ACOT8 Human

Acyl-CoA Thioesterase 8 Human Recombinant
Cat. No.
BT18184
Source
Escherichia Coli.
Synonyms
Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Acyl-CoA Thioesterase 8 (ACOT8) belongs to a family of enzymes responsible for breaking down acyl-CoAs into free fatty acids and coenzyme A (CoASH). This function enables ACOT8 to potentially control the levels of acyl-CoAs, free fatty acids, and CoASH within cells. ACOT8 plays a role in Nef-induced down-regulation of CD4 and competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrates like chenodeoxycholoyl-CoA. ACOT8 shows a preference for acyl-CoAs with medium-length fatty acid chains.
Description
Recombinant human ACOT8, expressed in E.coli, is a single, non-glycosylated polypeptide chain. It consists of 342 amino acids (amino acids 1-319) and has a molecular weight of 38.3kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The ACOT8 solution is provided at a concentration of 1mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 40% glycerol, and 2mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the product can be kept at 4°C. For longer storage, it should be frozen at -20°C. Adding a carrier protein such as 0.1% HSA or BSA is recommended for extended storage. Repeated freezing and thawing should be avoided.
Purity
Purity is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES KL.

Product Science Overview

Biological Properties

ACOT8 exhibits substrate specificity mainly for short- to long-chain acyl-CoA. It is known to hydrolyze a wide range of acyl-CoA substrates, including those with saturated and unsaturated fatty acids. The enzyme’s activity is crucial for maintaining cellular lipid homeostasis and energy production.

Expression Patterns and Tissue Distribution

ACOT8 is ubiquitously expressed in various tissues, with higher expression levels observed in metabolically active tissues such as the liver, kidney, and heart. Its expression is regulated by various factors, including nutritional status and hormonal signals, which modulate its activity to meet the metabolic demands of the organism.

Biological Functions

The primary function of ACOT8 is to hydrolyze acyl-CoA thioesters, thereby releasing free fatty acids and CoA. This reaction is vital for several metabolic processes, including:

  • Energy Production: By hydrolyzing acyl-CoA, ACOT8 helps in the mobilization of fatty acids, which can be oxidized to produce energy.
  • Lipid Metabolism: ACOT8 regulates the levels of acyl-CoA and free fatty acids, influencing lipid synthesis and degradation pathways.
  • Detoxification: The enzyme also plays a role in detoxifying acyl-CoA derivatives that may accumulate to toxic levels within cells.
Modes of Action

ACOT8 functions by catalyzing the hydrolysis of the thioester bond in acyl-CoA molecules. This reaction is facilitated by the enzyme’s active site, which binds to the acyl-CoA substrate and stabilizes the transition state, allowing the cleavage of the thioester bond. The enzyme’s activity is regulated by various factors, including the availability of substrates and cofactors, as well as post-translational modifications.

Regulatory Mechanisms

The expression and activity of ACOT8 are regulated by multiple mechanisms:

  • Transcriptional Regulation: The gene encoding ACOT8 is regulated by transcription factors that respond to metabolic cues, such as nutrient availability and hormonal signals.
  • Post-Translational Modifications: ACOT8 can undergo modifications such as phosphorylation, which can alter its activity and stability.
  • Feedback Inhibition: The enzyme’s activity can be modulated by feedback inhibition, where the accumulation of reaction products or intermediates can inhibit its function.
Clinical Significance

ACOT8 has been implicated in various metabolic disorders and diseases. For instance, alterations in its expression and activity have been associated with conditions such as obesity, diabetes, and cancer. In particular, ACOT8 has been identified as a potential biomarker for clear cell renal cell carcinoma, where its expression levels correlate with disease progression and prognosis .

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