Recombinant Human ITGa9 protein

ITGa9. also known as integrin alpha-9. is a cell surface receptor subunit that pairs with the β1 subunit to form the α9β1 integrin heterodimer. As a member of the integrin family, it plays critical roles in mediating cell-cell and cell-extracellular matrix (ECM) interactions, influencing cellular adhesion, migration, and signaling. ITGa9 is distinguished by its unique ligand-binding specificity, interacting with proteins such as vascular cell adhesion molecule-1 (VCAM-1), tenascin-C, and osteopontin. These interactions are essential in various physiological processes, including lymphangiogenesis, immune cell trafficking, and tissue repair.

The α9 subunit contains a large extracellular domain responsible for ligand recognition, a transmembrane region, and a short cytoplasmic tail that facilitates intracellular signaling. Its expression is observed in multiple tissues, particularly in endothelial cells, smooth muscle cells, and specific immune cells. Dysregulation of ITGa9 has been implicated in pathological conditions such as chronic inflammation, fibrosis, and cancer metastasis. For instance, elevated ITGa9 levels correlate with tumor progression by promoting angiogenesis and cancer cell invasion.

Recombinant ITGa9 protein is engineered to study its structural and functional properties, often produced in mammalian or insect cell systems to ensure proper post-translational modifications (e.g., glycosylation). This protein serves as a tool for elucidating binding mechanisms, screening therapeutic inhibitors, or developing diagnostic assays. Researchers also utilize it to investigate ITGa9’s role in disease pathways, offering insights for targeted therapies. Current studies explore blocking α9β1 integrin to mitigate pathological processes, highlighting its potential as a therapeutic target. Overall, ITGa9 recombinant protein remains pivotal in advancing both basic and translational research in immunology and oncology.