KREMEN1 Antibody
- Known as:
- KREMEN1 Antibody
- Catalog number:
- GWB-MP974B
- Product Quantity:
- 50ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- KREMEN1 Antibody
Related genes to: KREMEN1 Antibody
- Gene:
- KREMEN1 NIH gene
- Name:
- kringle containing transmembrane protein 1
- Previous symbol:
- KREMEN
- Synonyms:
- KRM1
- Chromosome:
- 22q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-22
- Date modifiied:
- 2016-04-25
Related products to: KREMEN1 Antibody
Related articles to: KREMEN1 Antibody
- 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 - Early-onset asthma (EOA) significantly increases the risk of chronic obstructive pulmonary disease (COPD), yet the causal mechanisms and molecular mediators underlying this progression remain poorly understood. Multi-omics integration provides a powerful framework for prioritizing potential mediating proteins and disease-specific therapeutic candidates. - Source: PubMed
Jiang YuhanGuo JuWang YifanGuo RunWei YongjianLi TianchunWang XuelinXia RuiwenLi WanyiZou YingxueYang Hongxi - Coxsackievirus A6 (CVA6) is a major pathogen of hand, foot, and mouth disease, yet the viral determinants of its severe pathogenicity remain undefined, hampering intervention strategies. Here, by comparing a highly lethal clinical isolate (CVA6-HeB) with an attenuated strain (CVA6-TW141), we identified the capsid-encoding P1 region as the primary virulence determinant in neonatal mice. Fine-mapping identified a single critical residue at position 238 of VP3 (VP3-238): glutamic acid (E) in virulent CVA6-HeB versus alanine (A) in attenuated CVA6-TW141. Introducing E238 into the attenuated CVA6-TW141 was sufficient to confer lethality, and conversely, reverting it to alanine in the lethal CVA6-HeB completely abolished virulence, demonstrating that VP3-E238 is necessary and sufficient for lethal disease. E238 is dominant (>93%) in circulating CVA6 strains, suggesting a significant fitness advantage. This residue is situated at the edge of the canyon, a key receptor-binding site. Replacing E238 with alanine (E238A) did not affect virion assembly or growth in cultured cells. However, this mutation drastically reduced binding to the essential murine entry receptor KREMEN1 and attenuated virulence by over 10,000-fold in mice, correlating with significantly lower tissue viral loads and pathology. Based on this mechanism, we rationally designed a live-attenuated vaccine candidate by introducing the attenuating E238A mutation. Immunization with this candidate provided complete protection against a subsequent lethal challenge with a heterologous CVA6 strain. Our study defines VP3-E238 as a key molecular switch for CVA6 pathogenicity and establishes a foundation for rational vaccine development. - Source: PubMed
Publication date: 2026/04/27
Liu KexinLiu ZeyuYan XingyuYang ZhenlinLi XueZhang Chao - Among dependence receptors (DRs), which induce apoptosis when unbound by their cognate ligands, Kremen1 was initially reported to drive cancer cell death in the absence of DKK1. However, the precise mechanism of Kremen1-induced cell death remains unclear. In this study, we demonstrate that Kremen1 induces cell death with autophagic features, contrasting with the apoptotic process typically associated with DRs. Functional experiments using pharmacological inhibition of autophagy or genetic silencing of key autophagy effectors, confirmed this cell death process. Protein–protein proximity assays through biotin labeling identified SEC24C, a component of the COP-II complex, as a critical effector of this process. Moreover, the proximity between Kremen1, SEC24C and ATG9A after vesicular trafficking, fosters the proximity of SEC24C with ATG8, ERGIC and ATG9A, likely increasing the number of autophagosomes and vesicles leading to cell death. Given that the Kremen1/DKK1 pair is frequently altered in cancers, its aberrant induction should be monitored and may be targeted to offer an alternative strategy to treat cancers resistant to current therapies. - Source: PubMed
Publication date: 2026/03/11
Brahim SoniaSchott ThomasGhasemi-Firouzabadi ShivaNegulescu AnaGeneste ClaraErrazuriz-Cerda ElisabethIchim GabrielMehlen PatrickMeurette Olivier - Reactive oxygen species (ROS) are critically implicated in ischemic stroke (IS), yet the transcriptional networks and predictive biomarkers underlying ROS dysregulation remain incompletely understood. - Source: PubMed
Publication date: 2026/03/10
Yang LifangLiang TianyuDing Xiaodi