PKM2 Human
Greater than 95.0% as determined by SDS-PAGE.
Description
PKM2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 551 amino acids (1-531 a.a.) and having a molecular mass of 60.1kDa. The PKM2 is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P.
Product Science Overview
Tumor Type M2 Pyruvate Kinase (PKM2) is a crucial enzyme in the glycolytic pathway, catalyzing the conversion of phosphoenolpyruvate (PEP) to pyruvate, with the concomitant production of ATP. PKM2 is one of four isoforms of pyruvate kinase, the others being PKL, PKR, and PKM1. PKM2 is particularly significant due to its unique role in cancer metabolism and tumorigenesis.
Pyruvate kinase has four tissue-specific isozymes in animals:
- PKL: Expressed in the liver.
- PKR: Found in red blood cells.
- PKM1: Present in the brain, skeletal muscle, and heart.
- PKM2: Expressed in early embryonic cells and other proliferating cells, including many types of tumors .
PKM2 is transcribed from the PKM gene via alternative splicing, which results in the inclusion of exon 10 and exclusion of exon 9, distinguishing it from PKM1 .
PKM2 can exist in two forms:
- Tetrameric Form: Active form with high binding affinity to PEP.
- Dimeric Form: Less active form with low binding affinity to PEP.
The tetrameric form is associated with normal cellular metabolism, while the dimeric form is often found in cancer cells and is linked to the Warburg effect, where cancer cells preferentially produce energy through aerobic glycolysis even in the presence of oxygen .
PKM2 plays a pivotal role in cancer metabolism and tumorigenesis. It not only functions as a metabolic enzyme but also has non-metabolic roles, such as acting as a protein kinase. In the nucleus, PKM2 can phosphorylate various protein targets, contributing to multiple physiological processes associated with cancer progression .
The activity and expression of PKM2 are regulated by several factors:
Human recombinant PKM2 is produced using recombinant DNA technology, allowing for the study of its structure, function, and role in cancer. This recombinant form is essential for research and therapeutic development, providing insights into targeting PKM2 for cancer treatment.
