Gene Related Peptide, α - CGRP, rat'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(2_Furoyl)_PAR_2 (2_6)_Orn amide (mouse, rat) Salt Trifluoroacetate Binding _ Synonym (2_Furoyl)_LIGRLOamide SumFormula C36H63N11O8(2_Furoyl)_PAR_2 (2_6)_Orn amide (mouse, rat) Salt Trifluoroacetate Binding _ Synonym (2_Furoyl)_LIGRLOamide SumFormula C36H63N11O8(Ala1)-PAR-4 (1-6) (mouse)
(Ala1)-Thrombin Receptor-Like 3 (1-6) (mouse), (Ala1)-Proteinase Activated Receptor 4 (1-6) (mouse), (Ala1)-Coagulation Factor II Receptor-Like 3 (1-6) (mouse), AYPGKF 98%(Ala1)-PAR-4 (1-6) amide (mouse)
AYPGKFamide, (Ala1)-Thrombin Receptor-Like 3 (1-6) amide (mouse), (Ala1)-Coagulation Factor II Receptor-Like 3 (1-6) amide (mouse), (Ala1)-Proteinase Activated Recepto Related articles to: OT7T022 (408_432)(Rat)(RFRP Receptor) _ 100ug
- The neuropeptide FF receptor 1 (NPFFR1) belongs to the RF-amide G protein-coupled receptor family. Even though it is a promising therapeutic target for the treatment of chronic pain, this receptor still has not been used as a drug target. A detailed understanding of its ligand binding and activation mechanisms is essential for the rational design of novel modulators. In this study, we developed a non-radioactive, nanoBRET-based ligand binding assay to investigate ligand interactions of neuropeptide FF (NPFF) and neuropeptide VF (NPVF) with the NPFFR1. Fluorescently labeled NPFF and NPVF analogs were synthesized by conjugating a 6-carboxytetramethylrhodamine fluorophore at distinct positions, while a nanoluciferase was fused to the N-terminus of the NPFFR1 to serve as the BRET donor. This approach enables quantitative measurement of ligand binding and provides insights into the relative orientation of the ligand and receptor. Distinct BRET signal profiles for NPFF and NPVF, with a smaller window for NPVF compared to NPFF when directly labeled with the fluorophore, indicate differences in the binding orientation. Furthermore, deletion of the N-terminal residues of the receptor revealed that this region is dispensable for ligand recognition and binding in the NPFFR1. The assay was confirmed for small molecule NPFFR1 ligands, such as hederagenin, offers new opportunities to explore subtype selectivity and will guide drug discovery targeting the RF-amide receptor family. - Source: PubMed
Publication date: 2026/05/20
Lentschat HannahBeck-Sickinger Annette G - Dabry's sturgeon (Acipenser dabryanus) is one of the precious large fish species unique to the upper reaches of the Yangtze River in China. Investigating the molecular mechanisms that regulate the hypothalamic-pituitary-gonadal axis is crucial for the conservation of Dabry's sturgeon. In the present study, transcriptome sequencing and analysis were conducted on hypothalamus, pituitary, and gonad tissues of male and female Dabry's sturgeon. Raw sequence data were compiled and duplicate entries were eliminated, yielding 603,597 unigenes with an average length of 843 base pairs and an N50 value of 1056 bp. In the hypothalamus, the representative up-regulated pathways and genes include fatty acid biosynthesis (fasn, acsl) and fatty acid metabolism (acd), while down-regulated pathways and genes include neuroactive ligand-receptor interactions (lhcgr, npffr1, gabrd). In the pituitary, the representative up-regulated pathways and genes include neuroactive ligand-receptor interactions (drd2, trhr), while down-regulated pathways and genes are unsaturated fatty acid biosynthesis (elovl6). In the gonad, the representative up-regulated pathways and genes include unsaturated fatty acid biosynthesis (fads2), tryptophan metabolism (cyp1a1 and cyp1b1), while down-regulated pathways and genes are ovarian steroid production (fshr, igf1, and cyp11a). These representative pathways and genes play an important role in the gonadal development of Dabry's sturgeon. These potential determinants provide a glimpse into of the molecular mechanisms of hypothalamic-pituitary-gonadal axis regulation in Dabry's sturgeon. CLINICAL TRIAL NUMBER: All fish handling and experimental procedures in this study have been approved by the Chinese Sturgeon Research Institute of China Three Gorges Corporation, and the Hubei Key Laboratory of Three Gorges Project for Conservation of Fishes (Chinese Sturgeon Research Institute of China Three Gorges Corporation). - Source: PubMed
Publication date: 2025/11/08
Shi XuetaoLi YangHuang HongtaoXiao KanYang Jing - Neuropeptide FF receptors 1 and 2 (NPFFR1 and NPFFR2) are RF-amide peptide receptors that couple to G proteins and regulate pain, opioid tolerance, and metabolism. Despite their physiological significance, their ligand selectivity and activation mechanisms remain unclear. Using cryoelectron microscopy, we resolved four NPFFR1 and NPFFR2 structures bound to NPFF or NPVF, revealing conserved C-terminal RF-amide interactions within the orthosteric pocket and N-terminal variations driving subtype specificity. Structural and mutagenesis analyses identified ECL2 and the receptor N terminus as key determinants of NPVF-NPFFR1 and NPFF-NPFFR2 selectivity. Additionally, the structures elucidate the activation mechanism and uncover distinct G-coupling features between NPFFR subtypes. These findings provide molecular insights into peptide recognition and receptor activation within the RF-amide family, offering a structural framework for designing selective NPFFR modulators to treat pain, addiction, and metabolic disorders with enhanced specificity and reduced off-target effects. - Source: PubMed
Publication date: 2025/08/19
Li XinzhuZhang HengHu WenWu KaiLi ShuaiJin SanshanYin YulingYuan QingningXu H EricPan BenxunJiang Yi - Type 2 diabetes (T2D) represents a complex and multifactorial disorder, and efforts to discover its treatment are necessary. Browning of white adipose tissue (WAT) as a therapeutic target for diabetes seems to be induced by exercise through neuropeptide FF (NPFF) signaling in the hypothalamus and adipose tissue. This study aimed to explore the role of endurance training on the browning of WAT by assessing the expression of the gene and protein of NPFF and its receptors in the hypothalamus and adipose tissue. - Source: PubMed
Mousavi Syiedeh MaryamGorji Fatemeh ZahraFallahmohammadi ZiyaNasiri KhadijehAkbari Abolfazl - Neuropeptide FF Receptor 2 (NPFFR2), a G-protein-coupled receptor, plays a role in pain modulation and diet-induced thermogenesis. While NPFFR2 is strongly activated by neuropeptides FF (NPFFs), it shows low activity in response to RF-amide-related peptides (RFRPs), despite the peptides belonging to a shared family. In contrast, NPFFR1, which shares high sequence similarity with NPFFR2, is activated by RFRPs and regulates reproductive hormone balance. The molecular basis for these receptor-specific interactions with their RF-amide peptides remains unclear. Here, we present cryo-electron microscopy structures of NPFFR2 in its active state bound to the agonist RF-amide peptide hNPSF, and in its ligand-free state. Structural analysis reveals that the C-terminal RF-amide moiety engages conserved residues in the transmembrane domain, while the N-terminal segment interacts in a receptor subtype-specific manner. Key selectivity-determining residues in NPFFR2 are also identified. A homology model of NPFFR1 bound to RFRP, supported by mutagenesis studies, further validates this selectivity mechanism. Additionally, structural comparison between the inactive and active states of NPFFR2 suggests a TM3-mediated activation mechanism. These findings provide insights into RF-amide peptide recognition by NPFF receptors. - Source: PubMed
Publication date: 2025/03/24
Kim JeesooHong SooyoungLee HajinLee Hyun SikPark ChaeheeKim JinukIm WonpilChoi Hee-Jung