Histone Code Peptide Microarrays

Product Code: His_MA_01

Extensive peptide library covering all known natural variants of histone sequences and modifications displayed on one microarray (> 3800 peptides).Amino Acid Sequence: See Product DocumentationAmount: 1 peptide microarray (each peptide is deposited 1x per subarray, 3 subarrays per slide) + dummy slides and spacers (needed for manual incubation) Delivery Format: Peptides immobilized onto glass slide (3 x 1 inches; 75 by 25 mm)Application(s): Binding experiments, Substrate identification, Antibody epitope discovery, Substrate SpecifityIndication(s)/Topic(s): Cancer, Histone Deacetylase, Histones, Gene regulation and expression, Epigenetics, Cell signaling, NucleosomeDelivery Time: 10 - 12 days

Histone Code Peptide MicroarrayAs histones are a major focus of epigenetics, JPTs computational scientists compiled this unique library of synthetic post-translationally modified and unmodified human histone peptides that is now available on a single peptide microarray or as individual biotinylated peptides. The peptide library consists of more than 1400 20mer peptides from Histone H1, H2A, H2B, H3 and H4. Peptides carry PTMs at reported sites (e.g. acetylation, methylation, phosphorylation, citrullination...) in various combinations representing all potential variants. This library is supplemented by 2444 peptides from an overlapping peptide scan through histone proteins carrying no or single modifications at reported sites.

Benefits of JPTs Histone Code Peptide Microarrays- Get hundreds of identical microarray copies- Small amounts of your precious samples are needed for incubation- Applicable to a variety of biological samples (e.g. serum, lysate, purified proteins, antibodies)- Low background on glass surface, read-out via fluorescence- Unprecedented resolution for mapping of protein-histone interactions due to coverage of natural sequence variants - Screen thousands of potential peptide substrates economically

Histone Code Peptide Microarrays

Selected References\"Histone H2A and H4 N-Terminal Tails are Positioned by the MEP50 WD-Repeat Protein for Efficient Methylation by the PRMT5 Arginine Methyltransferase\"Burgos et al., J. Biol. Chem. (2015) - PMID: 25713080 \"H3K23me2 is a New Heterochromatic Mark in Caenorhabditis elegans\" Vandamme et al., Nucleic Acids Res. (2015) - PMID: 26476455\"Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity\"Ho et al, PLOS ONE (2013) - PMID:23451136\"Use of High-Density Histone Peptide Arrays for Parsing the Specificity of a Histone-Modifying Enzyme Complex\"Shechter et al. Application Note (2013) (full text)

Application Notes\"Use of High-Density Histone Peptide Arrays for Parsing the Specificity of a Histone-Modifying Enzyme Complex\"Shechter et al. Application Note (2013) (full text)\"Comprehensive Characterization of Antibodies Directed towards Epigenetic Histone-Modifications\" Masch et al. Application Note (2015) (full text)

Testimonial“JPTs new extremely high-density histone peptide array is a dramatic leap forward for analysis of the histone code hypothesis. The complete sequence coverage across core histones and histone variants as well as the presence of common and rare histone posttranslational modifications – alone and in combination – makes this an unparalleled tool for studying the “writers” and “readers” of the histone code. My laboratory has used these arrays to ask the sequence and PTM dependence of a histone writer enzyme and we have discovered an activity specifying code that will keep us busy for years to come.”David Shechter, PhD (Department of Biochemistry, Albert Einstein College of Medicine, YU, NY, USA)

Histone Code Peptide Microarrays