Alanine aminotransferase (ALT, GPT, Gutamate pyruvate transaminanse), catalyzes the transamination reaction. ALT requires pyridoxal-5-phosphate (PLP) as prosthetic group. ALT was previously known as serum glutamic pyruvic transaminase (SGPT). ALT is a cytoplasmic enzyme that catalyzes the transamination of alpha-ketoglutarate and L-alanine, forming glutamate and pyruvate. ALT is found in liver, kidney, brain and heart , as two isoforms: cytosolic ALT and mitochondrial ALT. These enzymes function in cellular nitrogen metabolism and also liver gluconeogenesis. The highest activities of ALT are found in hepatocytes and striated (skeletal and cardiac) muscle cells. Therefore, increased serum ALT activity can accompany hepatocellular injury or necrosis of striated muscle. With cell injury or death, ALT (a "leakage" enzyme) escapes from the cytosol. Determination of ALT activity is a relatively sensitive indicator of hepatic damage in certain animal species and can help determine whether further diagnostic tests.
Recombinant ALT is a single, non-glycosylated, polypeptide chain containing 495 amino acids and having a molecular mass of 54,479D.
Protein Family:Belongs to the class-I pyridoxal-phosphate-dependent
Protein Domains:IPR004839 Aminotransferase, class I and II
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：1u
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：≥95% (RP-HPLC and SDS-PAGE.) Chromatographically purified.
Form：Supplied as a liquid in 40mM sodium acetate buffer, pH 5.5, 1mM DTT, 1mM EDTA, 5mM 2-oxoglutarate, 0.1mM pyridoxal-5'-phosphate.
