Alexa Fluor® 594 Anti-Aspartate Aminotransferase + FABP-1 antibody [EPR12145]

Supplementary info

Activity summary

Aspartate Aminotransferase (AST) also known as glutamate oxaloacetate transaminase is an enzyme that plays an important role in amino acid metabolism. AST transfers an amino group typically from aspartate to α-ketoglutarate forming oxaloacetate and glutamate. This enzyme approximately weighs 45 kDa. AST is widely expressed in tissues with especially high levels found in the liver heart skeletal muscle and kidneys.

Biological function summary

Aspartate aminotransferase participates in the malate-aspartate shuttle which facilitates the transfer of reducing equivalents across the mitochondrial membrane. This shuttle system is important in maintaining the balance of NADH and NAD+ between the cytosol and mitochondria. AST forms part of a protein complex that includes α-ketoglutarate and oxaloacetate which are central to its transaminase activity in cellular metabolism.

Pathways

Aspartate aminotransferase is significantly involved in the tricarboxylic acid (TCA) cycle and the urea cycle. Within the TCA cycle AST ensures the linkage between carbohydrate and amino acid metabolism by converting aspartate and α-ketoglutarate into oxaloacetate and glutamate. In the urea cycle the enzyme connects to argininosuccinate synthetase and argininosuccinate lyase facilitating the removal of excess nitrogen from the body.

Associated diseases and disorders

Elevated levels of aspartate aminotransferase are often indicative of liver damage including conditions like hepatitis and cirrhosis. Additionally the enzyme associates with myocardial infarction due to its high activity in cardiac tissue. Liver-related disorders may also involve fatty acid-binding protein 1 (FABP-1) which closely interacts with AST and serves as a marker for liver function and damage.