Data from commercial and research sources highlight the following properties:
CKM Human, Native serves as a biomarker for cardiac damage:
Serum Levels: Elevated MM-CK in serum correlates with myocardial infarction (MI). A study of healthy donors showed mean serum CKM levels of 115.3 U/L (range: 54.3–268.9 U/L) .
Diagnostic Sensitivity: MB-CK heterodimer (M and B subunits) is a more specific MI marker, but MM-CK remains critical for baseline calibration in clinical assays .
Cardiac Tissue: MM-CK constitutes ~80% of total creatine kinase activity, essential for ATP regeneration during muscle contraction .
Skeletal Muscle: Higher baseline expression compared to cardiac tissue, with variability observed across ethnic populations in genomic studies .
CKM Human, Native is utilized in:
Diagnostic Calibration: Standardizing assays for MI detection .
Therapeutic Studies: Investigating circadian effects on infarct size and cardiac medical therapies .
Population Genomics: The Mexican Biobank project identified ancestral variations in energy metabolism genes, including CKM, influencing disease susceptibility .
Genetic Diversity: Genome-wide association studies (GWAS) in diverse cohorts (e.g., Mexican Biobank) reveal CKM variants linked to metabolic traits .
Pangenome Reference: The Human Pangenome Reference Consortium includes CKM in its draft, improving SV detection by 104% compared to GRCh38 .
Commercial preparations meet stringent criteria:
Human Creatine Kinase M-Type is a protein naturally found in the heart muscle of humans.
Lyophilized Powder
The Creatine Kinase M-Type protein was lyophilized in a buffer solution containing 40mM Tris-HCL, 1mM EDTA at a pH of 7.5, and 10mM n-Acetyl cysteine.
Lyophilized CKMM remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C for extended periods. After reconstitution, CKMM should be stored at 4°C for a maximum of 2-7 days. For long-term storage, freezing below -18°C is advised. It is highly recommended to add a carrier protein like HSA or BSA (0.1%) for long-term storage and avoid repeated freeze-thaw cycles.
To reconstitute the lyophilized CKMM, it is recommended to dissolve it in sterile distilled water at a concentration of at least 100µg/ml. The reconstituted solution can be further diluted in other aqueous solutions as needed.
The biological activity of this Creatine Kinase M-Type is measured in units (U). One unit is defined as the amount of enzyme required to transfer 1 µmole of phosphate from Creatine Phosphate to ATP per minute at a temperature of 37 degrees Celsius. This activity is determined by measuring the production of NADH at 340nm in a coupled reaction. The specific activity of this product is greater than 100U/mg.
The purity of this product is determined to be greater than 10.0% based on SDS-PAGE analysis.
Human Cardiac Tissue.
Creatine kinase is an enzyme that catalyzes the conversion of creatine and adenosine triphosphate (ATP) to phosphocreatine and adenosine diphosphate (ADP). This reaction is vital for the storage and release of energy in muscle cells. Phosphocreatine serves as a rapidly mobilizable reserve of high-energy phosphates in skeletal muscle and the brain, which can be used to regenerate ATP during periods of high energy demand, such as intense physical activity .
Elevated levels of CK-MM in the blood can indicate muscle damage or disease. This can occur due to various reasons, including:
A creatine kinase test measures the amount of CK in the blood. Elevated CK levels can indicate muscle, heart, or brain damage. However, it is important to note that elevated CK levels do not specify the exact cause or location of the damage. Therefore, additional tests are often required to pinpoint the underlying issue .
The normal range for CK levels can vary based on several factors, including age, gender, and ethnicity. Generally, men tend to have higher CK levels than women due to greater muscle mass. For example, the upper normal limit for men can range from 200 to 395 U/L, while for women, it is up to 207 U/L .