ARPC2 Antibody
- Known as:
- ARPC2 Antibody
- Catalog number:
- AF1109a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- ARPC2 Antibody
Related genes to: ARPC2 Antibody
- Gene:
- ARPC2 NIH gene
- Name:
- actin related protein 2/3 complex subunit 2
- Previous symbol:
- -
- Synonyms:
- p34-Arc, ARC34
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-06
- Date modifiied:
- 2016-10-05
Related products to: ARPC2 Antibody
Related articles to: ARPC2 Antibody
- Idiopathic pulmonary fibrosis (IPF) is a chronic, progressive lung disease characterized by the pathological accumulation of collagen-rich extracellular matrix, resulting in irreversible lung remodeling and respiratory failure. The incomplete understanding of IPF pathogenesis has hindered the development of effective therapeutics. Here, we investigate the mechanism by which the actin-related protein 2/3 complex subunit 2 (ARPC2) contributes to the fibrotic response in lung fibroblasts. Modulating of ARPC2 expression levels altered the expression of profibrotic genes, including α-smooth muscle actin (), in TGF-β1-treated MRC-5 cells at the transcriptional level. We further show that ARPC2 regulates the TGF-β1-mediated nuclear translocation of myocardin-related transcription factor-A (MRTFA), a central driver of fibrotic gene induction. Our data indicate that ARPC2 plays a distinct role in profibrotic gene expression and MRTFA nuclear localization, distinguishing its function from other components of the actin-related protein 2/3 (ARP2/3) complex. Furthermore, ARPC2 appears to modulate the TGF-β1-dependent formation of MRTFA/G-actin complexes. Finally, transcriptomic analysis of cells depleted of ARPC2, ACTR2, or MRTFA revealed that ARPC2 and MRTFA co-regulate a specific repertoire of fibrotic genes. These observations support a profibrotic function for ARPC2 during fibroblast-to-myofibroblast transition (FMT), highlighting it as a potential therapeutic target for IPF. - Source: PubMed
Publication date: 2026/03/17
Du Eun JoKim HyunseongBae Seo-GyeongAn SihyeonRyoo Kanghyun - invasion of host respiratory epithelial cells is a critical mechanism driving acute exacerbations of chronic obstructive pulmonary disease (AECOPD). Although previous studies have extensively demonstrated that dynamic changes in the actin cytoskeleton are central to the invasion of host cells by , the detailed mechanisms underlying the specific upstream signaling pathways and key regulators driving this process remain incompletely understood. Our study identifies and validates the essential roles of key Rho GTPase regulators (CDC42, Rac1, ArpC2, ArpC4) in actin polymerization during infection, thereby elucidating a more comprehensive and specific molecular mechanism. Invasion assays and Transmission electron microscopy (TEM) showed that the Rho GTPase signaling pathway modulates bacterial load in A549 cells by regulating macropinosome volume. Further experiments used strains 73-OR and ATCC 25238 to invade wild-type A549 cells, CDC42 A549 cells, Rac1 A549 cells, ArpC2 A549 cells and ArpC4A549 cells respectively. Invasion assays and TEM were performed to quantify internalized bacteria, macropinosome volume changes, and bacterial distribution; Western blot analyses and cellular immunofluorescence were used to measure F-actin/G-actin ratios and microfilament fluorescence intensity. These results indicate that Rho GTPase signaling pathway modulates invasion by regulating actin polymerization dynamics. Specifically, CDC42 and Rac1 are essential for actin polymerization and bacterial internalization. ArpC4 contributes to actin remodeling without influencing invasion, while ArpC2 is uninvolved in both processes. These findings provide a theoretical basis for targeting innate immunity to prevent and treat -induced AECOPD. - Source: PubMed
Publication date: 2026/02/17
Ma RuiruiCheng GuixueWu YunChen JiaweiLu RongqiLiu Yali - Major depressive disorder (MDD) is a heterogeneous condition with substantial variability in antidepressant treatment response. Identifying predictive biomarkers could facilitate personalized treatment strategies and improve clinical outcomes. - Source: PubMed
Publication date: 2026/02/17
Kang JunhoKong NayeongKim ShinLee Hojun - De novo mutations in the syntaxin-binding protein 1 (STXBP1), encoded by STXBP1, are among the most prevalent causes of variable neurodevelopmental disorders, including epileptic encephalopathy, developmental delay, and movement disorders. Although STXBP1 has been proposed as a critical presynaptic protein controlling synaptic vesicle exocytosis, clinical phenotypes also suggest that its biological function could be more diverse. - Source: PubMed
Publication date: 2026/01/09
Yang TaoBanerjee RajatDeng YameiJahagirdar SheetalKim Joo HyunChen WuXue MingshanNesvizhskii Alexey IUhler Michael DParent Jack MWang Yu - RNA sequences with the potential to form G-quadruplexes (rGQs) are widespread but largely unfolded in cells by unknown mechanisms. rGQ folding status is a critical regulator of RNA splicing and translation. We show that rGQs can be unfolded by SR proteins, SR-related proteins, and other Arg-rich proteins, including SRSF1, SRSF3, SRSF9, U1-70K, and U2AF1. The length and composition of Arg-rich regions are key determinants of this activity: Arg residues are the primary drivers, while acidic residues attenuate the unfolding activity. To unfold ARPC2 rGQ, at least 13 Arg residues are required. Our findings identify Arg-rich proteins as previously unrecognized, helicase-independent regulators of rGQ structures, with potential broad impacts on RNA processing that merit further investigation. - Source: PubMed
Publication date: 2026/01/09
De Silva Naiduwadura Ivon UpekalaKunwar PuspaRifat Rahman Md IbnulKwao Joanna KoryoLehman NathanZhang ZihanPaul TrentonCheng ClaireTruex NicholasLee Hui-TingZhang Jun