The analysis of protein post translational modifications (PTMs) is challenging. Regular analysis often leads to incomplete amino acid sequence coverage and insufficient understanding of the crosstalk and selectivity of different PTMs and their impacts on cellular regulatory networks.

Over the years, we have developed highly efficient MS based proteomics technology for system-wide identification and quantification of PTM substrate proteins and mapping their PTM sites. We established the bioinformatics platform for understanding the functional relevance of the PTMs in cellular physiology. This integrated platform has profoundly benefited biomedical and pharmaceutical research, as demonstrated by continuous high profile publications and long-term collaborations with top drug discovery organizations.

The goal of our service is to make our cutting-edge technology accessible to the wider academic and industrial researchers. We are determined to help you achieve discoveries, whether you are seeking an understanding of mode-of-action for a drug candidate, enzyme substrate screening, biomarker discovery, or drug target screening.

ALL-IN-ONE

PTM SERVICE

We provide all-in-one biopharmaceutical and academic service for drug targeted PTM pathways and for basic research. This end-to-end service makes your drug discovery as easy as ONE, TWO, THREE. It covers essential steps from cell culture to affinity enrichment, from LC-MS/MS to bioinformatics. A unique feature is to integrate our powerful PTM antibody generation technology for reagent development against the identified PTM enzyme substrates. This service makes use of our PTM expertise to help you achieve discovery on target.

  • Both in vivo SILAC labeling and in vitro labeling technologies are available.
  • Integrated platform combining unique PTM antibodies, high-sensitivity PTM proteomics, and expertise bioinformatics;
  • High sensitivity to detect and quantify over 50 histone marks and 5,000 -10,000 PTM sites in one single experiment;
  • High reliability with strict data filtering and expert manual verification;
  • Powerful PTM antibody generation capability demonstrated by the world’s largest collection of PTM and histone antibodies.
Our Ph.D. trained scientists strive to provide the best support to each and every one of our customers. Free consultation is just one click away!

GLOBAL

PTM MAPPING

This service involves sample digestion with appropriate enzymes prior to LC-MS/MS analysis. Fractionation will be performed if necessary. The resulting peptides are subjected to immuno-affinity enrichment by proprietary reagents developed in-house. The resulting MS/MS data are searched against protein sequence databases. This approach maximizes sensitivity and PTM coverage for your proteins.

Our proprietary technologies enable comprehensive PTM mapping at the whole proteome level for well known (acetylation, phosphorylation, methylation and ubiquitination), as well as newly identified PTMs (crotonylation, succinylation, propionylation, butyrylation, and malonylation). Our technology features high sensitivity: capable of detecting over 10,000 PTM sites proteins in mammalian cells; and high reliability, with expert manual verification available. Using our technologies, the world’s largest acetylome in both mammalian and prokaryotic cells was identified. Expert bioinformatics analysis is available to link the data to biological functions. Customized analyses are available to investigate particular proteome fractions of your interests, such as nuclear proteins, histone proteins, mitochondrial proteins, membrane proteins, and more…

We accept samples from animals and plants, bacteria, body fluid, cell pellets, and cell lysates. Please also consider our featured all-in-one PTM service, an end-to-end PTM service designed to propel your biopharmaceutical research forward.

Guo, C., S. Xie, et al. (2016). “Bile Acids Control Inflammation and Metabolic Disorder through Inhibition of NLRP3 Inflammasome.” Immunity. PMID: 27692610.

He et al. (2016). Global Proteome Analyses of Lysine Acetylation and Succinylation Reveal the Widespread Involvement of both Modification in Metabolism in the Embryo of Germinating Rice Seed. Journal of proteome research. PMID: 26767346 

Xiong et al. (2016). A comprehensive catalog of the lysine-acetylation targets in rice (Oryza sativa) based on proteomic analyses. Journal of proteomics. PMID:26836501

Zhu et al. (2016). Quantitative Analysis of Global Proteome and Lysine Acetylome Reveal the Differential Impacts of VPA and SAHA on HL60 Cells. Scientific reports 6, 19926. PMID: 26822725

Wu et al. (2015). A chemical proteomics approach for global analysis of lysine monomethylome profiling. Molecular & cellular proteomics 14, 329-339. PMID: 25505155

Xie et al. (2015). Proteome-wide lysine acetylation profiling of the human pathogen Mycobacterium tuberculosis. The international journal of biochemistry & cell biology 59, 193-202. PMID: 25456444

Yang et al. (2015). Succinylome Analysis Reveals the Involvement of Lysine Succinylation in Metabolism in Pathogenic Mycobacterium tuberculosis H37Rv. Molecular & cellular proteomics PMID: 25605462

Mo et al. (2015). Acetylome Analysis Reveals the Involvement of Lysine Acetylation in Photosynthesis and Carbon Metabolism in the Model Cyanobacterium Synechocystis sp. PCC 6803. Journal of proteome research 14, 1275-1286. PMID: 25621733

Liu et al. (2015). Persistent human Borna disease virus infection modifies the acetylome of human oligodendroglia cells towards higher energy and transporter levels. Virology 485, 58-78. PMID: 26210075

Nie et al. (2015). Comprehensive profiling of lysine acetylation suggests the widespread function is regulated by protein acetylation in the silkworm, Bombyx mori. Proteomics. PMID: 26046922

Colak et al. (2015) Proteomic and biochemical studies of lysine malonylation suggests its malonic aciduria-associated regulatory role in mitochondrial function and fatty acid oxidation.pii: mcp.M115.048850. PMID: 26320211

Liu et al. (2014). CPLM: a database of protein lysine modifications. Nucleic acids research 42, D531-536.

Liao et al. (2014). Unexpected extensive lysine acetylation in the trump-card antibiotic producer Streptomyces roseosporus revealed by proteome-wide profiling. Journal of proteomics 106, 260-269. PMID: 24768905

Pan et al. (2014). Systematic analysis of the lysine acetylome in Vibrio parahemolyticus. Journal of proteome research 13, 3294-3302. PMID: 24874924

Li et al. (2014). Systematic identification of the lysine succinylation in the protozoan parasite Toxoplasma gondii. Journal of proteome research 13, 6087-6095. PMID: 25377623

Peng et al. (2011). The first identification of lysine malonylation substrates and its regulatory enzyme. Molecular & cellular proteomics 10, M111 012658. PMID: 21908771

Lu et al. (2011). Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation. PloS one 6, e28228. PMID: 22164248

Cheng et al. (2009). Molecular characterization of propionyllysines in non-histone proteins. Molecular & cellular proteomics 8, 45-52. PMID 18753126.

 

 

Our technology is featured with high sensitivity: capable of detecting and quantifying 8,000 – 10,000 proteins in mammalian cells; and high reliability: with expert manual verification available.
Our Ph.D. trained scientists strive to provide the best support to each and every one of our customers. Free consultation is just one click away!

PTM

IDENTIFICATION

This service is to detect PTM on particular proteins of your interests. PTM can be identified from purified proteins, recombinant proteins or proteins in complex mixtures and cellular lysates. Our technology features high sensitivity and reliability, capable of identifying PTMs with extremely low stoichiometry, and requiring only 1~10 ng or less for a given protein.

We can help you to identify…
Well-Known PTMs
  • Acetylation
  • Methylation
  • Ubiquitination
  • Phosphorylation
Newly Discovered PTMs
  • Crotonylation
  • Succinylation
  • Butyrylation
  • Propionylation
  • Malonylation
  • Glutarylation
  • 2-Hydroxyisobutyrylation
  • And more…
Novel PTMs
  • Novel mass shift analysis;
  • Custom method upon request
Samples from 2DE gel spots, 1DE bands, and protein mixtures in solution are accepted.
Our Ph.D. trained scientists strive to provide the best support to each and every one of our customers. Free consultation is just one click away!

QUANTITATIVE

PTM PROFILING

Dynamics of PTMs, such as phosphorylation, ubiquitination, acetylation, are critical to cellular mechinisms. Dysruglation of PTM pathways is associated with diverse diseases. The PTM-regulatory enzymes have been emerged as a major group of drug targets in the past two years. Accordingly, dynamic analysis of cellular PTMs are important to biological studies.

We are known for generating quantitative PTM proteomic datasets with high sensitivity. Our technology has contributed to quantitative analysis of widely studied PTMs, such as acetylation, phosphorylation, ubiquitination, methylation, in cultured cells with different genetic backgrounds and treatments, and in animal tissue and clinical human tissue samples. Both in vivo SILAC and in vitro labeling technologies can be used for quantitative PTM analysis.

This service involves sample labeling and sample digestion with appropriate enzymes prior to LC-MS/MS analysis. Fractionation will be performed if necessary. The resulting peptides are subject to immuno-affinity enrichment by proprietary reagents developed in-house. The resulting MS/MS data are searched against protein sequence databases to identify PTM sites and quantify their changes. Manual verification can be carried out to ensure reliable identification, if necessary.

We accept samples from animals and plants, bacteria, body fluid, cell pellets, and cell lysates. Please also consider our featured all-in-one PTM service, an end-to-end PTM service designed to propel your biopharmaceutical research forward.

  • Chen et al. (2012). Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Molecular & cellular proteomics 11, 1048-1062. PMID: 22826441
  • Zhang et al. (2013). Comprehensive profiling of protein lysine acetylation in Escherichia coli. Journal of proteome research 12, 844-851.PMID: 23294111
  • Kwon et al. (2015). Global analysis of phosphoproteome dynamics in embryonic development of zebrafish (Danio rerio). Proteomics.PMID: 26449285
  • Chen, et al. (2015) Comparative phosphoproteomic analysis of intestinal phosphorylated proteins in active versus aestivating sea cucumbers. J Proteomics , http://dx.doi.org/10.1016/j.jprot.2015.09.016.PMID: 26385000
  • Wu et al. (2015). Suberoylanilide hydroxamic acid treatment reveals crosstalks among proteome, ubiquitylome and acetylome in non-small cell lung cancer A549 cell line. Scientific reports 5, 9520. PMID: 25825284
  • Wang, Z. K., J. Wang, et al. (2016). “Proteomic and Phosphoproteomic Insights into a Signaling Hub Role for Cdc14 in Asexual Development and Multiple Stress Responses in Beauveria bassiana.” PLoS One 11(4): e0153007. PMID: 27055109
     

Our technology features high sensitivity: capable of detecting and quantifying over 50 histone marks and 10,000 lysine acetylation sites in mammalian cells in one single experiment; representing the highest possible sensitivity in industry; and high reliability: with strict data filtering and expert manual verification available.
Our Ph.D. trained scientists strive to provide the best support to each and every one of our customers. Free consultation is just one click away!