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Pyruvate Kinase, from Rabbit Muscle

Cat# TRA-050
Specification 1KU,5KU
Description Glycolysis is the primary pathway for glucose utilization in most organisms. In the final step, pyruvate kinase (PK) catalyzes the irreversible transfer of phosphate from phosphoenolpyruvate to ADP, yielding pyruvate and ATP. PK forms a homotetramer and serves as a key regulator of glycolytic flux and ATP production. Four mammalian isoenzymes exist: M1 (muscle, heart, brain), M2 (kidney, adipose, lung, liver, lymphocytes, intestine), L (liver, kidney), and R (red blood cells). Due to strong M2 overexpression in tumor cells and its release into body fluids, PK holds potential as a tumor marker.
Applications For biochemical reactions and enzyme analysis; for structural studies of the reaction mechanism in the final step of glycolysis; for investigating ATP-dependent phosphorylation of α-substituted carboxylic acids; as a component of the reconstitution buffer for malate dehydrogenase (MDH) assays; Used as a supplement component in detection reagent buffers for phosphoglycerate mutase (PGM) assays; employed in Pseudomonas cells to convert ADP to ATP; utilized in enzymatic assays for ADP, ATP, pyruvate, or PEP when bound to associated enzymes; applied in plant spectrophotometric measurements of ATP hydrolysis; also employed in studies of PK deficiency.
Synonyms Pyruvate kinase from rabbit muscle; ATP: pyruvate 2-O-phosphotransferase;
Form Lyophilized (freeze-dried) powder
Species Rabbit
Source Rabbit muscle
Activity 200 U/mg
Unit Definition One unit is defined as the amount of enzyme that convert 1.0 µmol of phosphoenolpyruvate to pyruvate per minute at pH 7.6 at 37°C.
Molecular Weight 237 kDa (Tetramer)
Purity >95% by SDS-PAGE; no detectable DNase and RNase; Creatine Kinase <2 U/mg; LDH <0.1 U/mg
Gene ID 100008676
Accession P11974
Storage Store at -20°C: Valid for 2 years. Store at 4°C or room temperature for 3 days shows no significant decrease in activity. Store at 37°C for 3 days reduces activity by approximately 10%.
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