ADH Protein, Drosophila melanogaster (His, Strep)

ADH Protein, Drosophila melanogaster (S2-I256) is a dimeric Zn-containing enzyme in the oxidoreductase family with acetaldehyde dehydrogenase and alcohol dehydrogenase activity, therefore, can oxidize primary and secondary alcohols. ADH Protein, Drosophila melanogaster (S2-I256) is E.coli-sourced and tag-free, the initiator methionine is naturally removed. ADH Protein, Drosophila melanogaster (His, Strep) is the recombinant ADH protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of ADH Protein, Drosophila melanogaster (His, Strep) is 255 a.a., .

Alcohol dehydrogenase proteins (ADHs) are a group of dimeric Zn-containing enzymes in the oxidoreductase family, ADHs have acetaldehyde dehydrogenase (acetylating) and alcohol dehydrogenase (NAD+) activity, enabling ADHs to oxidize the [CH-OH] group of primary or secondary alcohols using NAD+ or NADP+ as the electron acceptor. ADHs are located in cytosol and part of protein-containing complex. ADHs are expressed mainly in liver, and also exist in other structures, including circulatory system, digestive system, extended germ band embryo, fat body; and reproductive system. ADHs are up-regulated by retinoic acid, growth hormone and glucocorticoids while being down-regulated by androgens and thyroid hormone^[1][2][3].

Others

E. coli

N-Strep;N-6*His

P00334 (S2-I256)

3771877

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

<1 EU/μg, determined by LAL method.