Rabbit Anti-Human HBG1/2 monoclonal antibody for IF, ICC, IHC, WB. Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The ? (16p13.3; 5?- ? -pseudoz-pseudo ? 2-pseudo ? 1-? 2-? 1-œ1-3?) and ? (11p15.5) 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,
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