Anti-PKM1 antibody produced in rabbit

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.

PKM1 (pyruvate kinase M1/2) is an enzyme that belongs to the pyruvate kinase (PK) family. It is upregulated in majority of the cells other than adult muscle, brain and liver. PKM has two isoforms, M1 and M2, encoded by gene located on chromosome 15q23. PKM1 can exist as a tetramer whereas PKM2 can remain as dimer and tetramer.

The antibody detects endogenous levels of total PKM1 protein.

Peptide sequence around aa. 399-403 (V-R-A-S-S), according to the protein NP_872270.1

Pyruvate kinase (PK) is an important enzyme in glycolysis as it helps to convert phosphoenolpyruvate (PEP) into pyruvate. Pyruvate kinase-M2 (PKM2) knockdown prevents the multiplication, movement and invasion in ovarian cancer SKOV3 and OVCAR3 cells. It plays an important role in cell survival to oxidative stress. It also participates in the development of tumor.

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Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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