JPT/NB Histone Peptide H3 71:87 K79me1 (H3.12)/SP-His_nb_129/

NB Histone Peptide H3 71:87 K79me1 (H3.12)

Product Code: SP-His_nb_129

Synthetic Histone peptide carrying 1 modification (K79me1) derived from human Histone H3.12 (Swiss-Prot IDs: Q71DI3, P68431).
Amino acid sequence: H-VREIAQDF-Lys(Me)-TDLRFQSS-NH2
Amount: 1 vial containing 30 nmol (approx. 100 µg)
Purity: >70% (HPLC-MS)
Delivery format: Freeze-dried in amber type glass vials
Application(s): Enzyme kinetics, Substrate Specifity, Substrate identification, Competition experiments, Co-crystallization, NMR studies
Indication(s)/Topic(s): Cancer, Kinase, Methyltransferase, Acetyltransferase, Histones, Phosphatase, Gene regulation and expression, Epigenetics, Cell signaling, Nucleosome
Delivery time: 10-12 days

JPT's Non-Biotinylated Histone Code Peptides
In addition to our biotinylated histone peptides, JPT offers a non-biotinylated library of synthetic posttranslationally modified and unmodified human histone peptides that is now available as individual peptides. The peptide library consists of 160 peptides from different histone families. Peptides carry PTMs at reported sites (e.g. acetylation, methylation, phosphorylation...) in various combinations representing natural variants.
JPT's highly skilled and committed scientific staff ensures that the most appropriate methods and techniques are selected for every synthesis project. All of JPT's catalog peptides are provided with HPLC-MS analyses to confirm the identity and demonstrate the high quality of our peptides.

Benefits of JPT's Histone Code Peptides
- Whole production performed in a regulated European environment according to DIN EN ISO 9001:2015 & GCLP standards; audits welcome!
- For high-throughput screening JPT's Histone Code Peptide Microarray is available displaying more than 3000 peptides.
- Provision of freeze dried aliquots for enhanced stability
- Proven track record for many applications

NB Histone Peptide H3 71:87 K79me1 (H3.12)

Selected References for Histone Peptide Tools
"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)
"Comprehensive Peptide Microarrays for Histone Research"
Schnatbaum et al, 32th EPS (2012) (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 for Histone Code Peptide Microarray
"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, YU (NY, USA)