Recombinant Human Alcohol Dehydrogenase 1A (class I), Alpha Polypeptide, His-tagged

Cat.No. : ADH1A-1917H
Product Overview : Recombinant humanADH1A protein, fused to His-tag at N-terminus, was expressed in E. coli andpurified by using conventional chromatography techniques.
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Cat. No. : ADH1A-1917H
Description : ADH1Abelongs to the alcohol dehydrogenase family. ADH1A is a monomorphic andpredominant in fetal and infant livers, becoming less active in gestation andonly weakly active during adulthood. ADH1A plays a major role in ethanolmetabolism. With the coenzyme NAD, ADH catalyzes the reversible conversion oforganic alcohols to ketones or aldehydes.
Form : Liquid. In 20mMTris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 0.1M NaCl.
Molecular Weight : 42 kDa(395aa) confirmed by MALDI-TOF
Purity : > 90%by SDS-PAGE
Concentration : 1 mg/ml(determined by Bradford assay)
Sequences of aminoacids : MGSSHHHHHHSSGLVPRGSH MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQYTVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARIIAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTDGGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVPKLVADFMAKK FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF
Storage : Can bestored at +4°C short term (1-2 weeks). For long term storage, aliquot andstore at -20°C or -70°C. Avoid repeated freezing and thawing cycles.
Pathways : Biological oxida; Drug metabolism-cytochromeP450; Ethanol oxidation; Fatty Acid Omega Oxidation; Fatty acid metabo;Glycolysis / Gluconeogenesis; Metabolic pathways; Metabolism; Metabolism ofxenobiotics by cytochrome P450; Phase 1-Functionalization of compounds;Retinol metabolism; Tyrosine metabolism; Vitamin A and carotenoid metabolism
SDS-PAGE:
Gene Name : ADH1A alcohol dehydrogenase 1A(class I), alpha polypeptide [ Homo sapiens ]
Official Symbol : ADH1A
Synonyms : ADH1A; alcohol dehydrogenase 1A (class I),alpha polypeptide; ADH1; alcohol dehydrogenase 1A; ADH, alphasubunit; aldehyde reductase; alcohol dehydrogenase subunit alpha; alcoholdehydrogenase 1 (class I), alpha polypeptide; EC 1.1.1.1; Alcohol dehydrogenase 1A
Gene ID : 124
mRNA Refseq : NM_000667
Protein Refseq : NP_000658
MIM : 103700
UniProt ID : P07327
Chromosome Location : 4q23
Function : alcohol dehydrogenase activity; metal ionbinding; nucleotide binding; oxidoreductase activity; protein binding; zincion binding

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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Q&As (10)

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What are the regulatory mechanisms controlling ADH1A expression, and how do they respond to alcohol exposure or other metabolic factors? 09/27/2020

The expression of ADH1A is regulated by specific mechanisms, including transcriptional and post-transcriptional regulation, which can respond to alcohol exposure or metabolic factors such as hormonal signaling.

Are there any cofactors or coenzymes required for ADH1A activity, and how do they influence its catalytic function? 09/17/2019

ADH1A requires specific cofactors or coenzymes, such as NAD+ or NADH, for its activity, serving as electron carriers and modulators of ADH1A function.

How does ADH1A contribute to alcohol metabolism, and what is its catalytic efficiency and substrate specificity compared to other ADH isoforms? 07/12/2019

ADH1A plays a significant role in alcohol metabolism, showing specific catalytic efficiency and substrate specificity for the conversion of alcohol to acetaldehyde.

What are the consequences of ADH1A deficiency or knockout in experimental models, and how does it affect alcohol metabolism and related phenotypes? 04/13/2019

ADH1A deficiency or knockout in experimental models leads to altered alcohol metabolism and related phenotypes, such as decreased alcohol clearance and increased sensitivity to alcohol-induced effects.

What is the tissue-specific expression pattern of ADH1A, and how does it differ from other ADH isoforms in terms of its expression levels and distribution across organs and cell types? 02/16/2019

ADH1A exhibits a tissue-specific expression pattern, with higher expression levels in certain organs such as the liver, and its distribution may differ from other ADH isoforms, reflecting functional specialization.

Are there any genetic variations or polymorphisms in the ADH1A gene associated with differences in alcohol metabolism or susceptibility to alcohol-related disorders? 02/12/2018

Genetic variations or polymorphisms in the ADH1A gene have been associated with differences in alcohol metabolism and susceptibility to alcohol-related disorders, highlighting the impact of genotype on phenotype.

How does the expression or activity of ADH1A change in response to pharmacological agents or environmental factors, and what are the implications for alcohol metabolism or therapy? 02/02/2018

Pharmacological agents or environmental factors can modulate ADH1A expression or activity, potentially influencing alcohol metabolism and providing avenues for therapeutic interventions or personalized medicine.

Can ADH1A metabolize other substrates apart from alcohol, and what are the implications for its broader metabolic role? 11/11/2017

ADH1A has the capacity to metabolize other substrates beyond alcohol, suggesting its involvement in broader metabolic pathways and potential metabolic interactions.

How does ADH1A expression or activity vary in different species or populations, and what are the underlying genetic and environmental factors influencing these variations? 09/18/2017

ADH1A expression or activity may vary among different species or populations, influenced by genetic and environmental factors, contributing to inter-individual or inter-species differences in alcohol metabolism and tolerance.

What are the structural features of ADH1A, and how do they relate to its enzymatic activity and substrate binding? 11/11/2016

The structural features of ADH1A, such as its active site and binding domains, are critical for its enzymatic activity and substrate recognition, enabling efficient alcohol oxidation.

Customer Reviews (2)

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Reviews
09/09/2017

    Exhibits remarkable enzymatic activity under a wide range of pH conditions.

    06/09/2016

      Provides reliable and consistent results in protein folding and unfolding studies.

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