Recombinant Hemoglobin subunit alpha / HBA2 Antibody [HBA/9193R]

Summary

Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The α (16p13.3; 5'-Î �-pseudoÎ �-pseudoα2-pseudoα1-α2-α1- Î �1-3') and β (11p15.5) globin loci determine the basic Hgb structure. The globin portion of Hgb consists of two α chains and two β chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between α and β chains are weaker than between similar globin chains, thereby forming a cleavage plane that is important for oxygen binding and release. High affinity for oxygen occurs upon relaxation of the α1-β2 cleavage plane. When the two α1-β2 interfaces are closely bound, Hgb has a low affinity for oxygen. Hb A, which contains two α chains plus two β chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two α chains plus two d chains, and fetal hemoglobin (Hb F), which consists of two α chains together with two g chains.