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AB204536

Acetyltransferase Activity Assay Kit (Fluorometric)

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(5 Publications)

Acetyltransferase Activity Assay Kit ab204536 is a homogeneous mix-and-read fluorescent assay for the determination of any acetyl-CoA dependent acetyltransferase activity.

View Alternative Names

ACTL, ACAT2, Acetyl-CoA transferase-like protein, Cytosolic acetoacetyl-CoA thiolase

3 Images
Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)
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Supplier Data

Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)

Example Kinetic Assay Results.

100nM CAT was tested with 100μM Chloramphenicol substrate in the kinetic assay format. Mean relative fluorescence was plotted against the stop time interval to generate this graph. Obtained using Abcam's Acetyltransferase Activity Assay Kit (Fluorometric) (ab204536).

Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)
  • FuncS

Supplier Data

Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)

Chloramphenicol acetyltransferase (CAT) titration in acetyltransferase assay.

Chloramphenicol acetyltransferase (CAT) was titered in the assay using 100μM of the Substrate chloramphenicol. Serial dilutions of the enzyme were prepared in Transferase Assay Buffer. Mean relative fluorescence was plotted against CAT concentration to generate the following graph.

This is for illustration purposes only.

The investigator must titrate their enzyme / substrate system in the assay.

Based on this titration data, the acetyltransferase concentration of 100nM produces a maximum signal within the detection range of the plate reader, with a signal to noise ratio sufficient for easy detection of altered enzyme activity.

Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)
  • FuncS

Supplier Data

Functional Studies - Acetyltransferase Activity Assay Kit (Fluorometric) (AB204536)

Typical inhibition curve obtained using Abcam's Acetyltransferase Activity Assay Kit (Fluorometric) (ab204536)

Key facts

Detection method

Fluorescent

Sample types

Purified protein, Inhibitor compounds

Assay Platform

Microplate reader

Reactivity data

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Product details

Acetyltransferase Activity Assay Kit (Fluorometric) (ab204536) is a homogeneous mix-and-read fluorescent assay for the determination of any acetyl-CoA dependent acetyltransferase activity. It is suitable for end-point or kinetic read options, which is ideal for determining mechanism of action, kinetics, and screening candidate compounds. The assay is amendable to HTS and miniaturization.

This assay is a complete kit for the screening of candidate compounds that can alter normal acetyltransferase activity. For use with purified in vitro samples.

Acetylation is an important covalent molecular modification. Originally identified as the method by which certain bacteria were able to deactivate anti-microbial compounds, acetylation is now also known as an important partitioning and signaling modification.

Acetyltransferases are enzymes that covalently transfer an acetyl group from a donor molecule (Acetyl CoA) to an acceptor. Acetyl CoA serves as a universal donor while the acceptor varies with the acetyltransferase. Acceptors include histones, kinases, transcription factors, receptors, neurotransmitter precursors like choline and serotonin, and anti-microbial agents like chloramphenicol and fluoroquinones. Acetylation can signal an increase or decrease in activity based on the context of the message. Frequently located at critical junctions in metabolic pathways, Acetyltransferases and their regulation have become attractive therapeutic targets to treat everything from insomnia to cancer.

What's included?

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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
Multi
Appropriate long-term storage conditions
Multi
Storage information
Please refer to protocols

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ACAT2 also known as Acetyl-CoA acetyltransferase is an enzyme that plays a role in lipid metabolism catalyzing the conversion of two molecules of acetyl-CoA into acetoacetyl-CoA. It shares functionality with other acetyltransferases such as chloramphenicol acetyltransferase. ACAT2 has a molecular mass of approximately 41 kDa. Expression of ACAT2 is mainly in the liver and the cytosol of cells involved in sterol regulatory processes. It functions as a homotetramer and is essential in maintaining cellular levels of acetyl-CoA and related metabolites.
Biological function summary

This enzyme facilitates the synthesis of cholesterol and ketone bodies essential processes for cellular energy balance. ACAT2 works as an independent enzyme rather than as a component of a multi-enzyme complex unlike some other acetyltransferases. By managing acetyl-CoA levels it supports energy homeostasis and lipogenesis providing substrates for downstream processes that are critical for sustaining cellular function and response to energy demands.

Pathways

The acetyl-transfer reactions catalyzed by ACAT2 are integral to the cholesterol biosynthesis and ketogenesis pathways. These pathways are important for energy balance and lipid modification. Within these pathways ACAT2 acts in close relation with HMG-CoA synthase an important player in cholesterol biosynthesis. The enzyme’s actions provide acetoacetyl-CoA which is a substrate for the production of HMG-CoA highlighting its role in maintaining metabolic flux.

ACAT2's role in cholesterol metabolism links it to atherosclerosis and non-alcoholic fatty liver disease (NAFLD). Disruption in its function can lead to elevated levels of cholesterol and triglycerides risk factors for atherosclerosis. In NAFLD ACAT2 expression may influence lipid accumulation in the liver contributing to disease pathogenesis. Its connection with other proteins like LDL receptor and apolipoprotein B through cholesterol metabolism emphasizes its potential as a therapeutic target for managing lipid-related disorders.

Product protocols

Target data

Involved in the biosynthetic pathway of cholesterol.
See full target information ACAT2

Additional targets

ACAT1

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Signal transduction and targeted therapy 6:325 PubMed34465723

2021

A novel missense variant in ACAA1 contributes to early-onset Alzheimer's disease, impairs lysosomal function, and facilitates amyloid-β pathology and cognitive decline.

Applications

Unspecified application

Species

Unspecified reactive species

Rongcan Luo,Yu Fan,Jing Yang,Maosen Ye,Deng-Feng Zhang,Kun Guo,Xiao Li,Rui Bi,Min Xu,Lu-Xiu Yang,Yu Li,Xiaoqian Ran,Hong-Yan Jiang,Chen Zhang,Liwen Tan,Nengyin Sheng,Yong-Gang Yao

Antimicrobial agents and chemotherapy 65: PubMed33106268

2020

Acetylation of Isoniazid Is a Novel Mechanism of Isoniazid Resistance in Mycobacterium tuberculosis.

Applications

Unspecified application

Species

Unspecified reactive species

K B Arun,Aravind Madhavan,Billu Abraham,M Balaji,K C Sivakumar,P Nisha,R Ajay Kumar

BioMed research international 2019:8714363 PubMed31828139

2019

Atorvastatin Improves Hepatic Lipid Metabolism and Protects Renal Damage in Adenine-Induced Chronic Kidney Disease in Sprague-Dawley Rats.

Applications

Unspecified application

Species

Unspecified reactive species

Hardik Ghelani,Valentina Razmovski-Naumovski,Vamsi Inampudi,Dennis Chang,Srinivas Nammi

Cell chemical biology 24:133-140 PubMed28132892

2017

Mapping Proteome-wide Targets of Glyphosate in Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Breanna Ford,Leslie A Bateman,Leilani Gutierrez-Palominos,Robin Park,Daniel K Nomura

ACS chemical biology 12:635-642 PubMed28094496

2017

Chemoproteomic Profiling of Acetanilide Herbicides Reveals Their Role in Inhibiting Fatty Acid Oxidation.

Applications

Unspecified application

Species

Unspecified reactive species

Jessica L Counihan,Megan Duckering,Esha Dalvie,Wan-Min Ku,Leslie A Bateman,Karl J Fisher,Daniel K Nomura
View all publications
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