AlphaLISA® Acceptor beads conjugated to an antibody against human histone H3 di-methylated at lysine 36 (H3K36me2). These beads can be used for no-wash AlphaLISA epigenetic writer and eraser assays.
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|Product Number||Unit Size||List Price||Your Price||Quantity|
|AL123C||250 µg||1339.00 USD|
|AL123M||5 mg||7000.00 USD|
|AL123R||25 mg||24400.00 USD|
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AlphaLISA® Acceptor beads are designed to detect human Histone H3 peptide substrate that is di-methylated at lysine 36 (H3K36me2) 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 36 (H3K36me2) AlphaLISA Acceptor beads were used for the development and optimization of a JMJD2a demethylase assay using a biotinylated Histone H3 (21-44) peptide trimethylated at lysine 36 as substrate. A technical note describing the assay is available in our product literature.
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.
Disclaimer: For research use only. Not for use in diagnostic procedures.
|Bead Type or Core Bead Type||AlphaLISA Acceptor|
|Experimental Type||In vitro|
|One Unit Contains||250 µg|
|Product Brand Name||AlphaLISA|
|Shipping Condition||Blue Ice|
|Unit Size||250 µg|
|Resource Type||File Name||File Format|
|Brochure||Handle Large Biomolecular Interactions With Ease||PDF 798 KB|
|Guide||Alpha Protein-Protein Interaction Quick Start Guide||PDF 380 KB|
|Technical Note||AlphaLISA JMJD2A Histone H3-Lysine 36 Demethylase Assay||PDF 616 KB|
|Technical Note||AlphaLISA SET7/9 Histone H3-Lysine N-methyltransferase Assay||PDF 662 KB|
|Poster||AlphaLISA Assays are Homogeneous Sensitive Immunoassays for Detection of Analytesin a Variety of Biological Matrices||PDF 273 KB|
|Poster||Development of High-Throughput Assays to Study Histone H3K4 Methyltransferases & H3K9 Methyl- and Acetyltransferases||PDF 386 KB|
|Poster||Development of High-Throughput Assays to Study Methylases, Demethylases and Deacetylases Targeting Histone H3K4, H3K27 and H3K36 Residues||PDF 359 KB|
|Poster||Development of Homogeneous Non-radioactive Assays for Studying Histone H3 Methyltransferases and Demethylases||PDF 381 KB|
|Poster||Development of Homogeneous Proximity Assays for JMJD2A/2C Histone Demethylases||PDF 289 KB|
|Poster||Development of a Non-Radioactive, No-Wash Biochemical Assay for High-Throughput Screening of Small Molecule Modulators of DNA MethyltransferasesNathalie||PDF 386 KB|