Phosphorylation is one of the most common and important post-translational modifications of proteins in living organisms, which can be involved in the regulation of various life processes such as growth, development, adversity stress, and disease development by stimulating and regulating many signaling pathways. Phosphoproteomics aims to identify the phosphorylated proteins and the corresponding phosphorylation sites in the samples.

What We Offer

Lifeasible selects IMAC, phosphorylated antibody enrichment, or TiO2 enrichment according to experimental needs to achieve efficient enrichment of samples, and separates monophosphorylated peptides and polyphosphorylated peptides in separate steps during the enrichment of peptides so that they can be analyzed separately by mass spectrometry, avoiding the problem of ionization efficiency of polyphosphorylated peptides on monophosphorylated peptides during mass spectrometry The effect of the ionization efficiency on the identification and quantification of monophosphorylated peptides during mass spectrometry was avoided. We use Q ExactiveHF, Orbitrap Fusion, Orbitrap Fusion Lumos, and other advanced mass spectrometry platforms combined with Nano-LC to introduce quantitative phosphorylated plant proteome analysis service, just tell us your experimental purpose and send samples, Lifeasible is responsible for the project follow-up, which Including protein extraction, protein digestion, phosphorylated peptide enrichment, peptide separation, mass spectrometry, mass spectrometry raw data analysis, bioinformatics analysis all matters.

Service Flow

Technical Characteristics

• The mainstream IMAC, TiO₂, and Phosphorylated antibody enrichment method with high specificity and good enrichment efficiency is used to identify thousands of phosphorylation sites in one experiment and to rapidly construct phosphorylated protein modification profiles.
• Large-scale identification of the enriched phosphorylated peptides by high-resolution, high-scan speed mass spectrometry, which is not limited by the number of samples, overcomes the shortcomings of labeled quantitative techniques in quantifying multiple samples.
• The combination of commonly used quantitative techniques allows quantitative comparison of differences in phosphorylation levels between samples without the need for expensive isotope labeling reagents and at low experimental cost.
• Precise identification of protein phosphorylation sites, phosphorylation modifications can be localized to individual amino acid sites, and multiple fragmentation modes are available, such as CID, ETD, or HCD, to improve protein identification rates.

Reference

1. Park C. J., et al. "Protein phosphorylation in plant immunity: insights into the regulation of pattern recognition receptor-mediated signaling." Front Plant Sci, 2012, 3:177.

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For research use only, not intended for any clinical use.

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