adhT Protein, Geobacillus stearothermophilus (His, StrepⅡ)

adhT, a NAD(+)-dependent alcohol dehydrogenase, catalyzes the oxidation of alcohols, converting them to aldehydes or ketones while reducing NAD(+) to NADH. Its specificity enables participation in diverse metabolic pathways, contributing to alcohol breakdown and NADH regeneration. Integral to alcohol metabolism, adhT maintains cellular redox balance and energy homeostasis, crucial for processes like fermentation and energy production. adhT Protein, Geobacillus stearothermophilus (His, Strep) is the recombinant adhT protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

adhT is a NAD(+)-dependent alcohol dehydrogenase, a protein that catalyzes the oxidation of alcohols using NAD(+) as a cofactor. This enzymatic activity involves the conversion of alcohols to their corresponding aldehydes or ketones, accompanied by the reduction of NAD(+) to NADH. The specificity of adhT allows it to participate in various metabolic pathways, contributing to the breakdown of alcohols and the regeneration of NADH. As a key player in alcohol metabolism, adhT plays a role in maintaining cellular redox balance and energy homeostasis. Its activity is integral to processes such as fermentation, where the conversion of alcohols is a crucial step in energy production.

Others

E. coli

N-StrepⅡ;N-6*His

P12311 (K2-D337)

/

Partial

KAAVVEQFKKPLQVKEVEKPKISYGEVLVRIKACGVCHTDLHAAHGDWPVKPKLPLIPGHEGVGVIEEVGPGVTHLKVGDRVGIPWLYSACGHCDYCLSGQETLCERQQNAGYSVDGGYAEYCRAAADYVVKIPDNLSFEEAAPIFCAGVTTYKALKVTGAKPGEWVAIYGIGGLGHVAVQYAKAMGLNVVAVDLGDEKLELAKQLGADLVVNPKHDDAAQWIKEKVGGVHATVVTAVSKAAFESAYKSIRRGGACVLVGLPPEEIPIPIFDTVLNGVKIIGSIVGTRKDLQEALQFAAEGKVKTIVEVQPLENINDVFDRMLKGQINGRVVLKVD

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.