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C7886
Creatine Phosphokinase from bovine heart
Type III, salt-free, lyophilized powder, ≥30 units/mg protein
Synonym(s):
ATP: Creatine N-Phosphotransferase, CPK, Creatine Kinase, Phosphocreatine phosphokinase
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500 UNITS
CN¥827.01
1000 UNITS
CN¥857.09
3500 UNITS
CN¥2,545.04
17500 UNITS
CN¥10,047.77
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500 UNITS
CN¥827.01
1000 UNITS
CN¥857.09
3500 UNITS
CN¥2,545.04
17500 UNITS
CN¥10,047.77
About This Item
Recommended Products
biological source
bovine heart
Quality Level
description
Contains primarily isozyme MM
type
Type III
form
salt-free, lyophilized powder
specific activity
≥30 units/mg protein
mol wt
80 kDa
storage temp.
−20°C
Related Categories
1 of 4
This Item | C3755 | 2384 | C3921 |
|---|---|---|---|
| specific activity ≥30 units/mg protein | specific activity ≥150 units/mg protein | specific activity ≥300 U/mg, 25 °C, 750 U/mg, 37 °C | specific activity 10-15 units/mg protein |
| biological source bovine heart | biological source - | biological source rabbit skeletal muscle | biological source - |
| form salt-free, lyophilized powder | form salt-free, lyophilized powder | form lyophilized | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C |
| mol wt 80 kDa | mol wt 80-86.2 kDa | mol wt - | mol wt 45 kDa |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
Research area: Cell Signaling
Creatine phosphokinase (CPK) is an intracellular enzyme found predominantly in skeletal muscle, brain, and myocardium.[1] CPK consists of two polypeptide subunits, namely M (muscle type) and B (brain type). The lighter subunit is present in larger amounts.[2] The genes encoding these subunits are on distinct chromosomes, with B on 14q32 and M on 19q13. These subunits facilitate the development of three tissue-specific isoenzymes: CPK-MB (cardiac muscle), CPK-MM (skeletal muscle), and CPK-BB (brain).[3]
Creatine phosphokinase (CPK) is an intracellular enzyme found predominantly in skeletal muscle, brain, and myocardium.[1] CPK consists of two polypeptide subunits, namely M (muscle type) and B (brain type). The lighter subunit is present in larger amounts.[2] The genes encoding these subunits are on distinct chromosomes, with B on 14q32 and M on 19q13. These subunits facilitate the development of three tissue-specific isoenzymes: CPK-MB (cardiac muscle), CPK-MM (skeletal muscle), and CPK-BB (brain).[3]
Application
Creatine Phosphokinase from bovine heart has been used:
- in the reaction mix for the import of in vitro synthesized wild-type FLAG/MYC-tagged LYR Motif Containing 7 (LYRM7-F/M) or the LFK tripeptide replaced with alanine (LFK-AAA) mutant into isolated mitochondria[4]
- in autoubiquitination assay[5]
- in the preparation of premix buffer for adenylyl cyclase activity[6]
- in the preparation of E-mix for in vitro nuclear assembly and isolation[7]
- in in vitro vesicular fusion assay.[8]
- in ATP regeneration system, to facilitate the reactivation of nonmotile axonemes.[9]
- in subcellular in vitro fusion assay of autophagosome with lysosome.[10]
- in in vitro protein translation assay.[11]
- for tATPase assay of myofibrillar protein isolated from rabbit. This assay evaluated the kinetic influence of bound creatine kinase (CK) on Ca2+-activated myosin ATPase.[12]
- for the enzymatic hydrolysis of protein samples during tryptophan estimation by pyrolysis gas chromatography.[13]
Creatine phosphokinase from bovine heart has been used to investigate whether endothelial cell growth is stimulated by ischemic hearts. Creatine phosphokinase from bovine heart has also been used to evaluate the effect of high but nontoxic dietary intake of copper and selenium on metabolism in calves.
Biochem/physiol Actions
Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.[14] The molecular mass of the protein is found to be approximately 80,000 Da. It is made up of 2 subunits, each having a molecular weight of 40,000 ± 2000. The lighter subunit is present in larger amounts.[2]CPK is released from the cellular cytosol into the systemic circulation due to disruption of cell membranes caused by hypoxia or other injuries.[1] Furthermore, it serves as a diagnostic indicator for rhabdomyolysis and acute myocardial infarction (AMI), along with other medical disorders such as acute muscle injury, arrhythmias, and congestive cardiac failure.[3]
Caution
The use of 0.1% albumin in the reaction buffer is recommended to avoid inactivation due to dilution.
Unit Definition
One unit will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 at 30 °C.
Analysis Note
Protein determined by biuret.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Generation of cell-free extracts of Xenopus eggs and demembranated sperm chromatin for the assembly and isolation of in vitro-formed nuclei for western blotting and scanning electron microscopy (SEM)
Allen TD, et al.
Nature Protocols, 2(5), 1173-1173 (2007)
P K Clausen et al.
Journal of forensic sciences, 25(4), 765-778 (1980-10-01)
A pyrolysis-gas-liquid chromatographic method has been developed for the differentiation of adult and fetal bloodstains. In a blind-coded study, five adult and three fetal bloodstains were correctly identified on the basis of the pyrograms of stain extracts. The differentiation between
NRBF2 is a RAB7 effector required for autophagosome maturation and mediates the association of APP-CTFs with active form of RAB7 for degradation
Cai CZ, et al.
Autophagy, 17(5), 1112?1130-1112?1130 (2021)
Creatine Phosphokinase
Aujla RS, et al.
StatPearls [Internet] (2024)
A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants
Gabrielsen M, et al.
Molecular Cell, 68(2), 456-470 (2017)
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