Human PCK1 Antibody

PCK1 (Phosphoenolpyruvate carboxykinase 1; also PEPCK-C [cytosolic]) is a monomeric, 67-68 kDa member of the PEP carboxykinase family of enzymes. It is expressed in postnatal cells such as mammary epithelium, white and brown adipocytes, skeletal muscle cells and hepatocytes. PCK1 has multiple functions, some of which are cell-specific. In particular, PCK1 has both cataplerotic (Greek: to fill down, or remove) and anaplerotic (to fill up, or replace) activity, where it removes and replaces elements of the TCA cycle. It is also gluconeogenic, and promotes glucose formation via PEP generation. Finally, it is glyceroneogenic, creating glycerol-3-phosphate that is used to reesterify and store just-released free fatty acids in adipocytes. Mouse PCK1 is 622 amino acids (aa) in length. It contains one kinase domain (aa 27-615), and two potential acetylation sites at Lys70 and 71. There are four potential splice forms. Two have alternative start sites at Met460 and Met315, while two others show a deletion of aa 34-546, plus a three aa substitution for aa 85-204, respectively. Over aa 551-622, mouse PCK1 shares 93% and 82% aa identity with rat and human PCK1, respectively.