Nemo-like kinase (NLK) is a serine/threonine protein kinase belonging to the mitogen-activated protein kinase (MAPK) superfamily. Initially identified in *Drosophila* for its role in photoreceptor development, NLK has since been implicated in diverse cellular processes, including cell cycle regulation, apoptosis, and embryonic development. It interacts with multiple signaling pathways, notably the Wnt/β-catenin, Notch, and TGF-β pathways, often acting as a regulatory modulator. NLK phosphorylates transcription factors like LEF1/TCF and STAT3. influencing their activity and downstream gene expression. Dysregulation of NLK has been linked to cancers, neurodegenerative disorders, and developmental defects, highlighting its dual role as both tumor suppressor and oncogene depending on cellular context.
NLK antibodies are essential tools for studying its expression, localization, and function. These antibodies enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding research into NLK's involvement in disease mechanisms. Commercial NLK antibodies are typically validated for specificity against conserved regions of human, mouse, or rat NLK. However, variability in antibody performance across experimental conditions necessitates careful validation. Recent studies using NLK antibodies have uncovered its role in modulating stem cell differentiation and synaptic plasticity, suggesting therapeutic potential. Ongoing research aims to clarify NLK's complex regulatory networks and its utility as a biomarker or drug target.