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Tumor Type M2 Pyruvate Kinase (PKM2) is a key enzyme in the glycolytic pathway, specifically expressed at high levels in tumor cells. It plays a crucial role in the metabolic reprogramming of cancer cells, facilitating their rapid growth and proliferation. The enzyme is encoded by the PKM gene and is one of the four isozymes of pyruvate kinase found in mammals, the others being L, R, and M1 .
PKM2 catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), generating adenosine triphosphate (ATP) and pyruvate in the final step of glycolysis. This reaction is essential for the production of energy in cells. Unlike other pyruvate kinase isozymes, PKM2 can exist in different oligomeric states, including a highly active tetrameric form and a less active dimeric form. The dimeric form is often found in cancer cells and is associated with the Warburg effect, where cancer cells preferentially produce energy through aerobic glycolysis even in the presence of oxygen .
PKM2 is not only involved in glycolysis but also plays non-metabolic roles that contribute to tumorigenesis. It can translocate to the nucleus and act as a protein kinase, phosphorylating various substrates involved in cell proliferation and survival. This dual functionality makes PKM2 a critical player in cancer metabolism and a potential target for cancer therapy .
Mouse anti-human PKM2 antibodies are monoclonal antibodies specifically designed to target the human form of PKM2. These antibodies are used in research and diagnostic applications to detect and quantify PKM2 levels in various biological samples. They are particularly useful in studying the role of PKM2 in cancer and in developing therapeutic strategies targeting this enzyme .
Given its central role in cancer metabolism, PKM2 has emerged as a promising target for cancer therapy. Inhibitors of PKM2 activity, as well as agents that promote its tetramerization, are being explored as potential therapeutic strategies. For instance, TEPP-46 is a small molecule that induces the tetramerization of PKM2, thereby enhancing its glycolytic activity and reducing its non-metabolic functions that promote tumor growth .