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Protein Lipidation Analysis Service

Proteins lipidation refers to the covalent binding of lipid molecules to proteins, thereby revising the structure and function of proteins. Among the known covalent chemical modifications, the unique physicochemical properties of lipid molecules endow proteins with special structures and functions as well as greatly affect their membrane anchoring ability, transport and localization pathways, signal transduction, and protein interactions. The diversity of lipid structures and binding modes determines the functional complexity of lipidated proteins. Meanwhile, these lipidated proteins act in concert with other known or unknown modified proteins for the fine regulation of physiological activities. The structural and functional analysis of protein lipidation modifications is an important way to reveal the mechanisms of microbial infection, immune regulation, and tumor development and is important for discovering and screening disease markers and mining novel drug targets.

Existing analytical techniques have detected a very small fraction of lipids bound to proteins. Fatty acids, isopentenyl lipids, cholesterol, and glycosylphosphatidylinositol (GPI) are four common types of lipid molecules that can be covalently bound to proteins. The first three are lipid groups, and the last one is a glycolipid complex. Nevertheless, these four lipid molecules are covalently bound to proteins mainly by the N-, S-, and O- linkages.

Major lipid modifications of proteins

Major Analytical Methods of Protein Lipidation

Major analytical methods for protein Lipidation

Our Protein Lipidation Analysis Service

Creative Proteomics uses Thermo Fisher's Q ExactiveHF Mass Spectrometry platform, Orbitrap Fusion Mass Spectrometry platform, and Orbitrap Fusion Lumos Mass Spectrometry platform in combination with Nano-LC to provide protein lipidation identification services.

Customized Bioinformatics Services

Standard Analysis	Customized Analysis
a) Collection of output statistics b) Establishment of database and search for modified proteins c) Identification of modified proteins and modification sites d) Annotation of modified proteins e) Quantitative analysis of modified proteins f) Analysis of differential expression of modified proteins g) Functional enrichment analysis of differentially modified proteins GO/KEGG	Modified peptide motif analysis Protein network interaction prediction Protein domain prediction (Advanced Analysis) Protein subcellular localization analysis (Advanced Analysis)

Sample requirements

Fresh animal tissue: ≥600 mg
Fresh plant tissue: ≥6 g
Cell culture: ≥1×10⁷ cells/tube x 3 tubes
Fungi and bacteria: ≥600 mg
Serum, plasma: 450 μL × 4 tubes
Protein solution: total protein of 5-10 mg
Body fluid samples: urine of 15 mL × 4 tubes (centrifuge at 1000 x g for 5 minutes and discard sediment); or other body fluids (saliva, amniotic fluid, cell culture supernatant, etc.) > 15 mL

Advantages

High specificity and enrichment efficiency
Large-scale identification of lipidated protein with mass spectrometry of high resolution and high throughput
Combining commercially available quantitative techniques to analyze, compare, and correlate differences in lipidation levels between different samples quantitatively
A research team with extensive experience in PTMs

References

Luke H. Chamberlain, et al. The Physiology of Protein S-acylation. Physiol Rev. 2015 Apr; 95(2): 341–376.
PinJoe Ko, et al. Protein palmitoylation and cancer. EMBO Rep. 2018 Oct; 19(10): e46666.
Benjamin R. Sabari, et al. Metabolic regulation of gene expression through histone acylations. Nat Rev Mol Cell Biol. 2017 Feb; 18(2): 90–101.
Baoen Chen, et al. Protein lipidation in cell signaling and diseases: function, regulation and therapeutic opportunities. Cell Chem Biol. 2018 Jul 19; 25(7): 817–831.

Proteomics Sample Submission Guidelines

Ensure your samples are prepared and submitted correctly by downloading our comprehensive Proteomics Sample Submission Guidelines. This document provides detailed instructions and essential information to facilitate a smooth submission process. Click the link below to access the PDF and ensure your submission meets all necessary criteria.

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* For Research Use Only. Not for use in diagnostic procedures.

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From Our Clients

"I recently used their proteomics service for a project analyzing protein interactions in yeast models. The team was very responsive and helped clarify the methodology they employed, which made me feel confident in the results. The data quality was solid, with clear identification of several key proteins involved in our study. Their thorough analysis enabled me to pinpoint specific interactions that I hadn't considered before, which significantly improved the direction of my research. I appreciate their professionalism and support throughout the process."

Sarah Thompson, University of California, Berkeley

"Our lab collaborated with them on a project studying cancer biomarkers. The proteomics analysis provided was detailed and focused, specifically highlighting the differential expression of proteins between healthy and tumor samples. Their clear explanations of the data helped my team understand the biological implications. I also appreciated their willingness to revise the reports based on our feedback, ensuring that we had everything we needed for our publication. This collaborative spirit was invaluable."

Emily Rodriguez, Stanford University

"Our lab worked with them on a project studying the effects of diet on gut microbiota using proteomics. They used a label-free quantification method to analyze proteins in fecal samples before and after dietary intervention. The results showed significant changes in protein expression linked to microbial activity. This was pivotal for our hypothesis about diet-microbiota interactions. The clarity of their data presentation made it easy for our team to integrate these findings into our ongoing research."

Dr. Lisa Wong, University of Toronto

"My experience with Creative Proteomics during the mass spectrometry analysis was excellent. We sent in human saliva and mouse brain tissue samples, which they expertly analyzed using both LC-MS and GC-MS techniques. The results were invaluable, revealing key metabolites in the saliva and identifying biomarkers linked to brain function in the brain tissue."

Dr. Emily Carter, Senior Research Scientist

"The overall service from Creative Proteomics was outstanding. They made the entire process seamless and efficient, allowing us to focus on our research. We worked with leaf and root samples from various Arabidopsis genotypes for targeted metabolomics analysis. Their thorough profiling of primary and secondary metabolites gave us important insights into how the plants respond metabolically to environmental stress."

Dr. Laura Henderson, Plant Physiologist

"We had a pleasant collaboration with Creative Proteomics on mass spectrometry analysis of lipids. They conducted a detailed analysis of lipid species, providing us with important insights into lipid metabolism and its relationship with metabolic syndrome disease states."

Dr. Sarah Mitchell, Research Scientist

Online Inquiry

Please submit a detailed description of your project. We will provide you with a customized project plan to meet your research requests. You can also send emails directly to for inquiries.

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