Hemoglobin subunit gamma 1and2 Recombinant Rabbit Monoclonal Antibody [JM84-10] (ET1703-46)

UNIPROT #

P69891

PROTEIN NAME

Hemoglobin subunit gamma 1and2

SYNONYMS

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

SEQUENCE SIMILARITIES

Belongs to the globin family.

TISSUE SPECIFICITY

Red blood cells.

DEVELOPMENTAL STAGE

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).

POST-TRANSLATIONAL MODIFICATION

Acetylation of Gly-2 converts Hb F to the minor Hb F1.

SUBCELLULAR LOCATION

Cytosol, hemoglobin complex.

FUNCTION

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.