Recombinant Human ADH7 Protein (His Tag)
SKU: PKSH032051-50
Recombinant Human ADH7 Protein (His Tag)
SKU # | PKSH032051 |
Expression Host | HEK293 Cells |
Description
Synonyms | ADH7, Alcohol Dehydrogenase Class 4 Mu/Sigma Chain, Alcohol Dehydrogenase Class IV Mu/Sigma Chain, Gastric Alcohol Dehydrogenase, Retinol Dehydrogenase |
Species | Human |
Expression Host | HEK293 Cells |
Sequence | Met 1-Phe386 |
Accession | P40394 |
Calculated Molecular Weight | 42.5 kDa |
Observed Molecular Weight | 44 kDa |
Tag | C-His |
Bio-activity | Not validated for activity |
Properties
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
Background
Alcohol dehydrogenase class 4 mu/sigma chain (ADH7) is a cytoplasm enzyme which is a member of the alcohol dehydrogenase family. The expression of this gene makes it much more abundant in the stomach than the liver, thus it differs from the other known gene family members. ADH7 may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.