ADH1C Human, sf9

Alcohol Dehydrogenase 1C, Human Recombinant, sf9
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Cat. No.
BT6877
Source
Sf9, Baculovirus cells.
Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Molecular Structure and Production

ADH1C Human, sf9 consists of a single glycosylated polypeptide chain with 381 amino acids (residues 1–375) and an additional 6-amino-acid IgG His-Tag at the C-terminus. Key characteristics include:

PropertyDetail
Molecular Mass40.6 kDa
Expression SystemSf9 Baculovirus cells
Purity>95% (verified by SDS-PAGE)
FormulationPhosphate-buffered saline (pH 7.4) with 10% glycerol
StabilityStable at 4°C for 2–4 weeks; long-term storage at -20°C with 0.1% HSA/BSA

This recombinant enzyme retains the functional properties of native ADH1C, including zinc ion binding and oxidoreductase activity .

Functional Role in Ethanol Metabolism

ADH1C catalyzes the oxidation of ethanol to acetaldehyde, a critical step in alcohol metabolism. Its broader substrate specificity includes:

  • Retinol

  • Hydroxysteroids

  • Lipid peroxidation products .

The enzyme’s activity is influenced by genetic polymorphisms. The ADH1C Ile350Val (rs698) variant significantly impacts ethanol oxidation rates:

  • Ile350 (ADH1C*1): High-activity allele associated with faster acetaldehyde production .

  • Val350 (ADH1C*2): Low-activity allele linked to slower ethanol metabolism .

Genetic and Clinical Research Findings

Meta-analyses of ADH1C polymorphisms reveal its role in alcohol dependence (AD) and related diseases:

Table 1: Association of ADH1C Ile350Val with Alcohol Dependence

PopulationOdds Ratio (OR)Allelic P-ValueEffect Size
Combined1.51 (1.31–1.73)1×10<sup>-8</sup>Protective effect of Ile350
Asian2.14 (1.89–2.43)4×10<sup>-33</sup>Stronger protection
European1.21 (1.01–1.45)0.04Moderate association

Key findings:

  • Asian populations show the strongest protective effect due to higher ADH1C*1 allele frequency (91.7% vs. 8.3% for ADH1C*2) .

  • Carriers of ADH1C*1 have a 50–114% reduced risk of alcohol-related cirrhosis compared to ADH1C*2 homozygotes .

Comparative Allele Frequency Distribution

The ADH1C*2 allele exhibits marked ethnic variability:

PopulationADH1C*2 FrequencyClinical Relevance
East Asian8.3%Low prevalence limits homozygous cases
European25–30%Moderately associated with AD risk
African10–15%Understudied in alcohol-related diseases

Research Applications

ADH1C Human, sf9 is utilized in:

  1. Enzyme kinetics studies: Comparing catalytic efficiency of ADH1C variants .

  2. Drug development: Screening inhibitors or modulators of ethanol metabolism.

  3. Biochemical assays: Analyzing interactions with retinoids or toxic lipid derivatives .

Product Specs

Introduction
ADH1C, a member of the zinc-containing alcohol dehydrogenase family, plays a crucial role in metabolizing various substrates, including ethanol, retinol, aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. This monomorphic enzyme exhibits high activity in fetal and infant livers, gradually decreasing during gestation and becoming minimally active in adulthood.
Description
ADH1C Human Recombinant, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 381 amino acids (1-375) with a molecular weight of 40.6kDa. This recombinant protein is fused to a 6 amino acid IgG His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The ADH1C protein solution (1mg/ml) is supplied in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. It is crucial to avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% based on SDS-PAGE analysis.
Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
TVLTFHHHHH H.

Q&A

FAQs for Researchers on ADH1C Human (sf9)

Basic Research Questions

  • How is recombinant ADH1C Human (sf9) purified, and what quality control metrics ensure enzymatic integrity?

    • Methodological answer: ADH1C Human (sf9) is purified using proprietary chromatographic techniques, including affinity chromatography with a C-terminal His-Tag for immobilized metal affinity purification .

    • Quality control:

      • Purity: Validated via SDS-PAGE (>95% homogeneity) .

      • Activity: Enzymatic assays using ethanol or retinol substrates under standardized pH (7.4) and temperature (25°C) conditions.

      • Stability: Stored in PBS with 10% glycerol at -20°C; carrier proteins like HSA/BSA (0.1%) are recommended for long-term storage to prevent aggregation .

  • What substrates and experimental conditions are optimal for in vitro ADH1C activity assays?

    • Substrate specificity:

      SubstrateKinetic ParameterValueSource
      EthanolK<sub>m</sub>55 μM
      RetinolV<sub>max</sub>8.2 nmol/min/mg

    • Conditions:

      • Use NAD<sup>+</sup> as cofactor (1–2 mM) in phosphate buffer (pH 7.4) .

      • Avoid freeze-thaw cycles to prevent enzyme denaturation .

Advanced Research Questions

  • How do ADH1C polymorphisms (e.g., Ile350Val) influence enzymatic activity and disease risk?

    • Methodological approach:

      • Genotyping: Use PCR-RFLP or sequencing to identify rs698 (Ile350Val) variants .

      • Functional analysis: Compare kinetic parameters (K<sub>m</sub>, V<sub>max</sub>) between isoforms.

    • Key findings:

      • The Ile350 variant (ADH1C*1) shows 2.14× higher protection against alcohol dependence in Asians (OR = 2.14, P = 4×10<sup>−33</sup>) .

      • Val350 (ADH1C*2) correlates with slower ethanol metabolism, increasing acetaldehyde accumulation and toxicity .

  • What regulatory mechanisms control ADH1C expression in hepatic models?

    • Experimental design:

      • Treat primary hepatocytes with FXR agonists (e.g., GW4064) or bile acids (chenodeoxycholic acid) to assess transcriptional upregulation .

      • Use ChIP-seq to confirm FXR binding to ADH1A/ADH1B promoters .

    • Data interpretation:

      • FXR activation increases ADH1C mRNA by 3.5-fold and enzyme activity by 2.8-fold, linking bile acid signaling to ethanol metabolism .

  • How does ADH1C redundancy with other ADH isoforms (e.g., ADH1B) affect experimental outcomes?

    • Contradiction resolution:

      • Substrate competition: Co-express ADH1C with ADH1B in sf9 cells to quantify isoform-specific contributions using selective inhibitors (e.g., 4-methylpyrazole) .

      • Ethanol metabolism: ADH1C contributes <20% of total hepatic ADH activity in adults but dominates in fetal development .

Data Contradiction Analysis

  • Why do genetic association studies report conflicting results for ADH1C and alcoholism?

    • Factors:

      • Population stratification: ADH1C*1 shows stronger protection in Asians (OR = 2.14) vs. Europeans (OR = 1.22) .

      • Epistatic interactions: ALDH2*2 variants amplify ADH1C effects on acetaldehyde accumulation .

    • Resolution strategy:

      • Perform meta-regression adjusting for ancestry, ALDH2 status, and environmental factors (e.g., alcohol intake patterns) .

Method Optimization

  • What in vitro models best recapitulate ADH1C’s role in lipid peroxidation?

    • Protocol:

      • Use HepG2 cells transfected with ADH1C sf9 constructs under oxidative stress (H<sub>2</sub>O<sub>2</sub> or 4-HNE exposure).

      • Quantify malondialdehyde (MDA) via HPLC to assess lipid peroxidation inhibition .

Product Science Overview

Introduction

Alcohol Dehydrogenase 1C (ADH1C) is an enzyme that plays a crucial role in the metabolism of alcohols within the human body. This enzyme is part of the alcohol dehydrogenase family, which is responsible for the oxidation of alcohols to aldehydes or ketones. The recombinant form of ADH1C, produced in Sf9 cells, is a valuable tool for research and industrial applications.

Structure and Production

The recombinant ADH1C enzyme is produced in Sf9 Baculovirus cells. It is a single, glycosylated polypeptide chain containing 381 amino acids, with a molecular mass of approximately 40.6 kDa . The molecular size on SDS-PAGE appears at approximately 40-57 kDa . This recombinant form is designed to mimic the natural enzyme found in humans, allowing for detailed studies on its function and properties.

Function and Mechanism

ADH1C catalyzes the conversion of alcohols to aldehydes, a critical step in the metabolism of ethanol and other alcohols. The enzyme operates by binding to the alcohol substrate and facilitating its oxidation through the transfer of electrons. This process is essential for the detoxification of alcohols in the liver and other tissues.

Applications

The recombinant ADH1C enzyme has several applications in both research and industry:

  • Biochemical Research: It is used to study the metabolic pathways involving alcohols and aldehydes, providing insights into the detoxification processes in the human body.
  • Drug Development: ADH1C is utilized in the development of drugs targeting alcohol metabolism disorders, such as alcoholism and alcohol-induced liver disease.
  • Industrial Biotechnology: The enzyme is employed in the production of biofuels and other industrial processes involving the oxidation of alcohols.

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