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![Hemoglobin subunit gamma 1and2 Recombinant Rabbit Monoclonal Antibody [JM84-10] — image 1 of 3](https://cdn.genprice.uk/products/992/68dd1c8b061270361ea81612/imageurl/et1703-46.webp)
Product details
Catalog number ET1703-46
DiscontinuedPrice for ET1703-46
Size / count 100 µL
This variant is discontinued and cannot be added to your cart.
Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The α (16p13.3; 5′-ζ-pseudoz-pseudo α2-pseudo α1-α2-α1-?1-3′) and β (11p15.5) globin loci determine the basic hemoglobin structure. The globin portion of hemoglobin 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, hemoglobin 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 δ chains, and fetal hemoglobin (Hb F), which consists of two α chains together with two γ chains.
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