Mouse Anti-Human CD49b Antibody (AK-7)

CD49b, also known as integrin alpha-2 subunit or platelet GPIa, is a type I transmembrane glycoprotein whose core function is to non-covalently associate with the integrin beta-1 subunit (CD29) to form the heterodimeric complex VLA-2 (Very Late Antigen-2). Structurally, its extracellular domain contains a unique folded structure homologous to the collagen-binding domain of von Willebrand factor, conferring the molecule with the ability to bind to extracellular matrix components including type I, type II, and type XI collagens as well as laminin. Functionally, CD49b not only serves as the primary collagen receptor in the extracellular matrix, playing a critical role in platelet adhesion, aggregation, and hemostasis, but also deeply participates in immune cell migration and localization. For instance, it is essential for the homing of memory T cell precursors to the bone marrow to establish the resting memory T cell pool, and its expression level can define functionally distinct memory helper T cell subsets. Furthermore, in the tumor microenvironment, the dynamic expression of CD49b on tumor-infiltrating CD8+ T cells is closely associated with T cell dysfunction and spatial distribution. Its differential expression on platelets and various immune cells (including activated T lymphocytes and NK cells) makes it a key molecule in immune regulation and cancer research, as well as a potential therapeutic target.