Products >> Upgrades >> SimGlycan



SimGlycan® version 5.61 Released

The new version includes the following:

  1. Addition of New Glycans in SimGlycan Master Database: The SimGlycan master database is updated with curated (a) N-glycans derived from Monoclonal antibody (mAb), Bovine Fetuin, Chinese Hamster Ovary (CHO), (b) glycosaminoglycans derived from Low Molecular Weight Heparin (LMWH), and (c) polysaccharides derived from plants. Following are brief descriptions of the glycans and their sources:

    • N-Glycans of Monoclonal Antibody (mAb): Recombinant monoclonal antibody therapeutics (mAbs) represent the largest group of therapeutic proteins as a major new class of drug. SimGlycan database now includes 71 curated unique N-Glycan structures of mAb which play critical role in immunity, pathogenicity and other cellular processes.

    • N-Glycans of Chinese Hamster Ovary (CHO): Therapeutic proteins obtained from Chinese Hamster Ovary (CHO) cell lines show almost same glycosylation pattern as human, and hence, are most widely used in the development of biosimilar products. Now, we have added 130 curated unique N-Glycan structures into SimGlycan database.

    • N-Glycans of Bovine Fetuin: Fetuin (blood proteins) is an important component of bone metabolism regulation, insulin resistance, protease activity control etc. It has also been identified as a biomarker for neurodegenerative disease. We have now added 71 unique N-Glyan structures from Bovine fetuin, that play a critical role in these processes.

    • Polysaccharides of Plants: Plant polysaccharides' unique characteristics of the water-soluble colloids makes food highly nutritious and hence, has high value in food industry. 210 unique polysaccharides have been added into the SimGlycan database.

    • Low Molecular Weight Heparin (LMWH): Low Molecular Weight Heparins are coagulation inhibiting glycosaminoglycans. Because of the anti-coagulation nature, these glycosaminoglycans are therapeutically engineered to prevent thrombosis, and thus has high medicinal value. 317 glycosaminoglycans of LMWH have been added into the SimGlycan database.

      These structures were curated from the published papers in journals namely Analytical chemistry, Biochemistry, Carbohydrate Research, European Journal of Biochemistry, Food Hydrocolloids, Journal of Biological Chemistry, Journal of Chromatography, and Phytochemistry.

  2. Fixes to reported issues.

SimGlycan® version 5.60 Released

The new version includes the following:

  • Exclude Monosaccharide(s) Filter: SimGlycan can now filter glycan structures based on monosaccharide residues:

    1. SimGlycan Server
    Using the web-panel, you can search glycan structures which do not contain specific monosaccharide residues. **

    2. SimGlycan Client
    You can specify one or multiple monosaccharide residue(s) in the exclusion list while performing a glycan search. The program will not report glycan structures which contain any of the excluded monosaccharide residues in the result. This functionality helps eliminate false positives.

  • Curate Glycan Structures: SimGlycan's intuitive web-panel now enables you to curate glycans from the master database based on their biological sources. **

  • Fixes to the reported issues

** Available in SimGlycan Enterprise Edition only

SimGlycan® version 5.50 Released

The new version includes the following:

  • Identification of glycans labeled with dual modifications strategies and stable-isotope labeling techniques: SimGlycan now supports identification of glycans labeled using

    1. Dual modifications strategies
    - reducing end modified with a fluorophore e.g., 2-AA
    - modification of the fluorophore e.g., methylamidation
    - modifications of target carbohydrate residues e.g., labeling of sialic acids with methylamidation, or 1,2-diamino-4,5-methylenedioxybenzene (DMB)

    This functionality provides the first ever software solution, to the best of our knowledge, for Sialoglycomics.

    2. Stable-isotope labeling
    The software can identify glycans using MS/MS data of samples treated with stable isotopic labeling techniques. You can now compare isotopically distinct forms of the same glycan structure originating from different biological samples such as control and diseased.

  • Loading of raw data (DDA method) directly from Waters .raw file format: SimGlycan can now read DDA data directly from Waters .raw format files. This functionality is in addition to the peaklist support from Waters .lcs format files.

  • Identification of glycans labeled with RapiFluor-MS reagent: SimGlycan now facilitates structural analysis of glycoforms labeled with GlycoWorks RapiFluor-MS reagent (Waters Corporation), derived from complex mixtures.

  • Fixes to the reported issues.
Previous Versions >>

An Innovative Glycan and Glycopeptide MSn Data Analysis Tool SimGlycan® predicts the structure of glycans and glycopeptides using mass spectrometry data.

SimGlycan® accepts the experimental MS/MS and Multi Stage/Sequential mass spectrometry (MSn, n>2) data, matches them with its own database of theoretical fragments and generates a list of probable candidate structures. Each structure is scored to reflect how closely it matches your experimental data. Apart from the structural information, other biological information for the probable molecular structures such as the glycan class (N-Linked, O-Linked heparin, lipopolysaccharide etc.), reaction, pathway and enzyme are also made available for easy reference in case of structural elucidation of glycans while in the case of glycopeptide qualitative analysis, information such as Protein ID, Protein Name, Source, Classification, Class, peptide sequence, peptide mass etc. are made available for identified glycopeptides.

Glycan & Glycopeptide MS/MS Data Analysis for Studying Glycosylation

Protein Glycosylation, which is a key post-translational modification, is the result of addition of a glycan to a peptide sequence. Glycopeptides are known to exhibit multiple biological functions. In order to identify distinct functional properties for defined structural features, detailed information on the respective glycan moieties is essential. In order to understand all these phenomena, glycosylation analysis is an area of growing interest. Glycans have also been found to participate in many biological processes including embryonic development, inter and intracellular activities, coordination of immune functions, pathogens homing on their host tissues, cell division processes and protein regulations and interactions.


  • Robust Glycan and Glycopeptide Database
  • Support for MALDI MS/MS and LC-MS/MS Workflows
  • Data Input File Formats
  • Accurate Ranking Mechanism
  • Additional Filters For Precise Results
  • Comprehensive Result Analysis
  • LC-MS and LC- MS/MS Data Processing
  • High Throughput Analysis
  • TMT Quantitation
  • Multi Stage Mass Spectrometry (MSn) Data Analysis
  • Glycopeptide Qualitative Analysis
  • Project Management
  • Draw Glycans
  • Mass Spectra Interpretation


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