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Identification of Posttranslational Modification-Dependent Protein Interactions Using Yeast Display

Yeast surface displayed human proteome libraries have been used to identify protein fragments with affinity for various target molecules, including phosphorylated peptides. When combined with fluorescently activated cell sorting and high throughput methods for the analysis of selection outputs, yeast surface displayed human proteome libraries can rapidly and efficiently identify protein fragments with high affinity for any soluble ligand that can be fluorescently detected, especially for posttranslational modifications. Based on decades of experience and advanced technology, Creative Biolabs has constructed large libraries that display human protein fragments for identifying posttranslational modification-dependent protein interactions.

Identification of Posttranslational Modification-Dependent Protein Interactions

The posttranslational modifications (PTMs) play a critical role in signal transmission or functional regulation for many cellular processes. Over 200 types of PTM are generated by thousands of cellular enzymes, including phosphorylation, glycosylation, lipidation, sumoylation, acetylation, ubiquitination, and methylation (not limited). The identification of proteins that interact specifically with posttranslational modifications such as phosphorylation is usually essential to understand cellular signaling pathways.

Identification of Posttranslational Modification-Dependent Protein Interactions via Yeast Display

Yeast display, as a eukaryotic surface display system, is a new technique that allows direct affinity capture using modified ligands and ready identification of the binding protein based on a tight linkage between the protein and its encoding gene. Yeast human proteome display libraries provide a flexible and powerful tool for identifying protein fragments with affinity for most soluble target ligand and are particularly suitable for the study of PTM-dependent protein interactions. Since it has been demonstrated that yeast protein expression pathways are similar to those found in mammalian cells, human protein fragments displayed by yeast human proteome libraries are perfectly possible to be properly folded and functional. Compared with protein microarrays, yeast displayed human proteome libraries can be generated relatively quickly at low cost and are an easily renewable resource. When combined with a compatible method of high throughput nucleic acid analysis (e.g. exon microarrays or next-generation sequencing), selection outputs can be comprehensively screened, allowing the discovery of a greater diversity of interactions.

Identification of Posttranslational Modification-Dependent Protein Interactions Using Yeast Display

Why Choose Us?

At Creative Biolabs, our scientists have constructed large libraries that display human protein fragments (around 100-400 amino acids) on the yeast surface as C-terminal fusions to the yeast a-agglutinin subunit, Aga2p and successfully applied to identify protein fragments that bind to post-translationally modified phosphorylated peptides, small signaling molecule phosphatidylinositides, and monoclonal antibodies. With years of experience, Creative Biolabs can provide services in identifying posttranslational modification-dependent protein interactions using yeast surface displayed human proteome libraries for our worldwide clients.

If you are interested in learning more about Creative Biolabs’ yeast display services, please contact us for more details. We also offer other Yeast Display Library Screening services: Premade Human Antibody Library for Yeast Display.

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