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Anti-methyl-Histone H3 Lysine 9 (H3K9me2) AlphaLISA Acceptor Beads, 250 µg

AlphaLISA® Acceptor beads conjugated to an antibody against human histone H3 di-methylated at lysine 9 (H3K9me2). These beads can be used for no-wash AlphaLISA epigenetic writer and eraser assays.

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For research use only. Not for use in diagnostic procedures.

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AL117C
250 µg
874.00 GBP
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AL117M
5 mg
4540.00 GBP
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AL117R
25 mg
15910.00 GBP
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Detail Information

AlphaLISA® Acceptor beads designed to detect human Histone H3 di-methylated at lysine 9 (H3K9me2) in a homogeneous AlphaLISA assay. Broad species cross-reactivity is expected based on sequence similarity. Source of antibody: monoclonal.

The anti-methyl-Histone H3 Lysine 9 (H3K9me2) AlphaLISA Acceptor beads were used for the development and optimization of a G9a histone H3 methyltransferase assay using a biotinylated Histone H3(1-21) peptide as substrate. A technical note describing the assay is available in our product literature.

Features:

  • No-wash epigenetic assay
  • Fully-validated mark specificity
  • Substrate flexibility (peptide, protein, histone, nucleosome substrates)
  • Easy-to-automate
  • Fast assay optimization

AlphaScreen® and AlphaLISA® are bead-based assay technologies used to study biomolecular interactions in a microplate format. The acronym "Alpha" stands for amplified luminescent proximity homogeneous assay. As the name implies, some of the key features of these technologies are that they are non-radioactive, homogeneous proximity assays. Binding of molecules captured on the beads leads to an energy transfer from one bead to the other, ultimately producing a luminescent/fluorescent signal. To understand how a signal is produced, one must begin with an understanding of the beads. AlphaScreen and AlphaLISA assays require two bead types: Donor beads and Acceptor beads. Each bead type contains a different proprietary mixture of chemicals, which are key elements of the AlphaScreen technology. Donor beads contain a photosensitizer, phthalocyanine, which converts ambient oxygen to an excited and reactive form of O2, singlet oxygen, upon illumination at 680 nm. Please note that singlet oxygen is not a radical; it is molecular oxygen with a single excited electron. Like other excited molecules, singlet oxygen has a limited lifetime prior to falling back to ground state. Within its 4 µsec half-life, singlet oxygen can diffuse approximately 200 nm in solution. If an Acceptor bead is within that proximity, energy is transferred from the singlet oxygen to thioxene derivatives within the Acceptor bead, subsequently culminating in light production at 520-620 nm (AlphaScreen) or at 615 nm (AlphaLISA). In the absence of an Acceptor bead, singlet oxygen falls to ground state and no signal is produced. This proximity-dependent chemical energy transfer is the basis for AlphaScreen's homogeneous nature.

Specifications

Antibody Conjugates Anti-H3K9me2
Automation Compatible Yes
Bead Type or Core Bead Type AlphaLISA Acceptor
Detection Method Alpha
Experimental Type In vitro
Molecular Modification Methylation
Product Brand Name AlphaLISA
Shipping Condition Blue Ice
Unit Size 250 µg
Resources, Events & More
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Brochure

Handle Large Biomolecular Interactions With Ease

The interactions and bindingof proteins are implicated in a large number of biological processes. The needfor an efficient, highly sensitive assay to study large protein interactions is increasingly important. Alpha Technology is a highly flexible, homogeneous, no-wash assay ideal for the measurement of protein interactions and complexes as large as 200 nm in size

PDF 798 KB

Guide

Alpha Protein-Protein Interaction Quick Start Guide

Alpha has been used to study a wide variety of interactions, including protein:protein, protein:peptide, protein:DNA, protein:RNA, protein:carbohydrate, protein:small molecule, receptor:ligand, and nuclear receptor:ligand interactions. Both cell-based and biochemical interactions have been monitored, and applications such as phage display, ELISA, and EMSA (electrophoretic mobility shift assay) have been adapted to Alpha.

PDF 380 KB

Poster

AlphaLISA Assays are Homogeneous Sensitive Immunoassays for Detection of Analytesin a Variety of Biological Matrices

The AlphaLISA® assay is a homogeneous immunoassay alternative to classical ELISA. AlphaLISA assays were originally utilized to detect analytesin cell cultures upernatants or serum/plasma samples.

PDF 273 KB
Development of Homogeneous Non-radioactive Assays for Studying Histone H3 Methyltransferases and Demethylases

Anti-mark antibodies coupled to AlphaLISA Acceptor beads or labeled with LANCE Ultra europium chelate were used for the successful optimization of robust and, sensitive epigenetic assays using histone H3-derived peptides as substrates.

PDF 381 KB
Development of Homogeneous Proximity Assays for JMJD2A/2C Histone Demethylases

In eukaryotes, the covalent modification of histones has a crucial role in chromatin architecture and plays an important part in a plethora of cellular processes, from chromatinre modeling and transcriptional regulation, to DNA repair and cell cycle control.

PDF 289 KB
Development of a Non-Radioactive, No-Wash Biochemical Assay for High-Throughput Screening of Small Molecule Modulators of DNA MethyltransferasesNathalie

Covalen modification of DNA through methylation is catalyzed by specific DNA methyltransferases (DNMTs).

PDF 386 KB

Technical Note

AlphaLISA G9a Histone H3-Lysine N-methyltransferase Assay

The AlphaLISA technology allows performing no-wash homogeneous proximity immunoassays using Alpha Donor and AlphaLISA Acceptor beads. In this technical note, we present the optimization of an epigenetic enzymatic assay using a biotinylated histone H3-derived peptide as substrate.

PDF 667 KB