HBG2 Human

Hemoglobin Gamma G is composed of two gamma chains and two alpha chains, forming fetal hemoglobin (HbF). This structure is predominant during fetal development and is gradually replaced by adult hemoglobin (HbA) after birth . The gamma chains in HbF are crucial for its high affinity for oxygen, which is essential for efficient oxygen transport from the mother to the fetus.

The gamma globin genes, HBG1 and HBG2, are located on chromosome 11. The HBG2 gene encodes the gamma-G chain, which differs from the gamma-A chain (encoded by HBG1) at residue 136, where glycine is found in the gamma-G product and alanine in the gamma-A product . The gamma-G chain is predominant at birth and plays a significant role in fetal development.

Recombinant Hemoglobin Gamma G is produced using E. coli expression systems. The recombinant protein typically includes an N-terminal His-tag for purification purposes and corresponds to the amino acids 1-147 of the human HBG2 protein . This recombinant form is used extensively in research to study the properties and functions of fetal hemoglobin.

Understanding the regulation and function of Hemoglobin Gamma G is vital for developing therapies for hemoglobinopathies such as sickle cell disease and beta-thalassemia. By studying the molecular events that regulate hemoglobin switching and the potential reactivation of fetal hemoglobin in adult cells, researchers aim to develop new therapeutic approaches .