Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The (16p13.3, 5-ve OO-pseudove OO-pseudo2-pseudo1-2-1- ve OO1-3) and (11p15.5) globin loci determine the basic Hgb structure. The globin portion of Hgb 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, Hgb 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 d chains, and fetal hemoglobin (Hb F), which consists of two chains together with two g chains.
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
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