Myo Human w/o H
Description
Product Specs
Product Science Overview
Myoglobin consists of a single polypeptide chain of 153 amino acids and a heme prosthetic group. The heme group is responsible for the protein’s ability to bind oxygen. Myoglobin’s high affinity for oxygen allows it to effectively store and release oxygen as needed by muscle cells. This property is crucial for maintaining cellular respiration and energy production during physical exertion.
Heme-free myoglobin refers to the protein without its heme group. The removal of the heme group can be achieved through various biochemical techniques, resulting in an apo-myoglobin form. This form is often used in research to study the structural and functional properties of the protein without the influence of the heme group. Heme-free myoglobin can also be reconstituted with synthetic or modified heme groups to investigate the effects of different heme structures on the protein’s function.
Recombinant DNA technology allows for the production of human myoglobin in various host systems, such as bacteria, yeast, or mammalian cells. This recombinant myoglobin is identical to the naturally occurring protein in humans and can be produced in large quantities for research and therapeutic purposes. The recombinant production of myoglobin ensures a consistent and pure supply of the protein, which is essential for detailed biochemical and biophysical studies.
- Structural Studies: Heme-free myoglobin is used to investigate the folding and stability of the protein. By studying the apo form, researchers can gain insights into the role of the heme group in the overall structure and function of myoglobin.
- Oxygen Binding Studies: Recombinant myoglobin, both with and without heme, is used to study oxygen binding kinetics and the effects of various ligands on oxygen affinity. These studies are important for understanding how myoglobin functions under different physiological conditions.
- Therapeutic Potential: Myoglobin and its derivatives have potential therapeutic applications in conditions where oxygen delivery to tissues is compromised, such as in ischemic diseases. Recombinant myoglobin can be engineered to enhance its oxygen-binding properties or to deliver therapeutic agents to specific tissues.
