Thy1 binding protein EMSA Kit
- Known as:
- Thy1 binding protein EMSA Kit
- Catalog number:
- AY1414
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- Thy1 binding protein EMSA Kit
Related genes to: Thy1 binding protein EMSA Kit
- Gene:
- THY1 NIH gene
- Name:
- Thy-1 cell surface antigen
- Previous symbol:
- -
- Synonyms:
- CD90
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2015-07-22
Related products to: Thy1 binding protein EMSA Kit
Related articles to: Thy1 binding protein EMSA Kit
- Mesangial proliferative glomerulonephritis (MsPGN) is a common cause of end-stage renal disease, characterized by mesangial cell proliferation within glomeruli. Mesangial cell activation triggered by inflammation is a key factor in the development of MsPGN. However, effective therapeutic strategies targeting this process are still limited. Here, we uncovered, for the first time, the direct effects of chlorogenic acid (CGA), a naturally occurring small-molecule compound with anti-inflammatory and antiproliferative properties, on mesangial cells in an anti-Thy1 nephritis animal model. A multi-dimensional pharmacological platform integrating laser microdissection-coupled glomerular proteomics affinity deconvolution, surface plasmon resonance, molecular dynamics, and enzyme assays identified Ras-related C3 botulinum toxin substrate 1 (RAC1) as the direct target of CGA. Mechanistically, CGA competitively binds to the LYS15, PRO33, and THR34 amino acid residues-located within residues 57-65 of the GTP/GDP-binding domain of RAC1, inhibiting its activation and subsequently reducing AKT phosphorylation while suppressing Thrombospondin-1 secretion from mesangial cells-a key ligand for macrophage CD36 receptors. This interaction deactivates macrophages and lowers the levels of inflammatory cytokines, including TNF, IL1, and IL6. Significantly, as a novel natural RAC1 inhibitor, CGA disrupts mesangial-macrophage crosstalk by dual suppression of regional immunity and cellular proliferation, thus conferring renal protection in MsPGN models. Our findings highlight CGA as a promising pharmacotherapy, offering a mechanism-driven, natural product-based strategy to mitigate MsPGN progression. - Source: PubMed
Publication date: 2026/06/24
Qu YilunWu LinglingWang YongPeng FeiZhang JiePan DanWang TiantianZhou YenaXia JikaiHe JiayiShi ChunruZhao YinghuaWang XuLiu RanZhang YingjieLiu JiaonaWu JieDuan ShuweiCai GuangyanLi PingHong QuanChen Xiangmei - In multiple sclerosis (MS), mitochondrial dysfunction contributes to disease progression and may impair cognitive function, particularly in vulnerable regions such as the hippocampus. Gadolinium-based contrast agents (GBCAs) are widely used for imaging-based diagnosis of MS; however, evidence indicates that gadolinium (Gd) can be released from low-stability agents and retained in the brain. Whether retained Gd affects neuronal mitochondria, particularly under inflammatory conditions, remains unclear. We investigated hippocampal Gd retention following in vivo GBCA exposure and assessed associated mitochondrial effects in hippocampal slice cultures. - Source: PubMed
Publication date: 2026/09/21
Ludwig RebeccaSchannor MathiasTraub HeikeInfante-Duarte CarmenAnderhalten Lina - Primary endocardial fibroelastosis (pEFE) is characterized by accumulation of elastin-rich extracellular matrix (ECM) in the left ventricular endocardium in the absence of structural defects, but its pathophysiology remains unclear. We investigated dermal fibroblasts from a pEFE patient (proband) harboring a loss-of-function ALMS1 variant. Compared with control fibroblasts, proband cells displayed a myofibroblast-like phenotype, with increased ECM proteins and markers of fibroblast activation and endothelial-to-mesenchymal transition. Conversely, the thymus cell surface antigen (THY1) was downregulated in the proband fibroblasts, which also exhibited reduced ciliation. STED microscopy revealed ALMS1 as a concave, cap-like structure extending into the proximal end of the centriole lumen in control fibroblasts, while it was fragmented in proband fibroblasts and associated with reduced and disorganized Rootletin and C-NAP1 proteins and abnormal centriole separation. Importantly, soluble THY1 reduced production of matrix proteins and markers of fibroblast activation without effects on centriole organization or ciliation. These findings indicate that ALMS1 dysfunction contributes to pEFE pathology through both abnormal proximal centriole organization and THY1-negative fibroblast activation, implicating THY1 as a potential target for pEFE therapy. - Source: PubMed
Publication date: 2026/09/15
Zeigler AngelaColijn SarahGholkar AnkurYang SongKang XuedongZhao YanWolf CharlotteLi SongTorres JorgeNelson StanStratman AmberTouma Marlin - Nociceptive pain responses are mediated by neurons in the dorsal root ganglion. Certain voltage-gated sodium channels, such as Nav 1.8, are necessary for action potential firing and sensing pain. Prior work has demonstrated that interfering with voltage-gated calcium channel activity can also reduce acute and chronic pain. Furthermore, it is reported that dorsal root ganglion calcium response to electric-field stimulation was inhibited by voltage-gated sodium channel blockers. Here we aim to explore the intracellular calcium dynamics in dorsal root ganglion neurons in response to cold pain via intravital confocal imaging. Genetically encoded calcium indicators, such as the GCaMP family of proteins, have been widely used to assess neuron excitability, using fluorescence due to calcium flux as a surrogate for neuron depolarization. We utilized Thy1-GCaMP6f transgenic mice to image calcium transients in live animals or freshly-isolated dorsal root ganglion neurons to identify neuron activity. Measurement of calcium transients demonstrated response to a TRPV1 agonist, capsaicin, or a voltage-gated sodium channel agonist, veratridine, and this response could be inhibited by capsazepine: a TRPV1 antagonist; carbamazepine: a pan-voltage gated sodium channel blocker; or A-803467: a Nav 1.8 inhibitor. We demonstrated through intravital imaging that the cold paw swab increases calcium transients in dorsal root ganglion neurons, and this effect was inhibited by voltage-gated calcium channel blockers. We further demonstrated by in vivo imaging that the cold-pain induced calcium transients in dorsal root ganglion neurons is blocked by A-803467. These data demonstrate that imaging can be used to visualize and measure cold pain signaling in dorsal root ganglion neurons due to L-type voltage-gated calcium channel activity triggered by Nav 1.8 activation. - Source: PubMed
Publication date: 2026/09/18
Dey Moushumi RaniLi BaolinHeddleston JohnAihara Eitaro - : Congenital pulmonary airway malformation (CPAM) is a rare developmental disorder characterized by cystic lung lesions, yet its extracellular matrix (ECM) composition remains poorly understood. This study employed decellularization and data-independent acquisition (DIA) proteomics to compare ECM profiles between cystic (CPAM) and histologically normal non-diseased (ND) regions from the lungs of four patients. : The decellularized scaffolds retained their native architecture with minimal residual DNA (<50 ng/mg). Proteomic analysis revealed 431 differentially expressed proteins (DEPs), with 171 upregulated and 260 downregulated in CPAM. Key findings revealed CPAM-specific enrichment of collagens (COL4A6, COL4A2, COL10A1, COL21A1 and PIIINP), glycoproteins (SPP1, FRAS1, FREM1, FREM2, LTBP1 and FBLN7), ECM regulators (TENM2, ROR2 and OMD), and ECM-affiliated proteins (ANXA7), alongside downregulation of glycoproteins (VASN and ABI3BP), proteoglycans (PODN and MXRA7), ECM regulators (SCARA5, PAPPA, SAA4, CPXM1, CTSC, THY1, SERPINA6/A1/D1, BSG, LYVE1, ITIH4 and CD44), and ECM-affiliated proteins (LGALSL). Pathway analysis highlighted the dysregulation of TGF-β, PI3K-AKT, and mTOR signaling in CPAM and aberrant ECM-cell interactions in pathogenesis. We also evaluated their functional properties and investigated the impact of ECM-based hydrogels on recellularization. : These findings provide a comprehensive proteomic atlas of CPAM ECM alterations, offering insights into disease mechanisms and potential therapeutic targets. - Source: PubMed
Publication date: 2026/08/30
Li YananYang PingYuan MiaoZhu XinglongMao ShengqiangYang YingYao MenglinChen FeiZhou YanyanBao JiXu ChangLi Yi