Histone Modification Analysis
There are various types of histone post-translational modifications, which are related to a variety of biological functions. Mass spectrometry can qualitatively and quantitatively analyze histone modifications. Biotech company BGI provides mass spectrometry-based histone post-translational modification analysis services.Histone post-translational modification analysisservices.
Histone post-translational modifications
Histones are a class of highly conserved proteins, which are key components of chromatin and structural units of DNA packaging. The function of histones is mediated by their post-translational modifications. Histone post-translational modifications include covalent modifications such as phosphorylation of serine or threonine residues, methylation of lysine or arginine, acetylation and deacetylation of lysine, ubiquitination, and sulfonylation of lysine. These modifications are crucial for nuclear integrity as they can regulate chromatin structure and recruit enzymes involved in gene regulation, DNA repair, and chromosome condensation. Most histone post-translational modifications are located on the N-terminal tails as the N-terminus is the most exposed and flexible region of the protein. Analyzing histone post-translational modifications helps explore the relationships between histone modifications and biological functions such as chromosome condensation and DNA transcription.
Histone post-translational modification analysis
Histone post-translational modification analysis methods include traditional radioactive labeling, Edman sequencing, antibody-based techniques, and mass spectrometry-based methods. Mass spectrometry, as an analytical technique, can impartially analyze various modifications on histones and analyze the levels and differential modifications of histone modifications, i.e., qualitative and quantitative analysis of histone modifications.
Histone post-translational modification analysis
Related services:
How to order?
