ADA Recombinant Rabbit mAb (S-5470)

ADA, full name Adenosine Deaminase, is a widely distributed enzyme in the human body that plays a critical role in maintaining immune system function. Its core function is to catalyze the irreversible hydrolytic deamination of adenosine and 2'-deoxyadenosine, producing inosine and ammonia, thereby playing a key role in purine metabolism and the maintenance of adenosine homeostasis. Structurally, human ADA protein consists of 363 amino acids, with its activity dependent on a zinc ion coordinated with a histidine residue in the active site, adopting a classic α/β barrel fold to ensure its stability and catalytic function. The biological significance of ADA protein becomes particularly evident when it is deficient: mutations in its encoding gene can lead to loss of ADA activity, causing deoxyadenosine and its derivative dATP to accumulate in large amounts in lymphocytes (especially T cells), which are toxic to cells and impair DNA synthesis, ultimately resulting in a severe combined immunodeficiency disease known as ADA-SCID. Without treatment, affected infants are typically at risk of life-threatening severe infections during infancy. Because of its central role in the immune system, ADA has become an important drug target—for example, the inhibitor pentostatin has been approved by the FDA for clinical use, and both enzyme replacement therapy and gene therapy for ADA deficiency represent important practices in modern medicine