General Product Information: CKBB is isolated from human brain, CKMB is isolated from human heart, and CKMM is isolated from human skeletal muscle. All are supplied as a liquid in 5mM Succinate, 10mM Sodium Chloride, 1mM EDTA, 5mM β-mercaptoethanol, 50% Glycerol, ph 7.0 ± 0.1. Protein concentration for CKBB and CKMM is determined by absorbance at A280 using an extinction coefficient of 0.88 (Emg/ml = 0.88). Protein concentration for CKMB is determined by immunoassay. Activity is measured using a CK-NAc enzyme assay. One unit of enzyme converts 1 µmole of creatine phosphate to creatine per minute at pH 7.0 at the specified temperature.
Catalog No. C1124 (Part No. 90030) - CKBB
Purity: ≥ 98% by SDS-PAGE.
Activity: ≥ 200 units/ml at 30°C.
Contaminants: Only CKBB is detected by agarose electrophoresis when stained for creatine kinase activity.
Sample Certificate, MS Word
Catalog No. C1223 (Part No. 90060) - CKMB
Concentration: ≥ 0.5 mg/ml by immunoassay
Activity: ≥ 300 units/ml at 30°C.
Contaminants: Only CKMB is detected by agarose electrophoresis when stained for creatine kinase activity.
Sample Certificate, MS Word
Catalog No. C1224 (Part No. 90059) - CKMB
Concentration: ≥ 0.5 mg/ml by immunoassay
Activity: ≥ 600 units/mg based on assay at 37°C.
Contaminants: ≤ 2% LD by SDS-PAGE.
Only CKMB is detected by agarose electrophoresis when stained for creatine kinase activity.
Sample Certificate, MS Word
Catalog No. C1324 (Part No. 90048) - CKMM
Purity: ≥ 98% by SDS-PAGE.
Activity: ≥ 300 units/ml at 30°C.
Contaminants: Only CKMM is detected by agarose electrophoresis when stained for creatine kinase activity.
Sample Certificate, MS Word
Creatine Kinase (CK) is a dimeric enzyme composed of either M- or B-type subunits. The subunits, each encoded by a unique gene, associate to form three isoenzymic forms: BB, MB, and MM. These isoenzymes are expressed at different levels in various tissues in humans: CKBB is predominantly found in brain tissue, CKMB in heart muscle, and CKMM in skeletal and heart muscle.
CKBB is not normally present in measurable amounts in the serum of normal adults, although it may increase after severe damage to tissues containing CKBB. Elevated serum levels of CKBB are associated with cancer of the breast, ovary, prostate, colon, and other gastrointestinal carcinomas, and for small-cell anaplastic carcinoma of the lung. Serum levels of CKBB are also measured in conjunction with the other isoenzymes, CKMB and CKMM, to aid in the diagnosis of myocardial infarction.
CKMB is known to exist in two forms: CKMB2, the gene product, and CKMB1, which is modified upon release into the bloodstream. Carboxypeptidase cleavage of the C-terminal lysine residue of the M subunit transforms CKMB2 into CKMB1. In healthy individuals, CKMB2 is in equilibrium with the modified CKMB1 subform at a ratio of approximately 1:1. In the early hours of myocardial infarction, the abrupt release of CKMB2 from myocardium produces an upward shift in the serum CKMB2/CKMB1 ratio, usually before total CKMB (CKMB2 + CKMB1) exceeds normal levels. While assays for serum levels of total CKMB have long been used to aid in the diagnosis of myocardial infarction, determinations of the serum CKMB2/CKMB1 ratio are also proving useful.
Although CKMM is predominantly found in skeletal muscle, it is also the primary CK isoenzyme present in heart muscle. In fact, serum levels of CKMM elevate as early as six hours after the onset of myocardial infarction (MI). Serum assays for CKMM are sensitive for the detection of MI, but lack cardiac tissue specificity and, therefore, are used in conjunction with serum assays for the other CK isoenzymes, CKMB and CKBB, to confirm MI diagnosis.
Note: Monoclonal Antibodies are available for CKBB, CKMB, and CKMM
Polyclonal Antibodies are
available for CKMM.