Recombinant Human DECTIN1 protein

Dectin-1 (also known as CLEC7A) is a C-type lectin receptor predominantly expressed on immune cells, including dendritic cells, macrophages, and neutrophils. It plays a critical role in recognizing β-glucans, carbohydrate components found in fungal cell walls, thereby serving as a key pattern recognition receptor in antifungal immunity. Structurally, Dectin-1 contains an extracellular carbohydrate-recognition domain (CRD), a transmembrane region, and a cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM)-like signaling domain. Upon ligand binding, Dectin-1 triggers intracellular signaling cascades, often involving Syk kinase, to induce phagocytosis, reactive oxygen species production, and cytokine secretion, which collectively orchestrate innate and adaptive immune responses against fungal pathogens.

Recombinant Dectin-1 proteins are engineered versions of this receptor, typically produced in vitro using mammalian or insect cell expression systems. These proteins often include the extracellular CRD region to preserve ligand-binding functionality, sometimes fused with tags (e.g., Fc or His-tags) for purification or detection. Researchers utilize recombinant Dectin-1 to study receptor-ligand interactions, immune signaling mechanisms, and host-pathogen dynamics. It has also been explored for therapeutic applications, such as enhancing antifungal immunity or modulating inflammatory diseases. Additionally, recombinant Dectin-1 serves as a tool in vaccine development, where β-glucan recognition can be leveraged to boost adjuvant activity. Its role in autoimmune conditions and cancer immunotherapy is under investigation, reflecting its broad relevance in immunology and translational medicine.