ADH6 Human

Alcohol Dehydrogenase 6 Human Recombinant
Cat. No.
BT7063
Source
E.coli.
Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined 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

ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.
ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Alcohol dehydrogenase 6 (ADH6) is a member of the alcohol dehydrogenase family. These enzymes play a role in metabolizing various substrates such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and products of lipid peroxidation. ADH6 is found in both the stomach and liver. A notable feature of ADH6 is the presence of a glucocorticoid response element, a binding site for steroid hormone receptors, located upstream of its 5' UTR.
Description
Recombinant human ADH6, produced in E. coli, is a single polypeptide chain consisting of 399 amino acids (residues 1-375) with a molecular weight of 42.4 kDa. This protein includes a 24 amino acid His-tag fused at the N-terminus and is purified using specialized chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized through filtration.
Formulation
The ADH6 solution is provided at a concentration of 0.5 mg/ml and contains the following components: 20 mM Tris-HCl buffer (pH 8.0), 30% glycerol, 0.15 M NaCl, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the ADH6 solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). It is important to minimize repeated freeze-thaw cycles.
Purity
The purity of ADH6 is determined to be greater than 90% based on SDS-PAGE analysis.
Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.

Product Science Overview

Introduction

Alcohol Dehydrogenase 6 (ADH6) is a member of the alcohol dehydrogenase family, which plays a crucial role in the metabolism of alcohols in the human body. This enzyme is encoded by the ADH6 gene and is classified as a Class V alcohol dehydrogenase. The recombinant form of this enzyme is produced using recombinant DNA technology, which allows for the expression of the human ADH6 protein in various host systems, such as Escherichia coli.

Gene and Protein Structure

The ADH6 gene is located on chromosome 4 and encodes a protein that consists of 375 amino acids . The protein belongs to the zinc-containing alcohol dehydrogenase family and has a unique structure compared to other members of the ADH family . The enzyme contains multiple unique residues and structural properties that are not observed in other ADH proteins .

Expression and Function

ADH6 is primarily expressed in the liver and stomach, with higher expression levels observed in the liver of both fetuses and adults . The enzyme catalyzes the NAD-dependent oxidation of primary alcohols to their corresponding aldehydes and secondary alcohols to their corresponding ketones . This activity is essential for the metabolism of various substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products .

Recombinant Production

Recombinant human ADH6 protein is produced using Escherichia coli as the expression system . The recombinant protein is typically purified to a high degree of purity (>90%) and is suitable for various applications, including SDS-PAGE and mass spectrometry . The recombinant form of ADH6 allows researchers to study the enzyme’s structure, function, and role in various metabolic pathways in a controlled laboratory setting.

Clinical and Research Implications

ADH6 has been associated with several diseases, including anterior dislocation of the lens and calvarial doughnut lesions with bone fragility . The enzyme is also involved in important metabolic pathways, such as the oxidation by cytochrome P450 and the pharmacodynamics of cyclophosphamide . Understanding the function and regulation of ADH6 can provide insights into its role in these diseases and pathways, potentially leading to the development of new therapeutic strategies.

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