ALDOA Human

The gene encoding Aldolase-A is located on human chromosome 16p11.2 . This enzyme is ubiquitously expressed in various tissues, with high levels found in the developing embryo and adult muscle . In contrast, its expression is repressed in adult liver, kidney, and intestine, and it is present at similar levels to Aldolase-C in the brain and other nervous tissues .

Recombinant human Aldolase-A is typically produced in E. coli and purified using conventional chromatography techniques . The recombinant protein often includes a His-tag at the N-terminus to facilitate purification . The molecular weight of Aldolase-A is approximately 41.5 kDa .

Aldolase-A is essential for energy production through glycolysis. Its specific activity is greater than 10 units/mg, where one unit converts 1.0 µmol of fructose-1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate per minute at pH 7.5 and 37°C . This enzyme’s activity is crucial for maintaining the energy balance in cells, especially in muscle tissues where energy demand is high.

Deficiency in Aldolase-A has been associated with myopathy and hemolytic anemia . These conditions highlight the enzyme’s importance in muscle function and red blood cell integrity. Additionally, Aldolase-A has been identified as a lung cancer antigen (NY-LU-1), indicating its potential role in cancer diagnostics and therapeutics .

For research purposes, recombinant human Aldolase-A is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is recommended to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .

In summary, Aldolase-A (Human Recombinant) is a vital enzyme in glycolysis, with significant roles in energy production, muscle function, and potential clinical applications. Its recombinant form, produced in E. coli, provides a valuable tool for research and therapeutic development.