ARCN1
- Known as:
- ARCN1
- Catalog number:
- 001831A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ARCN1
Related genes to: ARCN1
- Gene:
- ARCN1 NIH gene
- Name:
- archain 1
- Previous symbol:
- COPD
- Synonyms:
- -
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-08-29
- Date modifiied:
- 2014-11-18
Related products to: ARCN1
ARC Gene activity-regulated cytoskeleton-associated proteinArchain,ARCN1,Bos taurus,Bovine,Coatomer subunit delta,COPD,Delta-coat protein,Delta-COPArchain,ARCN1,Chicken,Coatomer subunit delta,COPD,Delta-coat protein,Delta-COP,Gallus gallus,RCJMB04_7j3Archain,ARCN1,Coatomer subunit delta,COPD,Delta-coat protein,Delta-COP,Homo sapiens,HumanArchain,Arcn1,Coatomer subunit delta,Copd,Delta-coat protein,Delta-COP,Mouse,Mus musculusArchain,Arcn1,Coatomer subunit delta,Copd,Delta-coat protein,Delta-COP,Rat,Rattus norvegicusARCN1 293T Cell Transient Overexpression Lysate(Denatured)ARCN1 293T Cell Transient Overexpression Lysate(Denatured)ARCN1 3&_39;UTR Lenti-reporter-Luc VectorARCN1 antibodyARCN1 antibodyARCN1 AntibodyARCN1 Antibody (Center)ARCN1 Antibody (Center)ARCN1 Antibody (Center) Blocking Peptide Related articles to: ARCN1
- Decreased removal and increased production of apolipoprotein B (apoB) containing lipoproteins cause hypercholesterolemia, a major causal risk factor of atherosclerotic cardiovascular disease. By a genome-wide siRNA screen, we previously identified subunits of the Coat protein I (COPI) complex to limit low density lipoprotein (LDL) uptake into Huh-7 hepatocarcinoma cells. This study investigated the underlying mechanism and the role of impaired COPI function for hypercholesterolemia. - Source: PubMed
Publication date: 2026/08/25
Panteloglou GrigoriosRobert JérômeSmit MariekeHuijkman NicoletteKloosterhuis NielsLaw Christopher SWoods BrianOthman AlaaKleber Marcus EDelgado Graciela ETarugi PatriziaLone Museer AWolters Justina ClarindaRimbert AntoineKerksiek AnjaLütjohann DieterRohrer LuciaZanoni PaoloKakava SofiaHäusler StephanieSchlumpf EvelineFutema MartaHumphries Steve EChou JanetMärz WinfriedGeha Raif SShum Anthony KKuivenhoven Jan Albertvan de Sluis Bartvon Eckardstein Arnold - Reverse cholesterol transport by HDLs (high-density lipoproteins) is considered an antiatherogenic metabolic pathway. Hepatocytes are the main contributors to the efficacy of this pathway by the production of apoA-I (apolipoprotein A1) and its lipidation by ABCA1 (ATP-binding cassette transporter A1), selective uptake of cholesterol via SR-BI (scavenger receptor class B type 1), and uptake of entire HDL particles. The molecular determinants of the latter step are not well understood. - Source: PubMed
Publication date: 2026/08/13
Panteloglou GrigoriosZanoni PaoloLaw Christopher SWoods BrianOthman AlaaYalcinkaya MustafaNorrelykke Simon FRzepiela Andrzej JStoma SzymonStebler MichaelKerksiek AnjaVisentin MicheleSmit MariekeWolters Justina ClarindaKakava SofiaPotapenko AntonSchlumpf EvelineRadosavljevic SilvijaHäusler StephanieFutema MartaDalila NawarTybjaerg-Hansen AnneHumphries Steve EKuivenhoven Jan AlbertSluis Bart van deLütjohann DieterMeier RogerRobert JérômeChou JanetGeha Raif SShum Anthony KRohrer Luciavon Eckardstein Arnold - Decreased hepatic removal of low density lipoproteins (LDL) and increased apolipoprotein B (apoB) production cause hypercholesterolemia, a major causal risk factor of atherosclerotic cardiovascular disease (ASCVD). By a genome-wide siRNA screen, we previously identified subunits of the Coat protein I (COPI) complex to limit LDL uptake into Huh-7 hepatocarcinoma cells. - Source: PubMed
Publication date: 2026/06/03
Panteloglou GrigoriosRobert JérômeSmit MariekeHuijkman NicoletteKloosterhuis NielsLaw Christopher SWoods BrianOthman AlaaKleber Marcus EDelgado Graciela ETarugi PatriziaLone Museer AWolters Justina ClarindaRimbert AntoineKerksiek AnjaLütjohann DieterRohrer LuciaZanoni PaoloKakava SofiaHäusler StephanieSchlumpf EvelineFutema MartaHumphries Steve EChou JanetMärz WinfriedGeha Raif SShum Anthony KKuivenhoven Jan Albertvan de Sluis Bartvon Eckardstein Arnold - Microglial dysfunction is a hallmark of Alzheimer's disease (AD), yet the molecular mechanisms driving these impairments remain poorly defined. Genetic studies implicate several AD-associated genes in regulating microglial activity, including SORL1, which encodes the sorting receptor SorLA. Although SorLA is highly expressed in microglia, its functional role in cellular homeostasis has remained unclear. Here, we investigated SorLA function using human brain tissue, primary microglia from rapid autopsies, and CRISPR-engineered human iPSC-derived microglia and neurons. Integrated multi-omics analyses, including single-cell RNA sequencing, lipidomics, and proteomics, together with biochemical and functional assays, revealed that SorLA deficiency induces endoplasmic reticulum (ER) stress and interferon signaling, promotes lipid droplet accumulation, and impairs phagocytic and immune functions. Protein co-complex mapping and structural modeling identified ER-associated proteins co-enriched with SorLA, including SUN2, calnexin (CANX), and multiple COPI complex components (COPA, COPB1, COPG1, ARCN1), implicating SorLA in ER proteostasis and intracellular trafficking. Notably, SORL1 deletion in iPSC-derived neurons recapitulated key phenotypes observed in microglia, including lipid droplet accumulation and SorLA-SUN2 co-immunoprecipitation, indicating that this ER-associated pathway operates across distinct brain cell types. Together, these findings identify an ER-related role for SorLA that extends beyond its established function in endocytic trafficking. Loss of SorLA triggers maladaptive stress responses, perturbs lipid handling, and compromises cellular resilience, thereby contributing to AD-relevant cellular dysfunction. - Source: PubMed
Publication date: 2026/04/06
Haq ImdadulNgo Jason CRoy NainikaLee EmilyChoudhury Muniyat ASoni Rajesh KTeich Andrew FMayeux Richard PDe Jager Philip LHe YeWu XuebingBennett David AOlah MartaSher Falak - Respiratory syncytial virus (RSV), a filamentous, enveloped, negative-sense, single-stranded RNA virus, is a common cause of respiratory infections in pediatric and elderly populations, often leading to severe inflammation and lung damage. To date, there is no effective treatment for RSV infection. Therefore, elucidating the antiviral mechanism in RSV infection is critical for identifying potential effective therapeutic targets. Type I interferons (IFN-Is), especially IFN-β, play a key role in the immediate immune response against viral infection by inhibiting viral load and spread. Current studies have shown that ARCN1 (archain 1), the δ subunit of the coat protein complex I complex, is involved in intra-Golgi trafficking and protein transport from the Golgi apparatus back to the endoplasmic reticulum. In this study, we demonstrate that ARCN1 suppresses the anti-RSV innate immune response by promoting E3 ubiquitin ligase STUB1-mediated K48-linked polyubiquitination and subsequent proteasomal degradation of IKKε. Mechanistically, ARCN1 recognizes and binds to the δL motif of STUB1 via its flexible MHD domain while interacting with IKKε. This finding provides a theoretical basis for the development of new antiviral treatment strategies targeting ARCN1. - Source: PubMed
Publication date: 2025/12/04
Cai JiaminYe YunfeiChen ZhengrongXu FeiLi XiaopingWu MengyunZhou JiShao YuZhu PeijieZhao JingHu JingjingWang YufengLi CanchengTian XiaoyuHuang BeibeiXia TianWang WenjunHao ChuangliYang YiZhang Jinping