FPRL1 (aa328_339)
- Known as:
- FPRL1 (aa328_339)
- Catalog number:
- Y213505
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- FPRL1 (aa328_339)
Related genes to: FPRL1 (aa328_339)
- Gene:
- FPR2 NIH gene
- Name:
- formyl peptide receptor 2
- Previous symbol:
- FPRL1
- Synonyms:
- LXA4R, HM63, FPRH2, FMLPX, FPR2A, FMLP-R-II, ALXR
- Chromosome:
- 19q13.41
- Locus Type:
- gene with protein product
- Date approved:
- 1991-06-05
- Date modifiied:
- 2016-01-15
Related products to: FPRL1 (aa328_339)
1-2ml Cryovial Storage Box, As1-2ml Cryovial Storage Box, As Polycarbonate, 100 Place1-2ml Cryovial Storage Box, As Polycarbonate, 100 Place1-2ml Cryovial Storage Box, As Polycarbonate, 100 Place100_Place Cryogenic Box w_Li Holds 1.2 _ 2ml Tubes339
4_(Trifluoromethyl)benzohydrazide alpha,alpha,alpha_Triflu4_Amino_N_(3_trifluoromethyl_phenyl)_be 4_Amino_N_(3_trifluorom5430R Centrifuge, Knob w/ 16 x 5ml AT Rotor6_Fluoroindole 6_Fluoroindoleall-trans-Retinoic Acid Methyl Ester C21H30O2 CAS: 339-16-2all-trans-Retinoic Acid Methyl Ester CAS: 339-16-2 Formula: C21H30O2AMMONIUM FERROUS SULPHATE, (Mohra’s Salt), EXTRA PURE, (NH4)2 Fe(SO4)2.6H2O, CAS 7783_85_9AMMONIUM FERROUS SULPHATE, (Mohra’s Salt), EXTRA PURE, (NH4)2 Fe(SO4)2.6H2O, CAS 7783_85_9Anti Human FPRL1 Polyclonal Antibody Related articles to: FPRL1 (aa328_339)
- Neuroinflammation is a key therapeutic target for spinal cord injury (SCI). Apoptotic bodies (ABs) derived from mesenchymal stem cells may modulate early inflammation, promoting SCI repair. Stem cells from human exfoliated deciduous teeth (SHEDs), with neural crest origins, are promising for neurological therapies, but their ABs' role in SCI remains unclear. In this study, as exploratory research, we aimed to investigate the preliminary effects and mechanisms of SHEDs-derived ABs on the treatment of SCI. Herein, SHEDs-derived ABs enhanced functional recovery in SCI mice, improving BMS scores, joint movement, and bioelectrical conduction. Histologically, ABs boosted axonal growth and neuronal regeneration. Moreover, SHEDs-derived ABs significantly suppressed M1 polarization while enhancing M2 polarization in both in vitro and in vivo models. GO/KEGG analyses revealed AB enrichment in immune-related pathways. Mechanistically, the ANXA1/FPR2 axis was critical for ABs-induced microglia/macrophage polarization, with M1 regulation mediated by the NF-κB pathway and M2 modulation driven by the AKT/mTOR pathway. Thus, SHEDs-derived ABs may serve as a clinically translatable strategy for treating SCI by mediating immunomodulation via the ANXA1/FPR2 axis. - Source: PubMed
Publication date: 2026/04/23
Luo LihuaDong NaXu JunpengZhang ChenBao SaXu HaichaoWang XipingDai PengLi CaiyanZhang QiaoYing YiboJiang DaweiLi ShengcunWu PingMei LiqingLi XiaokunDeng JunjiePan YihuaiWang Zhouguang - Oral submucous fibrosis (OSF) is a betel quid chewing-associated precancerous disorder. Studies have shown that the traditional Chinese medicine Jiawei Danxuan Koukang (JDK) exhibits inhibitory effects on OSF, but its specific mechanisms and molecular targets remain unstated. This study aims to elucidate the pharmacological mechanisms of JDK and its component kaempferol in treating OSF. OSF rat model and in vitro cell models were induced by arecoline. Techniques, including hematoxylin-eosin (HE) staining, Masson staining, western blot, quantitative real-time polymerase chain reaction (qRT-PCR), enzyme-linked immunosorbent assay (ELISA), immunofluorescence (IF) staining, co-immunoprecipitation (Co-IP), and molecular docking were used to evaluate the effects of JDK and kaempferol on OSF pathological damage, Annexin-A1 (ANXA1) expression, neutrophil infiltration, collagen deposition, and fibroblast activation. JDK and kaempferol alleviated pathological damage in the oral mucosa tissues of OSF rats, inhibited collagen deposition and fibroblast activation marker expressions, including fibroblast activation protein (FAP), vimentin (VIM), alpha-smooth muscle actin (α-SMA), and matrix metalloproteinase-1 (MMP1), and improved mouth opening function. Further studies revealed that JDK and kaempferol upregulated ANXA1 expression, thereby suppressing neutrophil recruitment, pro-inflammatory cytokine release, and collagen deposition. In vitro experiments confirmed that kaempferol directly bound to ANXA1 in epithelial cells, enhancing its stability, and interacted with FPR2 signaling in fibroblasts to inhibit their activation, thereby restoring epithelial-fibroblast homeostasis. However, knockdown of ANXA1 reversed these protective effects. JDK and kaempferol attenuated OSF by upregulating the ANXA1/FPR2 axis, inhibiting neutrophil infiltration and fibroblast activation, suggesting ANXA1 as a potential therapeutic target for OSF. To our knowledge, this is the first study to demonstrate that JDK/kaempferol exert anti-fibrotic effects in OSF specifically through the ANXA1/FPR2 axis. - Source: PubMed
Publication date: 2026/04/15
Xiao YaoTan YisiLiu YanliChen RuiyiZhou TaoHu ZhaoyongTan Jin - The formyl peptide receptor (FPR), a class A GPCR, plays a pivotal role in the pathogenesis of various diseases, including lung injury. In this study, a phenotype-based Epic® label-free screening was integrated with FPR-mediated calcium flux assays to identify dual antagonists of FPR1 and FPR2 from a compound library. Through comprehensive functional characterization, which included NanoBiT-based assays for G protein dissociation and β-arrestin2 recruitment as well as FlAsH-NanoBRET-based conformation detection, Kobe2602 was identified as a dual antagonist of FPR1 and FPR2. Kobe2602 effectively inhibited multiple FPR-mediated responses, including G protein dissociation, β-arrestin2 recruitment, calcium mobilization, superoxide production, degranulation, cell migration, and receptor internalization. Competition binding and conformational biosensor assays further demonstrated that Kobe2602 directly bound to FPR1 and FPR2 and induced conformational changes in both receptors. In a mouse model of LPS-induced acute lung injury, pathological damage was attenuated by Kobe2602. Our findings suggest that Kobe2602 is a dual FPR1/FPR2 antagonist with therapeutic potential in lung injury. - Source: PubMed
Publication date: 2026/04/15
Wang JunlinZeng HekunXu TengyunLiu YezhouChang YixinLin XingyuNie HongYe Richard D - Understanding host-pathogen interactions at the molecular level requires methods capable of linking spatial context with proteomic information. Here, we present an integrated workflow combining matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) and laser microdissection (LMD)-based liquid chromatography-tandem mass spectrometry (LC-MS/MS) to investigate infection in murine lung tissue. Consecutive formalin-fixed, paraffin-embedded (FFPE) tissue sections were used for spatially resolved MALDI-MSI and subsequent LC-MS/MS analysis of laser-microdissected fungal-infected and non-infected regions. MALDI-MSI revealed reproducible / features specifically associated with infected areas. Corresponding tissue microregions were microdissected and analyzed by proteomics to identify candidate proteins underlying these spatial signals. Comparative proteomics of fungal-infected with non-infected alveolar lung regions via LC-MS/MS identified host proteins involved in leukocyte recruitment, inflammatory signaling, and reactive oxygen species formation, including a 424-fold increase in formyl peptide receptor 2 (Fpr2) during fungal invasion of the lungs. Fungal regions were also enriched in proteins encoded by the gliotoxin biosynthetic gene cluster. Spatial and proteomic data were linked by matching theoretical peptide-adduct masses to MALDI-MSI features, using a semi-quantitative scoring system to prioritize protein assignments. Fungal regions showed contributions from both host and pathogen proteins. This workflow establishes a conceptual basis for spatial proteomics of host-pathogen-interactions in fungal infections and enables association of characteristic signals with plausible protein candidates. - Source: PubMed
Publication date: 2026/03/23
Wolter SaskiaKrüger ThomasPelzel DanielaJacobsen Ilse DBrakhage Axel Avon Eggeling FerdinandKniemeyer Olaf - Neutrophil extracellular traps (NETs) constitute a critical antimicrobial mechanism, yet excessive or dysregulated NET release contributes to endothelial injury and tissue damage. Therefore, identifying physiological and pharmacological regulators of NET formation remains an important goal. Although the role of mitochondrial dynamics in NETs remains incompletely elucidated, accumulating evidence suggests that mitochondria may be underexplored regulators with therapeutic potential. In fact, in certain NET forms, their DNA is of mitochondrial origin. Here, we investigated how exogenous dimethyl fumarate (DMF), an ester of the tricarboxylic acid cycle (TCA) metabolite fumarate, modulates NET formation. Foremost, we observed that DMF markedly suppresses PAD4-dependent NET release by LPS-stimulated neutrophils of wild-type and PAD4-deficient mice. Mechanistic analyses demonstrated that DMF activates the nuclear factor erythroid 2-related factor 2 (Nrf2) pathway and increases the secretion of anti-inflammatory Annexin A1 (ANXA1). Functionally, inhibition of either Nrf2 or the ANXA1 receptor Fpr2 restores NET formation. To integrate these observations with mitochondrial function, we examined markers of mitochondrial dynamics. We found that DMF decreases phosphorylation of dynamin-related protein 1 (DRP1) at Serine 616, a modification typically associated with reduced mitochondrial fission. Consistently, pharmacological inhibition of DRP1 (Mdivi-1) also diminishes NET formation, whereas induction of mitochondrial fragmentation (CCCP) triggers PANoptotic neutrophil death and extracellular DNA release, both of which were prevented by DMF. Collectively, these data identify DMF as a mitochondria-linked immunometabolic regulator that suppresses NET formation through coordinated engagement of Nrf2 and ANXA1 signaling and modulation of mitochondrial dynamics. These findings highlight mitochondrial remodeling as a promising avenue for future exploration and position DMF as a potential pharmacological tool for controlling excessive neutrophil activation. - Source: PubMed
Publication date: 2026/03/31
Burczyk GabrielaKolaczkowska Elzbieta