PCK1 (phosphoenolpyruvate carboxykinase 1 (soluble))

Polyclonal antibody produced in rabbits immunized with a synthetic peptide corresponding to a region of Human PCK1.

Lyophilized powderWB: Antibody

1:62500

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. PCK1 is a main control point for the regulation of gluconeogenesis. The cytosolic enzyme encoded by this gene. along with GTP. catalyzes the formation of phosphoenolpyruvate from oxaloacetate. with the release of carbon dioxide and GDP. The expression of

Activity is affected by a number of hormones regulating this metabolic process (such as glucagon insulin or glucocorticoids).

Cytoplasm.

Defects in PCK1 are the cause of cytosolic phosphoenolpyruvate carboxykinase deficiency (cytosolic PEPCK deficiency) [MIM:261680]. PEPCK deficiency is a metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia hepatomegaly failure to thrive lactic acidosis and hypoglycaemia. Autoposy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family. Summary: This protein is a main control point for the regulation of gluconeogenesis. The cytosolic enzyme encoded by this gene along with GTP catalyzes the formation of phosphoenolpyruvate from oxaloacetate with the release of carbon dioxide and GDP. The expression of this gene can be regulated by insulin glucocorticoids glucagon cAMP and diet. A mitochondrial isozyme of the encoded protein also has been characterized. Hajarnis. S. . et al. . (2005) J Biol Chem. 280(31). 28272-80.