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Fetal hemoglobin also known as fetal Hb or HbF is a form of hemoglobin found in fetuses and neonates. HbF is composed of two alpha and two gamma globin chains and its molecular weight is around 64000 Daltons. This hemoglobin variant is mainly expressed in the red blood cells of the fetal liver and bone marrow. Expression of fetal hemoglobin typically declines after birth when beta globin chains replace gamma chains to form adult hemoglobin (HbA). However low levels of fetal hemoglobin can persist into adulthood in some individuals./ Biological function summary Fetal hemoglobin has a higher affinity for oxygen compared to adult hemoglobin. This characteristic allows efficient transfer of oxygen from maternal to fetal circulation which is vital for fetal development. Fetal hemoglobin is not part of any complex but its unique structure is adapted to its function in the fetal environment. The alpha and gamma globin chains together modulate its oxygen-binding properties ensuring proper oxygenation during fetal life./ Pathways The production and transition of fetal hemoglobin are linked to the globin gene switching pathway. This process involves the silencing of gamma globin genes and activation of beta globin genes postnatally a transition integral to producing adult hemoglobin. BCL11A and KLF1 are transcription factors that play essential roles in regulating this gene switching. Both proteins influence the repression of gamma globin genes therefore promoting the expression of beta globin./