Anti-Hemoglobin subunit zeta + Hemoglobin subunit alpha antibody [EP3607] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Hemoglobin subunit zeta (HBZ) and hemoglobin subunit alpha (HBA) are components of the hemoglobin complex primarily known for their role in oxygen transport. HBZ often referred to as embryonic hemoglobin typically predominates in early human development. HBA on the other hand persists throughout life as part of the adult hemoglobin complex. HBA has a molecular mass of approximately 15.1 kDa. Both subunits are highly expressed in erythroid cells within the bone marrow.

Biological function summary

Hemoglobin subunits partake in forming the tetrameric hemoglobin complex essential for efficient oxygen loading and unloading at the tissues. HBZ and HBA interact with other globin chains like beta globin (HBB) to make different forms of hemoglobin. For embryos the functional presence of HBZ is important in facilitating oxygen transport in low-oxygen environments of the fetal placenta. HBA's expression continues postnatally and partners with HBB to achieve the classical hemoglobin A in red blood cells providing important oxygen delivery throughout life.

Pathways

These subunits are integral to the erythropoiesis pathway and the oxygen transport pathway. Hemoglobin biosynthesis is tightly regulated within erythropoiesis controlled by proteins such as erythropoietin and GATA1. The interaction and regulation of globin genes ensure the proper assembly of functional hemoglobin complexes. Additionally these pathways ensure balanced production of globin chains preventing disorders like thalassemia.

Associated diseases and disorders

Abnormalities in HBZ and HBA expression or mutations often link to conditions like thalassemia and sickle cell disease. Thalassemia arises from inadequate production of HBA or HBB causing imbalanced hemoglobin tetramer formation and anemia. In sickle cell disease abnormalities in the HBB chain alter hemoglobin structure affecting how HBA interacts with it. Both disorders highlight the importance of these protein interactions and their maintenance for proper erythrocyte functionality.