Pyruvate kinase (PK) is a crucial enzyme in the glycolytic pathway, responsible for catalyzing the conversion of phosphoenolpyruvate (PEP) to pyruvate, with the concomitant generation of ATP. This enzyme plays a vital role in cellular metabolism and energy production. The liver and red blood cell (RBC) isoforms of pyruvate kinase are encoded by the PKLR gene, which undergoes alternative splicing to produce the L (liver) and R (RBC) isoenzymes .
The primary function of pyruvate kinase is to facilitate the final step of glycolysis, which is essential for ATP production. In red blood cells, pyruvate kinase activity is critical for maintaining cellular energy levels and membrane integrity. Deficient or abnormal PK activity can lead to inadequate ATP production, resulting in cellular dehydration, loss of membrane plasticity, and premature destruction of RBCs in the spleen or liver .
Pyruvate kinase deficiency is a genetic disorder that affects the enzyme’s activity, leading to hemolytic anemia. This condition is characterized by the premature destruction of RBCs, causing symptoms such as fatigue, jaundice, and an enlarged spleen. Management of pyruvate kinase deficiency involves supportive care, including blood transfusions and splenectomy in severe cases .
The mouse anti-human pyruvate kinase, liver and RBC antibody, is a monoclonal antibody derived from the hybridization of mouse myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PKLR. This antibody is used in various applications, including ELISA and Western blot analysis, to detect and study the PKLR protein .
The PKLR antibody is recommended for use in research settings to study the expression and function of pyruvate kinase in human cells. It is typically stored at -20°C for long-term use and at 4°C for short-term use. Proper storage and handling are essential to maintain the antibody’s stability and effectiveness .