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    O-Glycan Modification and Modification Site Analysis Service

      O-glycosylation is catalyzed by specific enzymes, such as O-glycosyltransferases, which recognize certain protein sequences and structures and transfer sugar units from donor molecules, typically nucleotide sugars, to amino acid residues on proteins. This glycosylation differs from N-glycosylation as it occurs at more varied sites and involves diverse sugar types, without relying on a consensus sequence. O-glycosylation predominantly affects serine (Ser) or threonine (Thr) residues, and occasionally tyrosine (Tyr) residues. Common in extracellular and transmembrane proteins, particularly those involved in cell signaling, recognition, and immune responses, O-glycosylation is crucial for protein function and stability, influencing protein folding, distribution, secretion, and interactions with other molecules. Additionally, it impacts biological activities, such as hormone and growth factor regulation and immune recognition.

       

      O-glycosylation involves linking sugar units to proteins, enhancing their diversity and functionality. Glycosylation analysis identifies the amino acid residues involved and the specific glycosylation types, essential for understanding protein functions, pathological state changes, and biopharmaceutical development. This analysis is vital in the biopharmaceutical industry to ensure drug consistency and activity, especially in producing recombinant proteins or antibodies.

       

      At MtoZ Biolabs, we enhance our O-glycan modification and site analysis services by focusing on four key areas: enrichment of O-glycoproteins and peptides, cleavage of O-glycans, structural determination of O-glycans, and their quantitative assessment. Simply inform us about the objectives of your study and provide your samples. Our dedicated team will handle all subsequent aspects of your project, ensuring comprehensive support and detailed analysis.

       

      o-glycan-modification-and-modification-site-analysis-service1

      Cavallero, GJ. et al. Anal Bioanal Chem. 2022.

      Figure 1. The Main synthetic Pathway of O-glycosylation

       

      Analysis Workflow

      1. Extraction and purification of proteins

      2. Digestion of proteins

      3. Enrichment and elution of peptides

      4. Analysis by mass spectrometry

      5. Interpretation of data

       

      Service Advantages

      1. High Sensitivity and Specificity: Advanced mass spectrometry techniques enable the detection of glycosylation modifications at low abundance, ensuring accurate identification and quantification even in complex samples.

      2. Comprehensive Analysis: Beyond identifying glycosylation sites, our services analyze sugar chain types and structures, providing detailed information essential for a deep understanding of protein interactions and functions.

      3. Bioinformatics Support: Professional bioinformatics analyses aid in extracting significant biological insights from data, including statistical analyses and biological interpretations, accelerating research and development.

      4. Customized Technical Support: We tailor our services to meet specific research needs, ensuring adaptability and practical value. Our team supports every analysis step, maintaining high standards.

       

      Applications

      1. Biopharmaceutical Development: O-glycosylation critically influences drugs' pharmacological properties, stability, and immunogenicity, essential for optimizing drug design and improving efficacy and safety.

      2. Disease Diagnosis: Specific glycosylation patterns linked to diseases like cancer and autoimmune disorders help develop diagnostic and monitoring biomarkers.

      3. Functional Studies: By regulating protein structure and function, O-glycosylation reveals complex cellular signaling and interactions, enhancing scientific understanding of these processes.

       

      Sample Requirements

      Protein: Minimum of 100 μg.

      Cells: At least 1x107 cells.

      Animal Tissue: Approximately 1 g.

      Blood: 1 mL, must be anticoagulated with EDTA.

      Serum: Between 0.2 to 0.5 mL.

      Urine: At least 2 mL.

      Microbial Samples: 200 mg in dry weight.

       

      Please note: Should you have any inquiries regarding sample submission, do not hesitate to reach out. Our expert team is available to assist you at all times.

       

      Deliverables

      1. Experimental Procedures

      2. Relevant Mass Spectrometry Parameters

      3. Detailed Information on O-Glycan Modification and Modification Site Analysis 

      4. Mass Spectrometry Images

      5. Raw Data

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