ADH Protein, Drosophila melanogaster (His, StrepⅡ)
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.
- Species: Others
- Source: E. coli
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Storage:Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
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.
Background
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].
Technical Parameters
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Species Others
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Source E. coli
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Tag N-StrepⅡ;N-6*His
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Accession
P00334 (S2-I256)
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Gene ID3771877
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Molecular Construction
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N-term
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StrepⅡ-6*His
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ADH (S2-I256)
Accession # P00334 -
C-term
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Protein Length
Full Length
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Synonyms
AVP; AVP-NPII; Prev. ARVP; Arginine Vasopressin (Neurophysin II, Antidiuretic Hormone, Diabetes Insipidus, Neurohypophyseal); ADH; Vasopressin-Neurophysin II-Copeptin; Prepro-Arginine-Vasopressin-Neurophysin II; Arginine Vasopressin-Neurophysin II; Vasopr
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AA Sequence
SFTLTNKNVIFVAGLGGIGLDTSKELLKRDLKNLVILDRIENPAAIAELKAINPKVTVTFYPYDVTVPIAETTKLLKTIFAQLKTVDVLINGAGILDDHQIERTIAVNYTGLVNTTTAILDFWDKRKGGPGGIICNIGSVTGFNAIYQVPVYSGTKAAVVNFTSSLAKLAPITGVTAYTVNPGITRTTLVHKFNSWLDVEPQVAEKLLAHPTQPSLACAENFVKAIELNQNGAIWKLDLGTLEAIQWTKHWDSGI
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Solution.
<1 EU/μg, determined by LAL method.
Please use rapid thawing with running water to thaw the protein.
Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Shipping with dry ice.
Documentation
References
[1]. Winberg JO, et al. Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF. Biochim Biophys Acta. 1982 May 21;704(1):7-16. [Content Brief]
[2]. Crabb DW, et al. Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology. Proc Nutr Soc. 2004 Feb;63(1):49-63. [Content Brief]
[3]. Sanghani PC, et al. Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes. Biochemistry. 2002 Sep 3;41(35):10778-86. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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