Recombinant Rat Adh5, His-tagged

• Cat.No.: Adh5-3257R
• Product Overview: Alcohol dehydrogenase class-3 (Adh5)

Specification

• Source: E. Coli or Yeast
• Species: Rat
• Tag: His
• Form: This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
• Protein length: 374
• Purity: >90%
• Notes: Small volumes of Adh5 recombinant protein may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice.
• Storage: Store at -20 degree C. For extended storage, store at -20 or -80 degree C.
• Storage Buffer: PBS pH 7.4, 50% glycerol
• Warning: This product is for research use only. Not for use in diagnostic or therapeutic procedures.

Gene Information

• Gene Name: Adh5 alcohol dehydrogenase 5 (class III), chi polypeptide [ Rattus norvegicus ]
• Official Symbol: Adh5
• Synonyms: ADH5; alcohol dehydrogenase 5 (class III), chi polypeptide; alcohol dehydrogenase class-3; FDH; FALDH; ADH-B2; GSH-FDH; alcohol dehydrogenase 2; alcohol dehydrogenase B2; alcohol dehydrogenase class-III; S-(hydroxymethyl)glutathione dehydrogenase; class III alcohol dehydrogenase, chi subunit; glutathione-dependent formaldehyde dehydrogenase
• Gene ID: 100145871
• mRNA Refseq: NM_001126120
• Protein Refseq: NP_001119592
• Pathway: Drug metabolism - cytochrome P450, organism-specific biosystem; Drug metabolism - cytochrome P450, conserved biosystem; Fatty Acid Omega Oxidation, organism-specific biosystem; Fatty acid metabolism, organism-specific biosystem; Fatty acid metabolism, con
• Function: S-(hydroxymethyl)glutathione dehydrogenase activity; S-(hydroxymethyl)glutathione dehydrogenase activity; alcohol dehydrogenase (NAD) activity; alcohol dehydrogenase (NAD) activity; alcohol dehydrogenase (NAD) activity; fatty acid binding; fatty acid binding; formaldehyde dehydrogenase activity; formaldehyde dehydrogenase activity; metal ion binding; nucleotide binding; oxidoreductase activity; protein homodimerization activity; protein homodimerization activity; zinc ion binding; zinc ion binding

Reviews

07/29/2022

Highly effective in stabilizing and enhancing the activity of enzymes in enzyme engineering.

05/29/2016

Demonstrates excellent resistance to aggregation and aggregation-prone conditions.

Q&As

What is the tissue-specific expression pattern of ADH5, and how is its expression regulated under normal physiological conditions and in response to specific stimuli?

ADH5 exhibits a tissue-specific expression pattern, and its expression is regulated by various factors such as transcriptional control and signaling pathways.

Can ADH5 efficiently metabolize different alcohol substrates, and how does its substrate specificity compare to other ADH enzymes?

ADH5 can efficiently metabolize different alcohol substrates, and its substrate specificity may differ from other ADH enzymes.

How does ADH5 expression and activity change in response to chronic alcohol exposure or alcohol withdrawal, and what are the molecular mechanisms underlying these changes?

ADH5 expression and activity can be influenced by chronic alcohol exposure or withdrawal, and studying the underlying molecular mechanisms can shed light on alcohol-related effects.

Can the activity or function of ADH5 be modulated by pharmacological agents or environmental factors, and are there potential therapeutic implications?

The activity or function of ADH5 can potentially be modulated by pharmacological agents or environmental factors, presenting potential therapeutic implications.

Are there any specific interacting proteins or cofactors that influence the activity or function of ADH5, and what are the underlying molecular mechanisms?

Interacting proteins or cofactors can modulate the activity or function of ADH5, and investigating the molecular mechanisms involved can enhance our understanding of its regulation.

What are the enzymatic kinetics and catalytic properties of ADH5, and how do they contribute to its overall activity?

The enzymatic kinetics and catalytic properties of ADH5 contribute to its overall activity and efficiency in alcohol metabolism.

Can ADH5 play a role in the metabolism of other endogenous compounds or xenobiotics, and if so, what are the implications for its broader physiological functions?

ADH5 may have implications in the metabolism of other endogenous compounds or xenobiotics, suggesting its involvement in broader physiological functions.

Are there any known genetic variations or polymorphisms in the ADH5 gene associated with altered alcohol metabolism or susceptibility to alcohol-related disorders?

Genetic variations or polymorphisms in the ADH5 gene may impact alcohol metabolism and susceptibility to alcohol-related disorders, emphasizing the role of genetic factors in its function.

What are the structural features of ADH5, and how do they contribute to its catalytic activity and binding affinity for alcohol?

The structural features of ADH5 play a crucial role in its catalytic activity and binding affinity for alcohol, and understanding these features provides insights into its function.

What is the impact of ADH5 deficiency or overexpression on alcohol metabolism and its physiological consequences?

Exploring the consequences of ADH5 deficiency or overexpression provides insights into its role in alcohol metabolism and its impact on physiological processes.