Human PFK2 / PFKFB3 Protein (His & GST Tag)

IPFK2,PFK2

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Catalog Number	P13230-H20B
Organism Species	Human
Host	Baculovirus-Insect Cells
Synonyms	IPFK2,PFK2
Molecular Weight	The recombinant human PFKFB3 /GST chimera consists of 757 amino acids and has a calculated molecular mass of 87.4 KDa. It migrates as an approximately 75 KDa band in SDS-PAGE under reducing conditions.
predicted N	Met
SDS-PAGE
Purity	> 85 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human PFKFB3 isoform 1 (Q16875-1) (Met 1-His 520) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Bio-activity	Kinase activity untested
Research Area	Immunology |Signal Transduction |Protein Kinase |Intracellular Kinase |Other Intracellular Protein Kinases
Formulation	Supplied as sterile 20mM Tris, 500mM NaCl, pH 7.0, 10% glycerol, 0.3mM DTT 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, is a potent activator of phosphofructokinase, which is a rate-limiting enzyme of glycolysis. Highly phosphorylated PFKFB3 protein was found in human tumor cells, vascular endothelial cells, and smooth muscle cells. Fructose 2,6-bisphosphate (Fru-2,6-BP) is an allosteric activator of 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in glycolysis. The concentration of PFK2 depends on the activity of the bifunctional enzyme, 6-phosphofructo-2-kinase / fructose-2,6-bisphosphatase (PFK-2 / FBPase). PFK2 controls the glycolytic flux via the allosteric activator fructose 2,6-bisphosphate. Because of its proto-oncogenic character, the PFK-2/FBPase-2 of the PFKFB3 gene is assumed to play a critical role in tumorigenesis. The hypoxia-inducible form of 6-phosphofructo-2-kinase / fructose-2,6-bisphosphatase (PFKFB3) plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions.
Reference	Kessler R, et al. (2008) 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3) is up-regulated in high-grade astrocytomas. J Neurooncol. 86(3):257-64. Yalcin A, et al. (2009) Nuclear targeting of 6-phosphofructo-2-kinase (PFKFB3) increases proliferation via cyclin-dependent kinases. J Biol Chem. 284(36):24223-32. Atsumi T, et al. (2002) High expression of inducible 6-phosphofructo-2-kinase / fructose-2, 6-bisphosphatase (iPFK-2; PFKFB3) in human cancers. Cancer Res. 262(20): 5881-7. Kim SG, et al. (2006) Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase / fructose-2,6-bisphosphatase (PFKFB3): a possible new target for cancer therapy. J Biol Chem. 281(5): 2939-44.