Key features and details
- Assay type: Enzyme activity
- Detection method: Colorimetric
- Platform: Microplate reader
- Sample type: Nuclear Extracts, Purified protein, Tissue Lysate
Product nameHistone Acetyltransferase Activity Assay Kit (Colorimetric)
See all Histone acetyltransferase kits
Sample typeNuclear Extracts, Purified protein, Tissue Lysate
Assay typeEnzyme activity
Species reactivityReacts with: Mammals, Other species
Abcam's Histone Acetyltransferase Activity Assay Kit offers a convenient, nonradioactive system for a rapid and sensitive detection of HAT activity in mammalian samples. The kit utilizes active Nuclear Extract (NE) as a positive control and acetyl-CoA as a cofactor. Acetylation of peptide substrate by active HAT releases the free form of CoA which then serves as an essential coenzyme for producing NADH. NADH can easily be detected spectrophotometrically upon reacting with a soluble tetrazolium dye. The detection can be continuous and suitable for kinetic studies. The kit provides a simple, straightforward protocol for a complete assay.
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HAT assay protocol summary:
- add samples to wells
- add HAT assay mix
- incubate for 1-4 hrs
- analyze with microplate reader
This product is manufactured by BioVision, an Abcam company and was previously called K332 HAT Activity Colorimetric Assay Kit. K332-100 is the same size as the 100 test size of ab65352.
Histone acetyltransferases (HATs) have been implicated to play a crucial role in various cellular functions, such as gene transcription, differentiation, and proliferation.
Abcam has not and does not intend to apply for the REACH Authorisation of customers’ uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Storage instructionsStore at -80°C. Please refer to protocols.
Components Identifier 100 tests 2X HAT Assay Buffer Amber 1 x 7.5ml HAT Reconstitution Buffer Clear 1 x 1.8ml HAT Substrate I Blue 1 vial HAT Substrate II Red 1 vial NADH Generating Enzyme Green 1 x 800µl Nuclear Extract (4 mg/ml ) Violet 1 x 50µl
RelevanceHistone acetyltransferases (HAT) are enzymes that acetylate conserved lysine amino acids on histone proteins. They have been implicated to play a crucial role in various cellular functions, such as gene transcription, differentiation, and proliferation.
Cellular localizationCytoplasmic and Nuclear. Note=Nuclear in S-phase cells and cytoplasmic.
- Histone acetyltransferase 1
HAT activity in NIH3T3 cells, which were transfected with the desired plasmids by using Lipofectamine 2000. After 24 hours from transfection, the nuclear protein was extracted and the Histone acetyltransferase activity was measured by using ab65352.
Histone acetylation activity assay for L.donovani cells over-expressing HAT1, HAT2, HAT3 and HAT4. The activities were compared to wild-type (WT) cells and pLPneo2 (vector) only transfected cells. The relative activity was determined using Histone Acetyltransferase acitvity assay kit (ab65352).
Analysis of Histone Acetyltransferase Activity in HeLa Nuclear Extract using ab65352. HeLa nuclear extract in various amounts was incubated with HAT substrate. Activity was analyzed in a micro plate reader at 440 nm according to the kit instructions.
ab65352 has been referenced in 44 publications.
- Rocha MA et al. RNAP II produces capped 18S and 25S ribosomal RNAs resistant to 5'-monophosphate dependent processive 5' to 3' exonuclease in polymerase switched Saccharomyces cerevisiae. BMC Mol Cell Biol 23:17 (2022). PubMed: 35399070
- Zhang K et al. FAM135B sustains the reservoir of Tip60-ATM assembly to promote DNA damage response. Clin Transl Med 12:e945 (2022). PubMed: 35979619
- Davegårdh C et al. VPS39-deficiency observed in type 2 diabetes impairs muscle stem cell differentiation via altered autophagy and epigenetics. Nat Commun 12:2431 (2021). PubMed: 33893273
- Chen Q et al. Acetyl-CoA derived from hepatic mitochondrial fatty acid ß-oxidation aggravates inflammation by enhancing p65 acetylation. iScience 24:103244 (2021). PubMed: 34746707
- Waghmare SG et al. Histone Acetylation Dynamics during In Vivo and In Vitro Oocyte Aging in Common Carp Cyprinus carpio. Int J Mol Sci 22:N/A (2021). PubMed: 34204879