Greater than 95% as determined by SDS-PAGE.
Recombinant NUP210 protein is a construct carrying multiple concatenated copies of the short cytoplasmic gp210 C-terminus (which contains the autoreactive epitopes) and having a molecular mass of 27kDa (pH 9.8). NUP210 protein is fused to a hexa-histidine purification tag.
NUP210 is characterized by its large molecular weight of approximately 210 kDa. It spans the nuclear envelope and is involved in the formation of the nuclear pore complex. The protein has a large luminal domain, a single transmembrane segment, and a short cytoplasmic tail. The luminal domain is heavily glycosylated, which is essential for its function and stability.
The primary function of NUP210 is to mediate the transport of macromolecules across the nuclear envelope. It interacts with other nucleoporins and transport receptors to facilitate the selective exchange of proteins and RNA between the nucleus and the cytoplasm. This transport is vital for numerous cellular processes, including gene expression, cell cycle regulation, and signal transduction.
Recombinant NUP210 is a laboratory-produced version of the protein, often used in research to study its structure, function, and interactions. The recombinant form is typically produced using expression systems such as bacteria, yeast, or mammalian cells. These systems allow for the production of large quantities of the protein, which can be purified and used in various experimental assays.
Recombinant NUP210 is particularly useful in studying the autoimmune response in certain diseases. The C-terminal region of NUP210 contains autoreactive epitopes, which are recognized by autoantibodies in conditions such as primary biliary cirrhosis. By using recombinant NUP210, researchers can investigate the mechanisms underlying these autoimmune responses and develop potential therapeutic strategies.
The study of recombinant NUP210 has several important applications in biomedical research: