Recombinant Human LRRC8E Protein

The leucine-rich repeat-containing 8 (LRRC8) family, including LRRC8E, comprises transmembrane proteins that form volume-regulated anion channels (VRACs). These channels regulate cellular processes such as osmotic balance, metabolite transport, and cell signaling. LRRC8 proteins typically function as heteromers, with LRRC8A being an essential subunit for channel activity. LRRC8E, one of the five family members (LRRC8A-E), contributes to the structural and functional diversity of VRACs by forming heterohexameric complexes with LRRC8A. This combinatorial assembly influences ion selectivity, gating, and substrate specificity, enabling tailored responses to cell swelling or shrinkage. Recombinant human LRRC8E protein is produced using heterologous expression systems (e.g., HEK293 or insect cells) for structural and functional studies. It aids in elucidating VRAC architecture, ion transport mechanisms, and roles in pathologies like cancer, stroke, and immune regulation. Research on recombinant LRRC8E also supports drug discovery, as VRACs are therapeutic targets for modulating cell volume-related disorders. The protein’s structure includes a conserved leucine-rich repeat domain and variable N- and C-terminal regions that mediate subunit interactions and regulatory signals. Studies leverage techniques like cryo-EM, electrophysiology, and gene editing to decode its biological and clinical relevance.