Histones are a class of highly conserved proteins with only a few amino acid differences between different variant sequences. The N terminus of histones can undergo various modifications such as methylation, acetylation, phosphorylation, ubiquitination, ADP ribosylation, etc. These covalent modifications are closely related to gene transcription, DNA damage repair, DNA replication, chromosome cohesion, etc. As an important epistatic marker, histone modifications are also linked to other epistatic markers, constituting a complex network, and the histone code greatly enriches the information content of the traditional epigenetic code.

What We Offer

In contrast to traditional quantitative proteomic analysis, the key step in the quantitative analysis of histone modifications is the isolation and purification of pure histone fractions. Lifeasible has established an experimental platform for the isolation and purification of histone proteins, which are located in the nucleus of cells. The nuclei are first obtained by low-speed centrifugation, and then the nuclei are broken up to separate histones and DNA, and the impurities are precipitated by high-salt precipitation, and the various histone fractions are separated and purified by HPLC, and then analyzed by subsequent mass spectrometry experiments. Meanwhile, to identify and quantify more histone post-translational modification information, we will use 2-3 different enzymes for protein samples in the enzymatic digestion process, which improves the peptide coverage of histones during mass spectrometry analysis and excludes the loss of histone post-translational modification information caused by inappropriate peptide length and low ionization efficiency.

Lifeasible provides the perfect solution for qualitative and quantitative analysis of plant histone modifications using an advanced mass spectrometry platform. All you need to do is tell us your experimental objectives and send us your samples, and we will take care of all the follow-up of the project, providing the identification of histone modifications, modification sites, and quantitative analysis.

Sample Requirement

• Plant leaves, rhizome, xylem, bast >2 g
• Total protein >3 mg

* If you are providing tissue samples, please send us the tissue samples on dry ice.
* If you are providing protein samples, protein extraction can be done with normal tissue and cell lysis solution.

Reference

1. Chunyan L., et al. “Histone Methylation in Higher Plants.” Annual Review of Plant Biology, 2010, 61(1): 395-420.

*If your organization requires the signing of a confidentiality agreement, please contact us by email.

For research or industrial use.

Related Services

• Phosphorylated Plant Proteome Analysis
• Acetylated Plant Proteome Analysis
• Ubiquitinated Plant Proteome
• Glycosylated Plant Proteome
• Methylated Plant Proteome
• Identification of Disulfide Bonds in Plant Proteins
• Detection of SUMOylation in Plant Proteins