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Aldolase
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| 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. | | | Catalog # | A1335 | | Activity | 8u/mg; 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: 0.03% | | Phosphoglucose Isomerase: 0.6% | | Triosephosphate Isomerase: 0.05% | | Storage and Stability | Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile buffer. Aliquot to avoid repeated freezing and thawing. Store 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. | | CAS Number | 9024-52-6 | | Molecular Weight | 161kD | | Source | Rabbit muscle | | Purity | ~ 80% | | Form | Supplied as a white lyophilized powder. | | | Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. | | Alternate names | EC=4.1.2.13; Rabbit Muscle |
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