CKM Human

Creatine Kinase exists in three isoenzymes: CK-MM (muscle type), CK-MB (hybrid type), and CK-BB (brain type). The CK-MM isoenzyme is predominantly found in skeletal muscle and heart muscle . The enzyme is a dimer composed of two subunits, which can be either M (muscle) or B (brain) types. The CK-MM isoenzyme is specifically composed of two M subunits .

Recombinant human CK-MM is produced using E. coli expression systems. The recombinant protein typically includes an N-terminal His-tag for purification purposes . The molecular mass of the recombinant CK-MM is approximately 44 kDa .

The primary function of CK-MM is to maintain energy homeostasis in muscle cells. It does so by catalyzing the reversible transfer of a phosphate group from ATP to creatine, forming phosphocreatine. Phosphocreatine serves as a rapidly mobilizable reserve of high-energy phosphates in muscle cells, which can be used to regenerate ATP during periods of high energy demand, such as muscle contraction .

Recombinant human CK-MM is used in various research and diagnostic applications. It is particularly useful in studying muscle physiology, energy metabolism, and neuromuscular diseases. Additionally, CK-MM levels are often measured in clinical settings to diagnose and monitor muscle damage, myocardial infarction, and other conditions .

Recombinant CK-MM is typically supplied as a sterile solution and should be stored at -20°C to -80°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity .