Hemoglobin subunit alpha Recombinant Antibody / HBA

Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The alpha and beta globin loci determine the basic Hgb structure. The globin portion of Hgb consists of two alpha chains and two beta chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between alpha and beta 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 alpha1-beta2 cleavage plane. When the two alpha1-beta2 interfaces are closely bound, Hgb has a low affinity for oxygen. Hb A, which contains two alpha chains plus two beta chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two alpha chains plus two delta chains, and fetal hemoglobin (Hb F), which consists of two alpha chains together with two gamma chains.