| Reactivity | HuSpecies Glossary |
| Applications | Enzyme Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to produce NADH during the oxidation of propionaldehyde. The specific activity is >150 pmol/min/μg, as measured under the described conditions. |
| Source | E. coli-derived human Aldehyde Dehydrogenase 1-A1/ALDH1A1 protein Ser2-Ser501, with an N-terminal Met and 6-His tag |
| Accession # | |
| N-terminal Sequence | Ser2 |
| Structure / Form | Noncovalently-linked homotetramer |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | ALDH1A1 |
| Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 56 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE | 57 kDa, reducing conditions |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Supplied as a 0.2 μm filtered solution in Tris, NaCl, DTT and Glycerol. |
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| Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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| Assay Procedure |
*Adjusted for Substrate Blank **Using the extinction coefficient 6220 M-1cm-1 ***Using the path correction 0.32 cm Note: the output of many spectrophotometers is in mOD Per Well:
|
Aldehyde dehydrogenases (ALDHs) are NAD(P)+-dependent enzymes that detoxify aldehydes by oxidizing them to carboxylic acids. Nineteen ALDHs are present in humans, expressed in a variety of organelles and having different substrate preferences (1). ALDH1A1 is a cytosolic enzyme that preferentially oxidizes retinaldehyde to retinoic acid (2). ALDH1A1 is expressed in the epithelium of many organs, including brain, liver, testis, eye lens and cornea (3). ALDH1A1 is highly expressed in brain dopaminergic neurons, where it produces the retinoic acid required for their differentiation and development (4). The retinoic acid produced by ALDH1A1 is also important for the differentiation of hematopoietic stem cells (5). ALDH1A1 is a major enzyme in the oxidation of acetaldehyde, a toxic metabolite of ethanol (6).
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