Lane 1: human placenta tissue lysate
Lane 2: human brain tissue lysate
Recombinant Rabbit monoclonal primary
Hemoglobin subunit gamma 1and2 Recombinant Rabbit Monoclonal Antibody [JM84-10] (ET1703-46)
Synthetic peptide within human hbg1 / 2 aa 2-45 / 147.
Human placenta tissue lysate, human brain tissue lysate, D3, MCF-7, PC-12, human tonsil tissue, human spleen tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Hemoglobin subunit gamma 1and2
Hemoglobin subunit gamma-1; Gamma-1-globin; Hb F Agamma; Hemoglobin gamma-1 chain; Hemoglobin gamma-A chain; HBG1; PRO2979; Abnormal hemoglobin antibody; FLJ76540 antibody; G gamma globin antibody; Gamma 2 globin antibody; Gamma-2-globin antibody; Hb F Ggamma antibody; HBG 2 antibody; HBG2 antibody; HBG2_HUMAN antibody; Hemoglobin gamma 2 chain antibody; Hemoglobin gamma G antibody; Hemoglobin gamma G chain antibody; Hemoglobin gamma-2 chain antibody; Hemoglobin gamma-G chain antibody; Hemoglobin subunit gamma 2 antibody; Hemoglobin subunit gamma-2 antibody; Methemoglobin antibody; OTTHUMP00000069638 antibody
Belongs to the globin family.
Red blood cells.
Expressed until four or five weeks after birth. Detected at very low levels in adults, where it constitutes about 1% of the total hemoglobin. In contrast, the levels of fetal hemoglobin F (two alpha chains and two gamma chains) are increased in children and adults with beta-thalassemia or sickle-cell disease. In cases of homozygous alpha-thalassemia, homotetrameric hemoglobin Bart's is highly expressed and is the predominant form of hemoglobin after 10 weeks of gestation. Its levels increase steadily after 10 weeks of gestation and until birth (at protein level).
Acetylation of Gly-2 converts Hb F to the minor Hb F1.
Cytosol, hemoglobin complex.
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.