ADA is expressed in virtually all tissues, with particularly high levels in T-lymphocytes . The enzyme’s activity is vital for the proper functioning of the immune system. ADA deficiency can lead to severe combined immunodeficiency (SCID), a condition characterized by a severely compromised immune system .
Recombinant human ADA (rhADA) is produced using advanced biotechnological methods. The recombinant form is typically expressed in systems such as Spodoptera frugiperda (Sf 21) cells using baculovirus vectors . The recombinant protein is purified to high levels of purity, often exceeding 95%, and is free from endotoxins .
Recombinant ADA is used in various research and clinical applications. It is employed in studies investigating the enzyme’s role in immune regulation and purine metabolism. Additionally, rhADA is used in enzyme replacement therapy for patients with ADA deficiency, providing a crucial treatment option for those suffering from SCID .
The stability of rhADA is maintained by storing it at temperatures ranging from -20°C to -70°C. It is essential to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity . The recombinant protein is supplied in a solution containing Tris, NaCl, and glycerol, ensuring its stability during storage and handling .