Human Alanine AminoTransferase (Recombinant)

Recombinant Human Alanine Aminotransferase

Synonym: ALT1, Glutamic-pyruvic transaminase 1, GPT 1, Glutamic-alanine transaminase 1, AAT1, ALT, ALAT, SGPT

Source: E.Coli

Background: The enzyme alanine aminotransferase (ALT) was previously known as serum glutamic pyruvic transaminase (SGPT). This enzyme also is correctly referred to as alanine transaminase. ALT is a cytoplasmic enzyme that catalyzes the transamination of alpha-ketoglutarate and L-alanine, forming glutamate and pyruvate.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

Description: Recombinant Alanine Aminotransferase produced in E. coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.

Recombinant ALT is purified by proprietary chromatographic techniques.

Physical Appearance: Sterile liquid formulation at a concentration of 1,430IU/ml.

Formulation: The protein (1mg/ml) was dialyzed against 40mM sodium acetate buffer (pH 5.5), 1mM DTT,1mM EDTA, 5mM 2-oxoglutarate and 0.1mM pyridoxal-5'-phosphate.

Stability: rALT although stable at 10°C for 5 days, should be stored desiccated below -18°C. Please avoid freeze-thaw cycles.

Purity: Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS PAGE.

Biological Activity: Recombinant ALT is fully biologically active when compared to standard. The specific activity was found to be 1000 U/mg.

Usage: For LABORATORY RESEARCH USE ONLY.