ADH-HT Protein, Geobacillus stearothermophilus (His, Strep)

The ADH-HT protein is a thermophilic NAD(+)-dependent alcohol dehydrogenase that functions primarily as an alcohol dehydrogenase. This protein plays a vital role in ethanol metabolism by catalyzing the conversion of ethanol to acetaldehyde using NAD(+) as a cofactor in the process. ADH-HT Protein, Geobacillus stearothermophilus (His, Strep) is the recombinant ADH-HT protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of ADH-HT Protein, Geobacillus stearothermophilus (His, Strep) is 338 a.a., .

ADH-HT Protein is a thermophilic NAD(+)-dependent alcohol dehydrogenase that predominantly functions as an ethanol dehydrogenase. This protein plays a crucial role in the metabolism of ethanol by catalyzing the conversion of ethanol to acetaldehyde, utilizing NAD(+) as a cofactor in the process. Its thermophilic nature enables ADH-HT to function optimally at high temperatures, making it particularly useful in industrial applications where elevated temperatures are required. The specificity of ADH-HT for ethanol and its reliance on NAD(+) make it a valuable enzyme in various biotechnological processes such as biofuel production and the synthesis of pharmaceutical intermediates. Understanding the characteristics and properties of ADH-HT Protein is vital for harnessing its potential applications in biotechnology and understanding its role in ethanol metabolism.

Others

E. coli

N-Strep;N-6*His

P42328 (K2-K339)

/

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.