Anti-DYRK1A / Dual-specificity tyrosine-phosphorylation-regulated kinase 1A

0.5mg/ml if reconstituted with 0.2ml sterile DI water. DYRK1A Antibody targets dual-specificity tyrosine-phosphorylation-regulated kinase 1A, a serine-threonine protein kinase encoded by the DYRK1A gene. Dual-specificity tyrosine-phosphorylation-regulated kinase 1A is a member of the DYRK family of kinases, which are characterized by their ability to autophosphorylate on tyrosine residues while phosphorylating substrates primarily on serine and threonine residues. DYRK1A plays a central role in cellular signaling pathways that regulate cell cycle progression, transcriptional control, neuronal development, and signal integration in both dividing and post-mitotic cells.Functionally, DYRK1A participates in phosphorylation-dependent regulation of a wide range of substrates involved in transcription, RNA processing, cytoskeletal organization, and cell fate determination. Through these activities, dual-specificity tyrosine-phosphorylation-regulated kinase 1A influences key biological processes including cell proliferation, differentiation, and survival. A DYRK1A Antibody supports studies focused on kinase signaling networks, phosphorylation-dependent regulatory mechanisms, and intracellular signal transduction pathways relevant to development and disease.DYRK1A is broadly expressed across tissues, with particularly important roles in the central nervous system. During development, DYRK1A contributes to neuronal proliferation, differentiation, and synaptic function, while in mature tissues it is involved in maintenance of cellular homeostasis and regulated signaling responses. Subcellular localization of dual-specificity tyrosine-phosphorylation-regulated kinase 1A is predominantly nuclear, although cytoplasmic distribution has also been reported depending on cell type and physiological context. This dynamic localization reflects the ability of DYRK1A to regulate both nuclear transcriptional programs and cytoplasmic signaling events.At the molecular level, DYRK1A contains a conserved kinase domain responsible for catalytic activity, along with regulatory regions that influence substrate recognition, localization, and interaction with binding partners. Autophosphorylation of DYRK1A is required for full catalytic activity and represents a defining feature of the DYRK kinase family. These structural and regulatory characteristics allow dual-specificity tyrosine-phosphorylation-regulated kinase 1A to function as an integrative signaling node that coordinates phosphorylation events across multiple cellular compartments.From a disease relevance perspective, DYRK1A has been extensively investigated in the context of neurodevelopmental disorders, neurodegenerative disease, and cancer. Altered DYRK1A expression or activity has been associated with changes in neuronal development and cognitive function, and the gene is located within the Down syndrome critical region, where gene dosage effects contribute to disease-associated phenotypes. In addition, DYRK1A has been studied for its involvement in cell cycle regulation and oncogenic signaling pathways, highlighting its broader relevance beyond neural systems. These findings underscore the importance of dual-specificity tyrosine-phosphorylation-regulated kinase 1A as a regulator of cellular signaling and developmental processes.DYRK1A Antibody reagents are valuable tools for investigating kinase signaling pathways, phosphorylation-dependent regulatory mechanisms, and disease-associated alterations in DYRK1A expression or localization. Such antibodies support research applications examining intracellular signaling, transcriptional regulation, and developmental biology, with NSJ Bioreagents providing antibodies intended for research use.