KREMEN1 polyclonal antibody (A01)
- Known as:
- KREMEN1 pab (anti-) (A01)
- Catalog number:
- H00083999-A01
- Product Quantity:
- 50 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- KREMEN1 polyclonal antibody (A01)
Related genes to: KREMEN1 polyclonal antibody (A01)
- Gene:
- ABRAXAS2 NIH gene
- Name:
- abraxas 2, BRISC complex subunit
- Previous symbol:
- KIAA0157, FAM175B
- Synonyms:
- Em:AC068896.4, ABRO1
- Chromosome:
- 10q26.13
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-16
- Date modifiied:
- 2017-04-27
- Gene:
- AKR1C3 NIH gene
- Name:
- aldo-keto reductase family 1 member C3
- Previous symbol:
- HSD17B5
- Synonyms:
- KIAA0119, DDX, HAKRB, PGFS
- Chromosome:
- 10p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-29
- Date modifiied:
- 2016-10-05
- Gene:
- ARHGAP4 NIH gene
- Name:
- Rho GTPase activating protein 4
- Previous symbol:
- -
- Synonyms:
- KIAA0131, C1, p115, RhoGAP4, SrGAP4
- Chromosome:
- Xq28
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2015-09-11
- Gene:
- ARHGEF7 NIH gene
- Name:
- Rho guanine nucleotide exchange factor 7
- Previous symbol:
- -
- Synonyms:
- KIAA0142, PIXB, DKFZp761K1021, Nbla10314, DKFZp686C12170, BETA-PIX, COOL1, P85SPR, P85, P85COOL1, P50BP, PAK3, P50
- Chromosome:
- 13q34
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-21
- Date modifiied:
- 2016-10-05
- Gene:
- BCLAF1 NIH gene
- Name:
- BCL2 associated transcription factor 1
- Previous symbol:
- -
- Synonyms:
- KIAA0164, BTF
- Chromosome:
- 6q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-13
- Date modifiied:
- 2017-06-09
Related products to: KREMEN1 polyclonal antibody (A01)
Related articles to: KREMEN1 polyclonal antibody (A01)
- Determining the organization of inputs to subtypes of striatal spiny projection neurons (SPNs) is essential to understand how the striatum integrates information to regulate motor control and decision making. Here, we employed monosynaptic rabies tracing in knock-in mice to map inputs to -positive ( ) SPNs, a subtype enriched in patch (striosome) compartments of the dorsal striatum. Starter cells were broadly distributed along the rostrocaudal axis of the dorsal striatum. Whole-brain analysis revealed that SPNs receive prominent inputs from motor, somatosensory, and prefrontal cortices, as well as from multiple thalamic nuclei. Additional inputs originated from the amygdala, basal ganglia, and midbrain regions, including dopaminergic populations. Quantitative analysis indicated a strong bias toward sensorimotor-related circuits. Together, these results provide a comprehensive whole-brain input map of SPNs and suggest that these neurons are positioned to integrate cortical, thalamic, and neuromodulatory signals within basal ganglia networks to regulate motor function. - Source: PubMed
Publication date: 2026/07/29
Smith Victor M MartinezDong JiePaletzki Ronald FChang LisaWang LupengGerfen Charles RCai Huaibin - Alzheimer's disease (AD) is a complex neurodegenerative disorder characterized by widespread dysregulation of gene expression and regulatory pathways. MicroRNAs (miRNAs) act as key post-transcriptional regulators by modulating messenger RNAs (mRNAs), and their disruption can influence synaptic function, neuroinflammation, and neuronal survival. In this study, we present a transcriptomic-driven framework in which differentially expressed genes (DEGs) are identified from gene expression data and integrated with curated miRNA-target interaction databases to infer putative AD-associated miRNA-mRNA regulatory signatures and potential candidate biomarkers. Transcriptomic and clinical data were obtained from the Alzheimer's Disease Neuroimaging Initiative (ADNI), and the GEO dataset GSE48552 was used as supplementary support to assess the consistency of observed transcriptomic patterns. Using an exploratory differential expression threshold with Welch's t-test and FDR correction, 123 candidate dysregulated genes (34 up-regulated, 89 down-regulated) were identified between AD and cognitively normal controls. To further assess robustness, threshold-sensitivity and cross-method concordance analyses were conducted, supporting the presence of a reproducible core transcriptional signal within the broader discovery-level DEG set. Experimentally validated and predicted miRNA-target interactions were integrated using miRTarBase, yielding 1,669,089 miRNA-gene interactions involving 3,055 unique miRNAs, with strong enrichment toward down-regulated gene targeting. Functional enrichment analysis revealed convergence of miRNA-regulated genes on synaptic signaling, neuronal communication, intracellular transport, apoptosis, oxidative stress, and PI3K-Akt/MAPK-related pathways. A bipartite putative miRNA-mRNA regulatory network (2,207 nodes connected by 11,437 edges, including 2,104 miRNAs and 103 significant genes) was constructed and analyzed using centrality metrics, prioritizing candidate hub genes, including PBX1 and KREMEN1, which were subsequently interpreted in the context of neuronal transcriptional regulation, Wnt-related signalling, synaptic vulnerability, and AD-associated pathway enrichment. Finally, supervised machine learning models trained on selected molecular features showed discriminative performance in the held-out test set, with Random Forest, Gradient Boosting, and LightGBM achieving the highest ROC-AUC values, indicating strong capability in distinguishing AD from control samples. Overall, the framework provides a biologically interpretable strategy for biomarker discovery, prioritizing AD-associated candidate biomarkers and putative regulatory interactions while highlighting targets for future experimental and clinical validation. - Source: PubMed
Publication date: 2026/08/05
Ray AbhishiktaAgarwal KomalJha ShrutikaSingh Abanindra MMajumder ShaliniLodh EkarsiChowdhury Tapan - KREMEN1 (KRM1) serves as a cellular receptor for a major group of enteroviruses causing hand, foot, and mouth disease (HFMD), including CVA2-CVA6, CVA8, CVA10, and CVA12. The viral VP2 residue K140 has recently been identified as completely conserved among these viruses and critical for interaction with KRM1 and viral infection. However, the molecular determinants on the receptor side that govern broad enterovirus recognition remain incompletely understood. Here, we identify KRM1 tryptophan 94 (W94) as an essential residue for KRM1-mediated enterovirus infection. Alanine scanning of 29 KRM1 residues at the CVA10-KRM1 interface revealed that only W94A nearly abolished CVA10 infection. Structural analysis revealed that KRM1 W94 engages in a π-cation interaction with the viral VP2 residue K140, which is critical for receptor binding. Unlike wild-type mice, which succumbed to CVA10 infection, CRISPR-engineered mouse Krm1 W94A mutant mice were fully resistant. Moreover, the W94A mutation conferred universal resistance to all KRM1-dependent enteroviruses (CVA2-CVA6, CVA8, CVA10, and CVA12), both in cell culture and , indicating that the W94 residue is essential for infection by these viruses. Collectively, these findings establish KRM1 W94 as a critical receptor determinant that pairs with the universally conserved VP2 K140 to enable enterovirus infection. This work provides a structural and mechanistic basis for the broad recognition of KRM1-dependent enteroviruses and offers insights that may guide the future development of broad-spectrum antiviral strategies.IMPORTANCEHand, foot, and mouth disease affects millions of children worldwide each year; however, no effective antiviral drugs are available. Many causative viruses, including coxsackievirus A10 and A6, rely on the cellular receptor KREMEN1 to enter human cells. However, which parts of the receptor are critical for viral binding and infection have remained unclear. Here, we identified tryptophan 94 (W94) of KREMEN1 as critical for viral infection. Introducing the W94A mutation abolished viral binding and infection. Structural analysis revealed that W94 interacts directly with a completely conserved residue K140 on the viral capsid protein VP2. Notably, mice carrying this mutation were completely resistant to all KREMEN1-dependent viruses. These findings provide a molecular basis for virus-receptor recognition and highlight a promising target for broad-spectrum therapies against hand, foot, and mouth disease. - Source: PubMed
Publication date: 2026/07/31
Li XiaohongLiu PanLi HongzhengZhu YouweiZhang RuiyiXie XingchenYu RuiZhou FeilongYan JingjingWang MinShu JiayiQiu ChenliZhang ShuoYang ZichenLiu ZhijunZhang XiaoyanXu JianqingZhang ChaoZhang Shuye - Coxsackievirus A10 (CVA10) is a major causative agent of hand, foot and mouth disease and utilizes KREMEN1 (KRM1) as its cellular receptor. While our previous work identifies VP2 residue K140 as a universal anchor for KRM1 binding among KRM1-utilizing enteroviruses, the functional significance of other receptor-interface residues remains poorly characterized. Here, through structure-guided mutagenesis, we demonstrate that VP3-T234, a completely conserved residue at the C-terminus of VP3, is essential for CVA10 infectivity. The T234A mutation does not affect virion assembly but abolishes both KRM1 binding and cellular attachment. Interestingly, this requirement shows remarkable virus specificity: the homologous residue is critical for CVA8, but is not required for other KRM1-utilizing enteroviruses including CVA2-CVA6 and CVA12. The T234A mutation significantly attenuates the pathogenesis of both CVA10 and CVA8 in neonatal mice. Moreover, the CVA8-T234A mutant provides complete protection as an attenuated vaccine against lethal CVA8 challenge. Our findings establish a model wherein KRM1 engagement relies on the conserved VP2-K140 anchor complemented by virus-specific secondary residues, with VP3-T234 representing a key determinant for CVA10 and CVA8. These insights advance our understanding of enterovirus-receptor interactions and provide new directions for vaccine development. - Source: PubMed
Publication date: 2026/07/08
Yan XingyuLiu ZeyuLiu KexinYang ZhenlinWang JianxingZhang Chao - Accurately quantifying protein-protein binding at the single-molecule level is essential for understanding the mechanisms of viral infection and therapeutic targeting. Here, we use solid-state nanopores (SSNs) to detect complex formation between the SARS-CoV-2 Spike receptor-binding domain (Spike RBD) and the alternative host receptors KREMEN1 and Asialoglycoprotein Preceptor 1 (ASGR1). Single-molecule translocation events were analyzed using unsupervised Gaussian mixture modeling and a control-anchored semisupervised classification framework to resolve overlapping free-protein and complex populations. This approach enabled direct identification of receptor-Spike RBD complexes and calculation of apparent dissociation constants under experimental conditions. The inferred affinities were 261.1 nM for ASGR1 and 56.6 nM for KREMEN1, in good agreement with reported literature values and can be used as rough estimates on Spike and its receptor affinities. A negative control using human serum transferrin and Spike RBD showed no emergent high-Δ population, supporting the specificity of the observed interactions. These results establish SSNs as a scalable and quantitative platform for single-molecule affinity measurements. - Source: PubMed
Publication date: 2026/05/17
O'Donohue MatthewThyashan NavodKim Min Jun