|Detection of Human, Mouse, and Rat PCK1 by Western Blot. Western blot shows lysates of human liver tissue, human kidney tissue, mouse kidney tissue, and rat liver tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human/Mouse/Rat PCK1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7316) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for PCK1 at approximately 68 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PCK1 (Phosphoenolpyruvate carboxykinase, cytosolic; also PEPCK-C) is a 67-69 kDa cytosolic member of the phosphoenolpyruvate kinase (GTP) family of enzymes. It is found in hepatocytes, adipocytes, intestinal and renal proximal tubule epithelial cells. PCK1 is one of two enzymes that drive the conversion of oxaloacetate plus GTP into PEP, GDP and CO2. The PEP generated in this reaction forms glucose via fructose phosphate intermediates. The other enzyme that has this activity is termed PEPCK-M and found in mitochondria. Human PCK1 is 622 amino acids (aa) in length. It contains a large catalytic region (aa 27-615) and three utilized acetylation sites. There is one potential alternative start site at Met315. Over aa 1-88, human PCK1 shares 80% aa sequence identity with mouse PCK1.
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