Myoglobin (MYO)

Myoglobin (MYO) is a small molecule pigmented protein, formed by the combination of bead protein and n-iron hemoglobin (Heme), which can be reversibly bound to oxygen to form MbO2, MbO2 is called oxygenated myoglobin, and Mb is called deoxymyoglobin. MbO2 is called oxygenated myoglobin and Mb is called deoxygenated myoglobin. It has the role of transporting and storing oxygen in myocytes. It diffuses out of the myocytes into the circulation when the myocardium is damaged. Myoglobin is found only in cardiac and skeletal muscle and is not found in other tissues, including smooth muscle. Myoglobin is responsible for the red coloration of muscle in most vertebrates. Myoglobin accounts for about 2% of total muscle protein. The low molecular weight of myoglobin gives it early release properties and makes it an early biomarker of myocardial ischemia (MI), and it was the first non-enzymatic protein used in the diagnosis of myocardial infarction. It is significantly more sensitive than CK or CK-MB activity. Myoglobin is now recognized as an early and optimal indicator for the determination of acute myocardial infarction, and in combination with cTn or CK-MB, it helps to rule out the diagnosis of acute myocardial infarction at an early stage.

KMD Bioscience, as an in vitro diagnostic raw material supplier, has been committed to the rapid development and large-scale production of in vitro diagnostic proteins and antibodies. KMD Bioscience can provide customers with antibodies that undergo rigorous testing to ensure their purity and sensitivity for use in a variety of different diagnostic platforms, such as LFIA, ELISA, CLIA, POCT, and more.

The inventory of reagents associated with MYO (Myoglobin) that KMD Bioscience can offer:

MYO Protein Characteristics:

MYO is an important intracellular pigment protein present in mammalian cells and is a member of the globin superfamily, which also includes hemoglobin. In structure and function. Hemoglobin has four polypeptide chains and four oxygen-binding sites. Myoglobin, on the other hand, has only one polypeptide chain and one oxygen-binding site, which results in the two proteins having different kinetics of oxygen binding. Structural features of MYO proteins: (1) Single-subunit, compact shape. (2) Rich in α-helices, its spatial structure is a compact globular protein composed of eight α-helices. (3) The amino acid residues on the inner and outer surfaces of the molecule are strictly limited. There are both hydrophilic and hydrophobic amino acid residues on the outer surface of the molecule, but the inner part of the molecule is mostly hydrophobic amino acid residues or the hydrophobic part of polar amino acid residues. In addition, myoglobin molecules have two His which are in the active site of the protein and form an oxygen binding site together with the heme cofactor. (4) There is a cleft on the surface of the molecule containing the heme cofactor. The hydrophobic propionate side chain of heme is flung on the surface of the molecule and is ionized at physiological pH; the rest of heme is embedded in the interior of the molecule, surrounded by hydrophobic residues of the polypeptide chain, and is near only 2 His. The amino acid residues in contact with heme come from different parts of the multichain primary structure, and they come close to each other when the polypeptide chain is folded, forming the heme binding site.

Figure 1 Schematic diagram of the molecular structure of MYO

Biological functions of MYO

Myoglobin is a low molecular weight serum protein and is the earliest biomarker of acute myocardial infarction. Serum myoglobin concentrations are elevated after myocardial infarction however, the presence of myoglobin in skeletal muscle limits its diagnostic specificity as baseline concentrations of circulating myoglobin are relatively high and elevated after skeletal muscle injury. Myoglobin concentrations are also elevated in patients with renal failure. Therefore, MYO has high sensitivity but low specificity, and it is usually necessary to combine it with other cardiac markers, such as cardiac troponin (cTnI), creatine kinase isoenzyme (CK-MB), etc., to better avoid omission and misdiagnosis caused by myoglobin testing alone.

MB is the gene that encodes human myoglobin. It encodes a single polypeptide chain with an oxygen-binding site that reversibly binds oxygen through heme residues and can bind and release oxygen depending on the oxygen concentration in the cell. Thus, its primary function is to provide oxygen to myocytes. Myoglobin also functions as a nitric oxide hemostat. In addition, it plays a role in the detoxification of reactive oxygen species. Its ability to bind oxygen is intermediate between that of hemoglobin and cytochrome oxidase.

KMD Bioscience currently has more than 700 types of antigen and antibody products, and the number of products accumulated over the past ten years can be said to be the product of a rigorous selection. In vitro diagnostics involves a wide range of diseases, including thrombosis, tumors, cardiovascular, metabolism, inflammation, and so on. As a supplier of antigen and antibody raw materials, we can only develop high-quality raw materials for use in disease diagnosis by conducting long-term and dedicated research on the disease and disease markers. KMD Bioscience's antibody diagnostic raw materials and antigen diagnostic raw materials are strictly monitored during the R&D and production phases, and the performance indexes (specificity, activity, stability, etc.) of antibodies/antigens are analyzed to ensure that IVD raw materials are characterized by small batch-to-batch/intra-batch variations, wide linear ranges, good stability, high sensitivity, and so on.