Myoglobin Human

Myoglobin is a member of the globin superfamily and is predominantly expressed in skeletal and cardiac muscles. The protein forms a monomeric globular hemoprotein that is primarily responsible for the storage and facilitated transfer of oxygen from the cell membrane to the mitochondria. This protein also plays a role in regulating physiological levels of nitric oxide .

Recombinant human myoglobin is produced using recombinant DNA technology, which involves inserting the human myoglobin gene into a suitable host organism, such as Escherichia coli (E. coli), to produce the protein in large quantities. The recombinant protein is then purified using conventional chromatography techniques .

The recombinant human myoglobin protein typically consists of 160 amino acids and has a predicted molecular mass of approximately 18.01 kDa . It is often formulated in a lyophilized form from a sterile buffer solution containing various protectants to ensure stability during storage and shipping .

Recombinant human myoglobin is widely used in research to study its structure, function, and interactions with other molecules. It serves as a model protein for understanding the mechanisms of oxygen storage and delivery in muscle tissues. Additionally, it is used in various biochemical assays and experiments to investigate its role in regulating nitric oxide levels and its interactions with other proteins involved in cellular respiration .

Mutations or abnormalities in the myoglobin gene can lead to various diseases and conditions. For example, myoglobinopathy is an adult-onset autosomal dominant myopathy characterized by the presence of sarcoplasmic inclusions in muscle cells . Other diseases associated with myoglobin include compartment syndrome and medullomyoblastoma .