Anti-PKM2 (C-terminal) antibody produced in rabbit

Pyruvate Kinase (PK) is a key regulatory enzyme in glycolysis and has four known isoforms, namely, L, R, M1 and M2. PK isoform M1 is expressed during the development of the embryo and is the dominant isoform in cardiac, brain and skeletal muscle tissues. The M2 isoform has been linked to cancer metastasis

Anti-PKM2 (C-terminal) antibody is suitable for use in immunoprecipitation (2-4 μg using A549 cell lysates) and western blot (approx. 60 kDa, 1-2 μg/mL using L8 and C2C12 cell lysates). The antibody may also be used for indirect immunofluorescence (2-4 μg using HeLa cells).

Anti-PKM2 (C-terminal) antibody produced in rabbit has been used in immunohistochemistry and immunocytochemistry.

Anti-PKM2 (C-terminal) antibody is specific for human, rat, and mouse PKM2. In immunoblotting, detection of the PKM2 band is specifically inhibited by the PKM2 immunizing peptide.

Phosphorylation of the M2 isoform at Tyr105 inhibits its activity and is common in human cancers, suggesting Tyr105 is a critical metabolic switch in cancer cells that promotes tumorigenesis. Tumor cells have been reported to exclusively overexpress the embryonic M2 isoform. The tumor metabolome is characterized by a high glycolytic turnover rate and tumor cells are able to proliferate under conditions of aerobic glycolysis, known as the Warburg effect. Knockdown of the M2 isoform in human cancer cell lines and its replacement by the M1 isoform has been shown to lead to reversal of the Warburg effect and reduced ability to form tumors in mouse xenografts.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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