As histones are a major focus of epigenetics, JPT’s Bioinformaticians have compiled a unique library of thousands of post-translationally modified and unmodified histone peptides. We offer this peptide library immobilized on Histone Code Peptide Microarrays or Histone Code Peptide ELISA and as stable isotope labeled and quantified SpikeTides™ Set.
Properties of the Histone Peptide Library:
- Peptides from Histone H1, Histone H2A, Histone H2B, Histone H3 and Histone H4
- Post-translational modifications in various combinations representing many potential variants
- Post-translational modifications: Lys[acetylation, (mono-, di-, tri-) methylation, butyrylation, propylation, succinylation, malonylation]; Arg[mono-methylation, di-methylation (symmetric and asymmetric], Citrullin, and Ser, Thr, Tyr [phosphorylation]
- Use our custom peptide synthesis for any histone peptide we do not have in stock.
Histone Code Peptide Microarrays
Histone Code Peptide ELISA
Histone Peptide Sets
- Mapping and validation of protein-histone interactions including PTM dependencies
- Testing of histone antibodies including PTM dependencies
- Enzymatic activity profiling including PTMs
Histone PTM Profiling Reveals Global and Specific Responses to Systematic Enzyme Ablations
by Feller et al.
Comprehensive Characterization of Antibodies Directed towards Epigenetic Histone-Modifications
by Masch et al.
Use of High-Density Histone Peptide Arrays for Parsing the Specificity of a Histone-Modifying Enzyme Complex
by Shechter et al.
- Coverage of all known natural variants (sequence variants and PTMs)
- Identical sequences on peptide microarray and as peptide ELISA for reliable and checkable results
- All-in-one Histone Code Analysis Service for antibody specificity & histone reader profiling
- Guaranteed purity for peptide ELISA
" JPT’s 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 post-translational 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, Yeshiva University, NY, USA