Recombinant Geobacillus stearothermophilus ADH Protein (K2-D339)
Cat.No. : | ADH-1512G |
Product Overview : | Recombinant Geobacillus stearothermophilus GG-adh(K2-D339 end) protein without tag was expressed in E. coli |
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Description : | Active with primary alcohols, including methanol. |
Source : | E. coli |
Species : | Geobacillus stearothermophilus |
Tag : | Non |
Form : | Liquid |
Protein length : | K2-D339 |
Endotoxin : | < 0.01 EU/μg of the protein |
Purity : | 90% |
Stability : | Samples are stable for up to twelve months from date of receipt at -20 to -80 centigrade |
Storage : | Store it under sterile conditions at -20 to -80 centigrade. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Storage Buffer : | Supplied as sterile 50 mM Tris-HCl (pH7.5), 200 mM NaCl, 20% glycerol |
Shipping : | It is shipped out with blue ice. |
Official Symbol : | adh |
Synonyms : | Alcohol dehydrogenase; adh; EC:1.1.1.1; ADH |
UniProt ID : | P42327 |
Official Symbol : | adh |
Synonyms : | Alcohol dehydrogenase; adh; EC:1.1.1.1; ADH |
UniProt ID : | P42327 |
Products Types
◆ Assay kits | ||
Kit-0051 | Alcohol Dehydrogenase Activity Assay Kit | +Inquiry |
Kit-0052 | Alcohol Dehydrogenase Detection Kit | +Inquiry |
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Customer Reviews (2)
Write a reviewDemonstrates high sensitivity in detecting low abundance proteins in complex samples.
Displays excellent membrane permeability in cell-penetrating peptide assays.
Q&As (10)
Ask a questionGenetic variations or polymorphisms in the ADH gene have been associated with differences in alcohol metabolism and susceptibility to alcohol-related disorders, linking genotype to phenotype.
ADH exhibits a tissue-specific expression pattern, with variations in expression levels and isoform distribution among different organs and cell types, reflecting its functional diversity.
The expression of ADH is regulated under normal physiological conditions, and it can be induced or suppressed in response to alcohol exposure or other metabolic factors, highlighting its adaptive nature.
The structural features and conformational changes of ADH upon substrate binding play a crucial role in its enzymatic activity, influencing the efficiency and specificity of alcohol metabolism.
Pharmacological agents or environmental factors can modulate ADH expression or activity, potentially affecting alcohol metabolism and offering avenues for therapeutic interventions or personalized medicine.
Different ADH isoforms display distinct kinetic properties, including substrate specificity, affinity, and catalytic efficiency, enabling them to metabolize alcohol and related substrates with varying efficiencies.
ADH can catalyze the oxidation or reduction of various substrates beyond alcohol, suggesting its involvement in broader metabolic pathways and potential metabolic interplay.
ADH activity or expression can vary among individuals with different levels of alcohol consumption and in populations with distinct alcohol-related cultural practices, reflecting the interplay between genetic and environmental factors.
ADH plays a central role in the overall metabolism and detoxification of alcohol, contributing to the conversion of alcohol to acetaldehyde and subsequently to acetic acid, with ADH deficiency or dysfunction leading to altered alcohol metabolism and potential susceptibility to alcohol-related pathologies.
ADH requires specific cofactors or coenzymes, such as NAD+ or NADH, for its activity, serving as electron carriers and regulators of ADH function.
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