Detection of Biotinylated Proteins by Mass Spectrometry

Services

The study of the proteome has progressed significantly in recent years by analyzing target subpopulations of proteins covalently labeled with biotin-containing tags. Biotin tags can be used to target subpopulations of proteins that meet for subsequent mass spectrometry analysis. A limitation of mass spectrometry strategies is that mass spectrometry does not readily distinguish contaminants from target proteins. Strategies to identify proteins involved in specific biological functions rely on the covalent labeling of biotin onto proteins. Recently, new genetic chemical strategies targeting biotinylases have been used to study specific intracellular proteomic studies. Novel flexible high-resolution analysis strategy for efficient analysis of biotin-labeled proteins. Analytical methods used for biotinylated proteins often do not recognize biotinylated peptides, making it difficult to distinguish genuine biotinylated proteins from contaminating proteins. Direct mass spectrometry analysis of biotinylated proteins is of great significance for the study of organelle proteomics. In the future, it is expected that a broader approach can be expanded to improve the accuracy of biotinylated protein-based assays.

The Services

Mass spectrometry services for biotinylated proteins that Alfa Chemistry can provide include but are not limited to:

Biotinylation click reaction for labeled proteins
protein precipitation
Enrichment of biotinylated peptides
Analysis of biotin content in samples
Protein elution and digestion
Western blot
Peptide chromatography and MS collection
Tandem mass spectrometry

The significance of mass spectrometry in the detection of biotinylated proteins

The analysis, identification and research of proteins is one of the important research purposes in biochemistry. Through the mass spectrometry analysis of biotinylated proteins, the functions, interactions and active sites of proteins can be understood. The traditional detection method is to combine biotinylated peptides and perform tandem mass spectrometry analysis. Due to the high binding force, the binding site of biotinylated lysine is difficult to elute, resulting in signal confusion. At present, an effective method is to combine tandem mass spectrometry detection analysis and elution of more lysine residues to more accurately locate biotinylated proteins, narrow the detection range, and speed up the analysis of key proteins.

Current research

The researchers developed a flexible high-resolution analysis strategy, direct detection with biotin tag (DiDBiT), which can be used in studies specialized in the analysis of biotin-labeled proteins. The method relies on direct mass spectrometric detection of biotinylated proteins and is applicable to a variety of protein labeling protocols in cell culture and in vivo. DiDBiT improves MS analysis of biotin-labeled proteins by enriching peptides, enabling high-level biotin detection of target proteins.

Figure 2. Researchers propose a novel assay (DiDBiT) for the analysis of biotinylated proteins, amenable to a wide range of labeling strategies and preparations

What can we provide?

Professional data analysis
Efficient detection schemes and strategies
Support global customer payment
Intelligent analysis platform, efficient and fast
Optimize service system and process
Item response biotinylation management

Alfa Chemistry provides professional high-efficiency mass spectrometry analysis of biotinylated proteins, and strives to apply it to a wider range of proteomics research, making it one of the most efficient research tools. If you are interested in our services, please contact us immediately.

References:

Lucio. M.S.; et al. Direct detection of biotinylated proteins by mass apectrometry. J. Proteome Res. 2014, 13(9): 3966-3978.

※ It should be noted that our service is only used for research, not for clinical use.

Online Inquiry

Name:

Phone:

* Email:

* Quantity

* Service & Products of Interest

Project Description:

* Verification Code