Recombinant Human CD42b protein

CD42b, also known as glycoprotein Ibα (GPIbα), is a critical subunit of the platelet membrane glycoprotein Ib-IX-V (GPIb-IX-V) complex, which plays a pivotal role in platelet adhesion and thrombus formation. This protein is encoded by the *GPIBA* gene and is predominantly expressed on the surface of platelets and megakaryocytes. CD42b interacts with von Willebrand factor (VWF) in the bloodstream, facilitating platelet attachment to damaged vascular endothelium under high shear stress conditions—a key step in primary hemostasis. Structurally, CD42b contains leucine-rich repeats, a ligand-binding domain, and a mucin-like region, enabling its functional versatility.

Recombinant CD42b protein is engineered using heterologous expression systems, such as mammalian cell lines (e.g., CHO or HEK293), to ensure proper post-translational modifications, including glycosylation, which is essential for ligand-binding activity. Researchers often produce soluble forms of CD42b by truncating its transmembrane domain or fusing it with tags (e.g., Fc or His tags) for purification and detection. This recombinant tool is widely utilized to study platelet activation mechanisms, screen anti-thrombotic drugs, and investigate bleeding disorders like Bernard-Soulier syndrome, which is linked to GPIb-IX-V complex defects. Additionally, it serves as an antigen in immunoassays for autoimmune platelet disorder diagnostics. Quality control involves verifying molecular weight, glycosylation patterns, and binding affinity to VWF or monoclonal antibodies. Its role in thrombosis and inflammation also makes it a potential therapeutic target for cardiovascular diseases.