ALDOC Mouse

Aldolase C, also known as Fructose-Bisphosphate Aldolase C (ALDOC), is an enzyme that plays a crucial role in glycolysis and gluconeogenesis. It belongs to the class I fructose-bisphosphate aldolase family, which also includes aldolase A (ALDOA) and aldolase B (ALDOB) . This enzyme is specifically expressed in the brain, particularly in the hippocampus and Purkinje cells .

Aldolase C catalyzes the reversible aldol cleavage of fructose-1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively . This reaction is a key step in the glycolytic pathway, which is essential for energy production in cells.

Recombinant Mouse Aldolase C is produced in Escherichia coli (E. coli) and is available as a full-length protein with a His-tag at the N-terminus . The recombinant protein is purified using proprietary chromatographic techniques to achieve a purity of over 95% . It is suitable for various applications, including SDS-PAGE and mass spectrometry (MS) .

The enzyme’s mode of action involves the cleavage of fructose-1,6-bisphosphate into two three-carbon products, which are then further processed in the glycolytic pathway to produce ATP, the energy currency of the cell . This process is vital for maintaining cellular energy levels, especially in brain cells where Aldolase C is predominantly expressed.

The expression of Aldolase C is regulated at the transcriptional level and is influenced by various factors, including cellular energy status and metabolic demands . Additionally, post-translational modifications such as phosphorylation can affect the enzyme’s activity and stability.

Recombinant Mouse Aldolase C is widely used in research to study its role in metabolism and its potential implications in neurological disorders. Its high purity and activity make it a valuable tool for biochemical assays and structural studies .