CKM, also named as CKMM and M-CK, is a member of the ATP:guanido phosphotransferase protein family. It is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. CKM reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. CK isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. CK MB consists of a dimer of nonidentical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. Inactivation of creatine kinase by gliotoxin was accompanied by the formation of a 37-kDa form of the enzyme.This oxidized form of creatine kinase was rapidly reconverted to the 42-kDa species by the addition of reducing agents concomitant with restoration of activity..
Western Blot: Mouse Heart Tissue, 1:1000-1:10000; IHC: Human Skeletal Muscle Tissue, 1:20-1:200; IF: HepG2 Cells, 1:10-1:100
Type: Primary
Antigen: Creatine Kinase MM-Specific
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Mouse, Rat