ACOT11 Human

Acyl-CoA Thioesterase 11 Human Recombinant
Cat. No.
BT17913
Source
Escherichia Coli.
Synonyms
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
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.
Shipped with Ice Packs
In Stock

Description

ACOT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 268 amino acids (19-250 a.a) and having a molecular mass of 29.9kDa. ACOT11 is fused to a 36 amino acid His-tag at N-terminus.

Product Specs

Introduction
ACOT11, a member of the acyl-CoA thioesterase family, catalyzes the conversion of activated fatty acids to their corresponding non-esterified fatty acids and coenzyme A. Studies in mice have shown that the expression of an ACOT11 homolog in brown adipose tissue is increased by cold temperatures and decreased by warm temperatures. Obesity-resistant mice exhibit elevated expression levels compared to obesity-prone mice, suggesting a role for ACOT11 in obesity. ACOT11 demonstrates acyl-CoA thioesterase activity towards both medium-chain (C12) and long-chain (C18) fatty acyl-CoA substrates.
Description
Recombinant human ACOT11, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising the topological domain (amino acids 19-250) and a 36-amino acid His-tag at the N-terminus. The protein has a molecular weight of 29.9 kDa.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
ACOT11 is supplied as a 1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSNRTS RKSALRAGND SAMADGEGYR NPTEVQMSQL VLPCHTNQRG ELSVGQLLKW IDTTACLSAE RHAGCPCVTA SMDDIYFEHT ISVGQVVNIK AKVNRAFNSS MEVGIQVASE DLCSEKQWNV CKALATFVAR REITKVKLKQ ITPRTEEEKM EHSVAAERRR MRLVYADTIK DLLANCAIQG DLESRDCSRM VPAEKTRVES VELVLPPHAN HQGNTFGGQI MAWMENVA

Product Science Overview

Function and Importance

ACOT11 is involved in the regulation of intracellular levels of acyl-CoA and free fatty acids, which are essential for various metabolic processes. By maintaining the balance between these molecules, ACOT11 helps regulate energy production, lipid synthesis, and degradation . This enzyme is particularly important in tissues with high metabolic activity, such as the liver, where it contributes to fatty acid oxidation and ketogenesis .

Structure and Mechanism

ACOT11 belongs to the type II acyl-CoA thioesterase family, which is characterized by the “hot dog” fold structure . This structural motif is crucial for the enzyme’s catalytic activity. The enzyme’s active site binds to acyl-CoA substrates, facilitating the hydrolysis reaction that releases free fatty acids and CoASH .

Recombinant Production

Human recombinant ACOT11 is produced using recombinant DNA technology, which involves inserting the human ACOT11 gene into a suitable expression system, such as Escherichia coli . This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant ACOT11 retains the same biochemical properties and functions as the naturally occurring enzyme, making it a valuable tool for studying lipid metabolism and developing potential treatments for metabolic disorders .

Research and Applications

Research on ACOT11 has expanded our understanding of lipid metabolism and its role in various physiological and pathological conditions. Studies have shown that ACOT11 is involved in the regulation of lipid homeostasis, energy metabolism, and cellular signaling . Dysregulation of ACOT11 activity has been linked to metabolic disorders such as obesity, diabetes, and cardiovascular diseases .

In addition to its physiological roles, ACOT11 is also being explored as a potential therapeutic target. Modulating ACOT11 activity could provide new strategies for treating metabolic diseases by altering lipid metabolism and improving energy balance .

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