You ship your biological samples (cells, tissues, or histone extracts) to our specialized laboratory using our provided guidelines to ensure stability.
Formylation is a newly discovered and critically important regulatory histone modification. CD BioSciences provides comprehensive histone lysine formylation analysis services based on high-resolution mass spectrometry (MS) to help you elucidate its key roles in gene expression, cell fate, and disease pathogenesis, thereby accelerating your research progress.
Histone lysine formylation (Kform) is an emerging epigenetic modification where a formyl group (-CHO) is attached to specific lysine residues on histone proteins. Functionally, it serves as a dynamic regulatory signal involved in transcriptional activation, DNA damage repair, and cellular stress response, often acting in coordination or competition with other modifications like acetylation. Its study holds significant research value as Kform provides a direct mechanistic link between cellular metabolism—particularly one-carbon metabolism—and chromatin regulation, offering novel insights into development, aging, and diseases such as cancer and neurodegenerative disorders. Advancing Kform research not only deepens our understanding of epigenetic complexity but also may reveal new therapeutic targets in precision medicine.
Fig.1 N6-formyl-lysine residues arising from products of oxidative DNA damage are chemical analogs of the biologically important lysine N6-acetylation. (Jiang T, et al., 2007)
To address the significant challenges in detecting and quantifying the elusive histone lysine formylation modification, CD BioSciences provides a comprehensive histone lysine formylation analysis service. Leveraging our cutting-edge high-resolution mass spectrometry platform and optimized chemical derivatization protocols, we offer sensitive and accurate identification, localization, and absolute quantification of Kform sites. Our end-to-end solution empowers researchers to reliably explore the functional roles of this critical modification in gene regulation, disease mechanisms, and metabolic signaling, accelerating discovery in next-generation epigenetics.
Our platform delivers a comprehensive suite of analytical services designed to map, measure, and monitor histone lysine formylation (Kform) with precision. We offer everything from discovery-phase global profiling to highly sensitive targeted quantification, empowering researchers to fully characterize this low-abundance modification across diverse biological contexts.
| Service | Description |
|---|---|
| Discovery & Identification Service | Comprehensive profiling to identify all potential formylation sites on histones (e.g., H3K4, H3K9, H3K27, H4K5). This unbiased analysis is ideal for exploratory research and novel target discovery. |
| Targeted Quantification Service |
|
| Dynamic Change Analysis Service | Time-course or dose-response experiments to track the kinetics of Kform deposition and removal. This analysis is key to understanding the temporal regulation and stimulus-responsive nature of the modification. |
| Customized Panel Development Service | We offer customized assay development to simultaneously quantify key Kform sites alongside other relevant histone modifications (e.g., acetylation, methylation) from a single sample, enabling the study of epigenetic crosstalk and providing a more comprehensive view of chromatin state. |
Our service follows a streamlined, end-to-end workflow designed to ensure the highest data quality and reliability for detecting the challenging histone lysine formylation modification.
You ship your biological samples (cells, tissues, or histone extracts) to our specialized laboratory using our provided guidelines to ensure stability.
Our experts perform gentle, acid-based extraction followed by high-purity purification to isolate core histones, minimizing modification loss or artifacts.
To enhance the stability and detection specificity of formyl groups, we apply our optimized chemical derivatization protocol. Histones are then enzymatically digested into peptides for LC-MS/MS analysis.
Peptides are separated by nano-flow liquid chromatography and analyzed using our state-of-the-art high-resolution tandem mass spectrometer. This step provides precise mass data for modification identification and quantification.
Raw data is processed using advanced software for peak identification, formylation site localization, and quantitative comparison. Statistical validation is performed to ensure confidence in the results.
You receive a detailed report containing all experimental procedures, raw and processed data, visualizations of key results (spectra, graphs), quantitative findings, and a clear biological interpretation of the data.

At CD BioSciences, our expertise extends far beyond histone lysine formylation. We provide a comprehensive suite of services for analyzing a full spectrum of histone post-translational modifications (PTMs), including acetylation, methylation (mono-, di-, tri-), phosphorylation, ubiquitination, crotonylation, lactylation and more. Contact us today to discuss your project and receive a personalized proposal.
Reference
1. Jiang T, Zhou X, Taghizadeh K, et al. N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage[J]. Proceedings of the National Academy of Sciences, 2007, 104(1): 60-65.
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