CKMBITII Human

Creatine Kinase (CK) is a crucial enzyme involved in energy homeostasis, facilitating the reversible transfer of phosphate between ATP and various phosphogens such as creatine phosphate . CK exists in multiple isoforms, including CK-MM (muscle), CK-BB (brain), and CK-MB (myocardial). The CK-MB isoenzyme is particularly significant as a biomarker for myocardial injury, such as in the case of a heart attack .

CK-MB is a dimeric protein composed of two subunits: M (muscle) and B (brain). The Type-II isoenzyme possesses the naturally occurring carboxy-terminal amino acid lysine, which is cleaved in the bloodstream during a myocardial infarction, creating CK-MB Type-I . This structural change is crucial for its role as a biomarker.

Recombinant human CK-MB Type-II is produced using various expression systems, including Escherichia coli and Pichia pastoris . The recombinant form is engineered to be identical to the native enzyme, ensuring its functionality and stability. The production process involves tandem affinity purification (TAP) to isolate the CK-MB isoenzyme from other isoforms .

Recombinant CK-MB Type-II is widely used in clinical laboratories as a standard or reference material for measuring CK-MB activity or mass. Its high purity and stability make it an ideal candidate for diagnostic applications, particularly in the context of myocardial injury . The enzyme’s activity is defined by its ability to catalyze the transphosphorylation of phosphate from creatine phosphate to ADP, a critical reaction in energy metabolism .