Citrullination Proteomics Service
Citrullination, also known as deimination, is a post-translational modification (PTM) that converts arginine residues into citrulline through the action of peptidylarginine deiminases (PADs). This subtle but irreversible change can significantly impact protein structure, function, and interactions. MtoZ Biolabs offers a specialized Citrullination Proteomics Service to support researchers in accurately identifying and quantifying citrullinated proteins across various biological samples. Our service combines advanced detection technologies with targeted enrichment strategies to deliver reliable, site-specific insights.
Figure 1. Schematic Representation of the Citrullination Reaction Catalyzed by Peptidylarginine Deiminases (PADs)
Citrullinated proteins play crucial roles in multiple biological processes. Notably, they are involved in epigenetic regulation, where histone citrullination influences chromatin dynamics and gene expression. In the immune system, aberrant citrullination has been linked to autoimmune diseases, such as rheumatoid arthritis, through the generation of autoantigens and the production of anti-citrullinated protein antibodies (ACPAs). Additionally, citrullination contributes to inflammation, apoptosis, and cancer progression, making it a valuable target for both basic research and clinical investigation.
Figure 2. Summary of the Pathogenic Roles of ACPAs in Rheumatoid Arthritis
Service at MtoZ Biolabs
MtoZ Biolabs' Citrullination Proteomics Service platform is designed to address the challenges of low-abundance citrullinated peptides and site localization, enabling researchers to comprehensively map the citrullinome, quantify modification dynamics, and uncover regulatory roles across diverse biological systems.
Our Analytical Strategies Include:
💠Mass Spectrometry-Based Profiling: High-resolution LC-MS/MS is used to identify citrullinated peptides, determine site-specific modifications, and quantify differential expression under various conditions. Both label-free and labeled quantification (e.g., SILAC, DIA) are available.
💠Antibody-Based Enrichment and Detection: Anti-citrulline antibodies enable selective enrichment or detection of citrullinated proteins. These methods are useful for validating specific targets, Western blotting, or ELISA-based profiling.
💠Biochemical Assays for PAD Activity: Quantitative biochemical assays are available to measure citrullination levels by monitoring PAD enzyme-catalyzed reactions. These assays are suitable for evaluating PAD activity or quantifying citrulline production in vitro and in cellular systems.
Service Advantages
✔️Advanced Mass Spectrometry Platforms: High-resolution LC-MS/MS systems enable confident identification and precise localization of citrullination sites.
✔️Comprehensive Quantitative Capabilities: Supports both label-free and labeled quantification (SILAC, DIA) to assess dynamic changes in citrullination under different conditions.
✔️One-Stop Service: From sample preparation to data interpretation, we offer a streamlined workflow under one roof—saving time, effort, and coordination.
✔️Experienced Scientific Team: Our proteomics experts bring extensive experience in PTM analysis, ensuring high-quality data generation and result interpretation.
✔️Fully Customizable Analysis: Flexible service modules and workflow adjustments tailored to your sample type, research goals, and technical needs.
Applications
1. Autoimmune Disease Research
Identify citrullinated autoantigens and profile their expression in diseases such as rheumatoid arthritis, multiple sclerosis, and systemic lupus erythematosus. Support biomarker discovery and ACPA-related mechanism studies.
2. Cancer Biology
Investigate the role of citrullination in tumor progression, immune evasion, and metastasis. Analyze PAD enzyme activity and its downstream targets in various cancer types.
3. Epigenetics and Chromatin Remodeling
Study citrullinated histones and their influence on chromatin structure, transcriptional regulation, and gene silencing.
4. Drug Discovery and Development
Quantify global or site-specific citrullination changes in response to PAD inhibitors and assess their therapeutic impact.
Case Study
PAD2-Mediated Citrullination Regulates Macrophage Polarization
A study explored the role of PAD2-mediated citrullination in macrophage function during acute lung injury induced by Pseudomonas aeruginosa. Using single-cell RNA sequencing and mass spectrometry-based proteomics, researchers identified a novel citrullination site at arginine 171 (R171) on NF-κB p65, catalyzed by PAD2. This modification was shown to influence nuclear import and downstream macrophage polarization. Based on these findings, a nanoparticle-based PAD2 inhibitor was developed to selectively target pro-inflammatory macrophages. This study demonstrates how site-specific citrullination profiling supports the discovery of functional PTM mechanisms and informs therapeutic strategies—an application well supported by Citrullination Proteomics Service.
Figure 3. Identification of PAD2-dependent Citrullination Site within NF-κB p65
FAQ
Q: Can this service detect crosstalk between citrullination and other PTMs?
Absolutely. Our platform supports integrated PTM analysis to investigate potential interactions or competition between citrullination and modifications such as methylation or acetylation.
Deliverables
1. Comprehensive Experimental Details
2. Materials, Instruments, and Methods
3. Total Ion Chromatogram & Quality Control Assessment (project-dependent)
4. Data Analysis, Preprocessing, and Estimation (project-dependent)
5. Bioinformatics Analysis
6. Raw Data Files
To explore citrullination in your biological system, contact MtoZ Biolabs today. Our integrated Citrullination Proteomics Service platform, from enrichment to in-depth analysis, delivers the sensitivity and specificity your research demands.
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