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Drosophila Protein Modification Analysis

Protein post-translation modification (PTM) is the process of adding modification groups or enzymatic cleavage to change the properties of proteins. PTM of eukaryotic proteins mainly includes glycosylation, disulfide bond pairing, methylation, acetylation, phosphorylation, ubiquitination, hydroxylation, ribosylation, etc. The modified proteins are widely involved in various important physiological regulatory activities in Drosophila, including biological clock regulation, chromatin regulation, embryonic development, and disease onset. Traditional transcriptomics cannot identify PTMs, therefore comprehensive protein modification omics is very important in Drosophila research to reveal the involvement of different proteins in gene regulation, signal transduction, reproductive development, neural activity, metabolism, tumorigenesis and other key life activities.

CD BioSciences uses advanced proteomics techniques to identify protein modifications and loci in different tissues of Drosophila. We support the analysis of protein modifications such as acetylation, methylation, phosphorylation, and ubiquitination, etc. Relying on a comprehensive biochemical modification detection and bioanalytical platform, CD BioSciences provides identification, detection, and characterization of modified proteins and loci. The accuracy and reproducibility of results are further ensured by specific enrichment and sensitive detection.  

Statistics and functional implication of the PTMsFig.1 Statistics and functional implication of the PTMs (Minguez et al.2012)

What We Offer

The identification of protein post-translational modifications is fundamental to elucidating the molecular mechanisms within cells. As opposed to labor-intensive, time-consuming experimental work, CD BioSciences provides accurate, easy and fast total PTMs solutions using technologies such as high-throughput mass spectrometry and bioinformatics PTMs prediction and analysis. We generate valuable information and technical support for our clients to speed up your research.

  • Sample Preparation - Strict quality control ensures protein sample concentration and purity.
  • Peptide Pre-Separation - CD BioSciences uses peptide pre-separation to reduce the impact of high abundance proteins on low abundance modified proteins.
  • Advanced Enrichment Strategies - CD BioSciences develops the most effective and rapid enrichment strategies based on target modifications, including immunoprecipitation (acetylation, ubiquitination), lectin affinity assay (glycosylation), IMAC and other chromatographic separations such as SCX and MOAC (phosphorylation), and other enrichment techniques to reduce deletions in peptide measurements.
  • Tandem MS - CD BioSciences not only has an electrospray mass spectrometry (ESI) and matrix-assisted laser ionization (MALDI) protein analysis platform, but also is equipped with a variety of mass spectrometry detectors, including time-of-flight (TOF), quadrupole, ion traps, and ion cyclotron resonance (ICR), which can be used to discover and identify new patterns of PTMs, and to perform quantitative studies to determine how a particular PTM changes during cellular physiology or pathology.
  • In-House Database - CD BioSciences has developed an in-house protein modification database that can improve the depth and accuracy of our clients' modification proteomics studies and applications. 

General Workflow

General Workflow

Why CD BioSciences?

  • Rich experience in Drosophila protein post-translational modifications 
  • Professional platforms improving sensitivity for quantification of modified peptides
  • Automated sample processing to support large samples and reduce error
  • Fast turnaround, cost-effective and transparent pricing

CD BioSciences is an advanced sequencing and big data analysis biotechnology company. We are technology-oriented and provide total solution for Drosophila protein modifications analysis. Our professional team provides 24 × 7 customer service to every client for saving time and effort. There are no limitations of our service. If you need any further information or have any question, please feel free to contact us.

Reference

  1. Minguez P, et al. (2012). Deciphering a global network of functionally associated post‐translational modifications. Molecular systems biology. 8(1), 599.

For research use only. Not intended for any clinical use.

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