|Tested species reactivity||Human, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||KLH conjugated synthetic peptide between 669-699 amino acids from the C-terminal region of human PFKL|
|Purification||Size-exclusion - Dialysis, Ammonium sulfate precipitation|
|Contains||0.09% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Phosphofructokinase (PFK), a major regulatory enzyme in all cells of the body, catalyzes the metabolism of sugar, and thereby is pivotal in the production of energy to maintain normal cell function. In human there are three structural loci controlling PFK: M (muscle), L (liver), and P (platelet) type subunits, which are variably expressed in different tissues; human diploid fibroblasts and leukocytes express all three genes. PFK, a tetramer formed by the random association of the products of two separate gene loci to form the five possible tetramers. PFKs of muscle and liver are homotetramers of the M and L subunits, respectively. Red cells have all five isozymes: M4, M3L, M2L2, ML3, and L4. PFK is an allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. PFK catalyzes the key controlling step of glycolytic pathway. PFK deficiency can present as mild to life-threatening episodic illness. A hallmark sign of this disease is intermittent dark urine, with the color of the urine ranging from orange to dark coffee-brown, which commonly develops following strenuous exercise. The mean red cell PFK is elevated in persons with Down syndrome.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.