Recombinant ANO6 protein (His tag)

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Recombinant Human Anoctamin-6 Fragment (residues 744-836) is a high-purity, stable protein fragment derived from the ANO6 gene. This 93-amino acid segment is engineered for structural and biochemical studies, offering researchers a soluble and functional unit to investigate the calcium-activated channel and phospholipid scramblase activities critical in platelet function, bone mineralization, and viral infection mechanisms.

Anoctamin-6 (ANO6), also known as the small-conductance calcium-activated nonselective cation (SCAN) channel or transmembrane protein 16F, is a multi-pass membrane protein localized to the cell membrane in humans. It functions as a key regulator of calcium-dependent phospholipid scrambling, facilitating the surface exposure of phosphatidylserine in platelets to trigger clotting and in osteoblasts for bone mineralization via hydroxyapatite deposition. Additionally, ANO6 can generate outwardly rectifying chloride channel currents in epithelial and immune cells. Notably, it plays a role in SARS-CoV-2 infection, where it is activated by the viral spike protein to enhance calcium signaling and promote syncytia formation. The provided fragment (residues 744-836) represents a computationally selected, stable region ideal for elucidating these complex functional mechanisms in vitro.