Rabbit Anti-Human HBG1/HBG2 monoclonal antibody for WB, ICC/IF, IHC. Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The ? and ? globin loci determine the basic hemoglobin structure. The globin portion of hemoglobin consists of two ? chains and two ? chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between ? and ? 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 ?1-?2 cleavage plane. When the two ?1-?2 interfaces are closely bound, hemoglobin has a low affinity for oxygen. Hb A, which contains two ? chains plus two ? chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two ? chains plus two ? chains, and fetal hemoglobin (Hb F), which consists of two ? chains together with two ? chains.
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