Aldolase (EC 4.1.2.13, Rabbit Muscle)

Aldolase is present in all animal and plant tissue and in most microorganisms. Class I aldolase, found in animal and higher plant tissue, is characterized by not requiring a bivalent metal cofactor and by the formation of a ketimine Schiff base intermediate with the substrate dihydroxyacetone phosphate. (This base may be reduced by NaBH4 and the enzyme inactivated). Class II aldolase, found in primitive cells, such as yeast and bacteria, requires a metal cofactor and is inhibited by EDTA. Appearance: Supplied as a white lyophilized powder. Purity: >80% (Biuret), Activity: >8u/mg, Unit Definition: 1 unit will convert 1 micromole of Fructose-1,6-Diphosphate to Dihydroxyacetone phosphate and glyceraldehyde-3-phosphate per min at pH 7.4, 25ºC. Enzymatic Impurities: Pyruvate Kinase: <0.1%, Lactic Dehydrogenase: <0.03%, GAPD: < .03%, Phosphoglucose Isomerase: <0.6%, Triosephosphate Isomerase: <0.05%, Storage and Stability: Lyophilized powder may be stored at -20°C. Stable for 6 months at -20°C. Reconstitute with sterile ddH2O immediately before use. 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.