Hemoglobin subunit alpha
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.
Human, Mouse, Rat
Recombinant Rabbit Monoclonal Antibody
Human lung tissue, human spleen tissue, mouse embryo tissue.
Alpha 1 globin antibody
Alpha globin antibody
Alpha one globin antibody
Hemoglobin alpha 1 antibody
Hemoglobin alpha 1 chain antibody
Hemoglobin alpha 1 globin chain antibody
Hemoglobin alpha 2 antibody
Hemoglobin alpha chain antibody
Hemoglobin subunit alpha antibody
Store at +4℃ after thawing. Aliquot store at -20℃ or -80℃. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
ProA affinity purified
Cytosol, membrane, extracellular region
Fig1: Immunohistochemical analysis of paraffin-embedded human lung tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.
Fig2: Immunohistochemical analysis of paraffin-embedded human spleen tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.
Fig3: Immunohistochemical analysis of paraffin-embedded mouse embryo tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.
1. Banerjee S et al. Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions. Free Radic Biol Med 53:1317-26 (2012).
2. Shephard F et al. A mitochondrial location for haemoglobinsdynamic distribution in ageing and Parkinson's disease. Mitochondrion 14:64-72 (2014).
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