Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.
Greater than 85% as determined by SDS-PAGE.
PKM2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 60.2kDa. PKM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.
MGSSHHHHHH SSGLVPRGSH MGSMPKPHSE AGTAFIQTQQ LHAAMADTFL EHMCRLDIDS APITARNTGI ICTIGPASRS VEMLKEMIKS GMNVARLNFS HGTHEYHAET IKNVREATES FASDPILYRP VAVALDTKGP EIRTGLIKGS GTAEVELKKG ATLKITLDNA YMEKCDENIL WLDYKNICKV VEVGSKIYVD DGLISLQVKE KGADFLVTEV ENGGSLGSKK GVNLPGAAVD LPAVSEKDIQ DLKFGVEQDV DMVFASFIRK AADVHEVRKV LGEKGKNIKI ISKIENHEGV RRFDEILEAS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC NRAGKPVICA TQMLESMIKK PRPTRAEGSD VANAVLDGAD CIMLSGETAK GDYPLEAVRM QHLIAREAEA AIYHLQLFEE LRRLAPITSD PTEAAAVGAV EASFKCCSGA IIVLTKSGRS AHQVARYRPR APIIAVTRNP QTARQAHLYR GIFPVLCKDA VLNAWAEDVD LRVNLAMDVG KARGFFKKGD VVIVLTGWRP GSGFTNTMRV VPVP.
Tumour Type M2 Pyruvate Kinase (PKM2) is a crucial enzyme in the glycolytic pathway, which is responsible for the conversion of phosphoenolpyruvate (PEP) to pyruvate, producing ATP in the process . PKM2 is one of the four isoforms of pyruvate kinase, the others being PKL, PKR, and PKM1 . This enzyme is particularly significant in cancer research due to its unique role in tumor metabolism and its potential as a diagnostic marker.
Pyruvate kinase exists in four isoforms, each with tissue-specific expression:
PKM2 is predominantly expressed in tumor cells and exists mainly in its dimeric form, which has a lower affinity for PEP compared to its tetrameric form . This dimeric form, often referred to as Tumor M2-PK, is associated with the metabolic reprogramming of cancer cells, known as the Warburg effect . This effect describes how cancer cells preferentially produce energy through aerobic glycolysis rather than oxidative phosphorylation, even in the presence of sufficient oxygen .
In addition to its metabolic role, PKM2 has non-metabolic functions that contribute to tumorigenesis. It can translocate to the nucleus and act as a protein kinase, phosphorylating various targets and influencing multiple physiological processes . This dual functionality makes PKM2 a critical player in cancer cell metabolism and proliferation.
The unique properties of PKM2, particularly its dimeric form in tumor cells, make it a valuable biomarker for cancer diagnosis and monitoring . Quantifying Tumor M2-PK in plasma and stool samples can aid in the early detection of tumors and in tracking the effectiveness of cancer therapies . Furthermore, targeting PKM2’s activity and its regulatory mechanisms holds promise for developing novel cancer treatments .