ACAA1 Human

Acetyl-COA Acyltransferase Human Recombinant
Cat. No.
BT2126
Source
Escherichia Coli.
Synonyms
ACAA, PTHIO, THIO.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec'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.
Shipped with Ice Packs
In Stock

Description

ACAA1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (27-424 a.a.) and having a molecular mass of 43.8 kDa. The ACAA1 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
ACAA1, an enzyme belonging to the thiolase family, plays a crucial role in lipid metabolism. This peroxisome-localized enzyme catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA within the fatty acid oxidation pathway. Exhibiting high enzymatic activity in rat liver, kidney, intestine, and white adipose tissue, ACAA1 deficiency is linked to pseudo-Zellweger syndrome.
Description
Recombinant Human ACAA1, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 419 amino acids (27-424 a.a.). With a molecular mass of 43.8 kDa, it features a 21 amino acid His-Tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The ACAA1 protein solution is provided at a concentration of 1 mg/ml and contains 20mM Tris pH 8.0, 0.1M NaCl, 1mM DTT, and 20% glycerol.
Stability
While stable at 4°C for up to one week, ACAA1 Human should be stored at -18°C or below to ensure long-term stability. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.
Synonyms
ACAA, PTHIO, THIO.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLSGAPQASA ADVVVVHGRR TAICRAGRGG FKDTTPDELL SAVMTAVLKD VNLRPEQLGD ICVGNVLQPG AGAIMARIAQ FLSDIPETVP LSTVNRQCSS GLQAVASIAG GIRNGSYDIG MACGVESMSL ADRGNPGNIT SRLMEKEKAR DCLIPMGITS ENVAERFGIS REKQDTFALA SQQKAARAQS KGCFQAEIVP VTTTVHDDKG TKRSITVTQD EGIRPSTTME GLAKLKPAFK KDGSTTAGNS SQVSDGAAAI LLARRSKAEE LGLPILGVLR SYAVVGVPPD IMGIGPAYAI PVALQKAGLT VSDVDIFEIN EAFASQAAYC VEKLRLPPEK VNPLGGAVAL GHPLGCTGAR QVITLLNELK RRGKRAYGVV SMCIGTGMGA AAVFEYPGN.

Product Science Overview

Introduction

Acetyl-CoA Acyltransferase, also known as thiolase, is an enzyme that plays a crucial role in the metabolism of fatty acids and the biosynthesis of ketone bodies. This enzyme catalyzes the thiolytic cleavage of 3-ketoacyl-CoA into acetyl-CoA and a shortened acyl-CoA molecule. The human recombinant form of Acetyl-CoA Acyltransferase is produced using recombinant DNA technology, allowing for the study and application of this enzyme in various biochemical and medical research fields.

Structure and Function

Acetyl-CoA Acyltransferase is a homotetrameric enzyme, meaning it consists of four identical subunits. Each subunit contains an active site where the catalytic reaction occurs. The enzyme’s primary function is to facilitate the breakdown of fatty acids through β-oxidation, a process that generates acetyl-CoA, which can then enter the citric acid cycle to produce energy.

In addition to its role in fatty acid metabolism, Acetyl-CoA Acyltransferase is involved in the synthesis of ketone bodies, which are important energy sources during periods of fasting or low carbohydrate intake. The enzyme’s activity is regulated by various factors, including substrate availability and post-translational modifications.

Recombinant Production

The production of human recombinant Acetyl-CoA Acyltransferase involves the insertion of the human gene encoding the enzyme into a suitable expression vector. This vector is then introduced into a host organism, such as Escherichia coli or yeast, which expresses the enzyme. The recombinant enzyme is subsequently purified using techniques such as affinity chromatography, ensuring high purity and activity.

Recombinant production offers several advantages, including the ability to produce large quantities of the enzyme, consistency in enzyme activity, and the elimination of potential contaminants found in enzymes extracted from natural sources.

Applications

Human recombinant Acetyl-CoA Acyltransferase has numerous applications in research and medicine. It is used to study the mechanisms of fatty acid metabolism and ketogenesis, providing insights into metabolic disorders such as diabetes and obesity. The enzyme is also employed in drug discovery and development, where it serves as a target for potential therapeutic agents aimed at modulating its activity.

Furthermore, Acetyl-CoA Acyltransferase is utilized in the production of biofuels and bioplastics, where its ability to catalyze the formation of acetyl-CoA is harnessed to generate renewable energy sources and environmentally friendly materials.

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