Recombinant hemoglobin subunit alpha (HBA) is a synthetically produced globin protein critical for oxygen transport in vertebrates. While native hemoglobin is a tetramer of two α- and two β-subunits, recombinant versions allow controlled production for research and therapeutic applications .
Oxygen Carrier Development: Recombinant HBA serves as a scaffold for engineered hemoglobin-based oxygen carriers (HBOCs) with reduced nitric oxide dioxygenation (NOD) activity .
Mutagenesis Studies: Key residues (e.g., Trp(B10), Gln(E7)) are modified to alter O₂ affinity and stability .
Antibody Validation: Used as a control in western blotting to test specificity of anti-hemoglobin antibodies .
Tetramer Stability: Genetic crosslinking (e.g., rHb0.1) prevents dimer dissociation under physiological conditions .
Post-Translational Modifications: Variants like Thionville retain the initiator methionine, affecting acetylation .
Heme Incorporation: E. coli systems require exogenous heme for functional tetramer assembly .