Ask about this productRelated genes to: HECA antibody
- Gene:
- HECA NIH gene
- Name:
- hdc homolog, cell cycle regulator
- Previous symbol:
- -
- Synonyms:
- HDCL, hHDC, HDC, dJ225E12.1
- Chromosome:
- 6q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-10
- Date modifiied:
- 2016-10-05
Related products to: HECA antibody
Related articles to: HECA antibody
- To validate the combined marker Hematoma Maturity Score (HMS) in non-contrast computed tomography (NCCT) scans of patients with spontaneous intracerebral hematomas (ICH) for predicting functional outcomes at discharge, compared to individual radiological signs. - Source: PubMed
Publication date: 2026/03/04
Catelani B TSantos Armentia EHarvey G BRazzini ASobral Viñas PSilva Priegue NLópez Rueda A - Fluorophores with excellent emission often come at the cost of cell permeability, and this long-standing dilemma has limited their effective applications in fluorescence bioimaging to some degree. We report a paradigm-shifting discovery that carbonized polymer dots (CPDs) can function as a versatile, noncovalent translocation platform for a vast spectrum of otherwise impermeable fluorophores. Our investigation began with the serendipitous observation that a new molecule, 1-(2-hydroxyethyl)-5-oxo-1,2,3,5-tetrahydroimidazo[1,2-a]pyridine-7-carboxylic acid (HECA), forms a stable, cell-permeable nanocomplex with carbonized polymer dots (CPDs-280) via noncovalent interactions (loading capacity ∼50.8%). This prompted a systematic exploration, which revealed that CPDs-280 possess a remarkable capacity to override the innate targeting signals of diverse organelle-specific dyes, rerouting them to the cytosol and demonstrating a carrier-dominated localization mechanism. The platform's generality was rigorously proven by delivering custom-designed, membrane-impermeable amphiphilic dyes (ESY-Na and ESY), which remained inert alone but produced intense intracellular luminescence upon noncovalent complexation. This robust, cargo-agnostic delivery capability is rooted in the abundant orthogonal anchor domains on the CPD's surface, enabling multimodal binding without chemical modification. This work unveils a generic strategy to breach biological barriers, instantly unlocking the vast repository of underutilized fluorescent probes for advanced bioimaging and theranostics. - Source: PubMed
Publication date: 2026/01/10
Shan FeishiFu LijuanLiao ChengshuangZhang JingWen MingyueYu Xiao-QiWang ZhouyuYang BaiWang Leyong - With the growing accumulation of scattered single-cell data and the rapid advancement of artificial intelligence (AI), there is a pressing need for a high-quality, well-organized, and AI-ready single-cell data resources to support large-scale model. Here, we present version 2.0 of human Ensemble Cell Atlas (hECA), a cell atlas incorporating both single-cell RNA sequencing (scRNA-seq) and single-cell ATAC sequencing (scATAC-seq) data. It expands the scRNA-seq data collection to 10,831,024 human cells with unified labels, and adds the new modality of scATAC-seq profiles with 1,450,511 cells. The data cover 42 human organs and tissues. To ensure cross-dataset consistency and quality, we standardized gene expression and chromatin accessibility matrices, harmonized cellular metadata, and manually re-annotated cell types based on the unified Hierarchical Annotation Framework (uHAF). The strength of the dataset has been shown in pre-training the large generative cellular AI model scMulan. hECA2.0 provides a well-structured and ready-to-use data resource, serving as a robust data foundation for AI-driven single-cell research. - Source: PubMed
Publication date: 2025/12/15
Xi XiChen YixinWu XinzeHao MinshengLi JiaqiBian HaiyangMeng QiuchenLi FanhongLi ChenXiao ChuxiDong XiaominYou RenkeXiong YifanYang PengGao ZijingCui XuejianPan YanLi ZhenLi WenruiLi ZhuofengChen XiaoyangCui YanfeiLv HairongJiang RuiWei LeiZhang Xuegong - Despite many studies on binding patterns of commercial lectins and other glycan binding proteins, unexpected recognition motifs are still revealed, highlighting the necessity to (re-)investigate these specificities deeply, as they are used for rapid screening of glycosylation patterns or diagnostic histochemistry. The current work is an extension of previous defined glycan microarrays, displaying a library of natural anionic structures not only including N-acetylneuraminic acid but also N-glycolylneuraminic acid as well as sulfated galactose, N-acetylglucosamine or glucuronic acid based on using recombinant glycosyl- and sulfo-transferases. Moreover, anionic modifications on linear tetrasaccharides versus on typical biantennary N-glycan core structures were compared regarding binding pattern and intensities. As in our previous studies, 2-amino-N-(2-amino-ethyl)-benzamide (AEAB)-labeled glycans were probed with various plant lectins, C-type lectins, sialic-acid specific lectins, different antibodies, e.g. anti-NeuGc and recombinant prokaryotic lectins (RPLs). Indeed, expected binding patterns were observed; however, some proteins revealed more narrow specificities. The L2 anti-HNK-1 elicits its specificity for GlcAβ1-3Galβ1-4GlcNAc without the necessity of sulfation also for linear glycans. For anti-Le (clone L5) it is known that sialic acid masking of the epitope is not tolerated, while here we demonstrate that anti-Le antibody (clone T174) can interact with α2,3 Neu5Ac and Neu5Gc capped epitopes. HECA-452 recognizes sialyl Le and sialyl Le, but only with Neu5Ac attached. This anionic glycan array contains most common anionic glycan modifications, can be flexibly modified and reveals commonly-overlooked specificities providing insights into sialic acid-specific interactions, including the often neglected N-glycolylneuraminic acid, thereby applying these findings also to murine or other deuterostome models. - Source: PubMed
Publication date: 2025/11/05
Nuschy LenaWilson Iain B H - Cells have means to adapt to environmental stresses such as temperature fluctuations, toxins, or nutrient availability. Stress responses, being dynamic, extend beyond transcriptional control and encompass post-transcriptional mechanisms allowing for rapid changes in protein synthesis. Previous research has established as a fundamental gene for stress responses and survival of the adult progenitor cells (APCs). However, the molecular role of Headcase has remained elusive. Here, we identify Headcase as a component of ribonucleoprotein (RNP) granules. We also show that, Headcase is required for proper RNP granule formation and remodeling upon stress and is crucial for translation control. Likewise, the human Headcase homolog (HECA) is identified as a component of RNP granules and has similar roles in translational regulation and stress protection. Thus, Headcase proteins define a new family contributing to specific roles among the RNP heterogeneous network. - Source: PubMed
Publication date: 2025/03/28
Ricolo DeliaCasanova JordiGiannios Panagiotis