Histone lysine SUMOylation is a critical regulatory modification that fine-tunes chromatin structure and gene expression in response to cellular signals. CD BioSciences offers specialized histone lysine SUMOylation analysis services to empower your investigation into this dynamic and influential epigenetic mechanism. Our tailored solutions deliver precise, publication-ready data, accelerating your discovery of SUMOylation-dependent pathways in health and disease.
Histone lysine SUMOylation is a reversible post-translational modification wherein small ubiquitin-like modifier (SUMO) proteins are covalently attached to specific lysine residues on histone tails via an enzymatic cascade analogous to ubiquitination. This modification introduces a substantial protein moiety that can sterically hinder interactions or serve as a docking platform for downstream effector proteins. Biologically, SUMOylation plays multifaceted roles in transcriptional repression, genome stability maintenance, DNA damage repair, and cellular stress responses. It often functions as a molecular switch that modulates other modifications, such as acetylation and methylation, creating a complex layer of epigenetic crosstalk. Dysregulation of histone SUMOylation has been implicated in oncogenesis, neurological disorders, and other pathological states, underscoring its significance as a key regulatory node and a promising therapeutic target.
Fig.1 Models for the functions of histone SUMOylation in transcriptional repression. (Ryu H Y, Hochstrasser M., 2021)
As a leading provider of epigenetic research services, CD BioSciences delivers expert histone lysine SUMOylation analysis services by integrating high-sensitivity enrichment strategies with cutting-edge mass spectrometry. Our service is designed to overcome the inherent challenges of studying this low-abundance, labile modification, providing you with reliable data to uncover its specific functions in development, disease, and cellular signaling pathways.
Our platform provides an integrated analytical framework to fully characterize histone SUMOylation. We offer end-to-end solutions, from unbiased discovery of novel sites to precise quantification of specific events, enabling systematic investigation of this complex modification across different biological contexts.
| Service | Description |
|---|---|
| Global SUMOylome Profiling | Comprehensive identification and mapping of SUMOylation sites across all core histones. |
| Site-Specific Quantification | Targeted relative or absolute quantification of specific SUMOylation events (e.g., H4K12su, H2BK6su). |
| SUMO Paralogue Differentiation | Analysis distinguishing between modifications by different SUMO family members (SUMO-1, SUMO-2/3). |
| Dynamic Monitoring | Time-course studies to track SUMOylation changes in response to stimuli (e.g., heat shock, DNA damage). |
| Crosstalk Analysis | Integrated profiling of SUMOylation alongside other PTMs to study cooperative regulation. |
Project Consultation & Design
We begin with a collaborative consultation to define your research goals and customize the analytical strategy, selecting the optimal approach for discovery or targeted analysis.
Sample Preparation & Enrichment
Histones are extracted under native conditions, followed by affinity-based enrichment using high-specificity reagents to isolate SUMOylated targets from complex backgrounds.
High-Resolution LC-MS/MS Analysis
Samples are analyzed via nanoLC coupled to high-resolution mass spectrometry, using DIA or PRM acquisition modes for comprehensive or sensitive quantification of SUMOylated peptides.
Data Processing & Bioinformatics
Raw data undergoes specialized processing for accurate SUMOylation site localization, quantitative comparison, and statistical validation using tailored algorithms and databases.
Reporting & Delivery
You receive a detailed report with biological interpretation, annotated spectra, quantitative results, and all supporting data, formatted to support publication and further research.

Beyond histone SUMOylation, CD BioSciences is your trusted partner for a full spectrum of epigenetic analysis. We provide extensive services for studying acetylation, methylation, phosphorylation, ubiquitination, formylation, succinylation, crotonylation, lactylation, glutarylation, and ADP-ribosylation, among others. Our platform is built for flexibility, allowing us to create fully customized, multi-PTM profiling solutions tailored to your unique research questions. If you are interested in our services, please feel free to contact us for more details and quotation information of related services.
Reference
1. Ryu H Y, Hochstrasser M. Histone sumoylation and chromatin dynamics[J]. Nucleic Acids Research, 2021, 49(11): 6043-6052.
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