MALDI-TOF-MS Intact Protein Analysis

The development and quality assessment of biopharmaceuticals, especially protein and peptide drugs, require a series of analytical techniques to assess the integrity of bioactive molecules during formulation and administration. MALDI-TOF-MS provides accurate mass measurement and high-throughput analysis of intact biomolecules ranging from 1 to 100 kDa. This technique can reveal detailed structural information at the molecular level through ion fragments of small molecule samples in 5 minutes. Compared to ESI-MS technology, MALDI-TOF produces fewer multi-charged ions and allows full-spectrum analysis of protein samples without additional deconvolution steps. This method is particularly suitable for determining the chemical modification of proteins and peptide drugs and for identifying the covalent interaction between protein and peptide bioactive substances in polymer drug formulations.

From early research and development, characterization analysis, process optimization to CMC and QC analysis, biopharmaceuticals have complexity and uncertainty in every link. Creative Proteomics provides high resolution mass spectrometry biopharmaceutical solutions to support your product from development to production.

MALDI-TOF-MS Intact Protein Analysis Matrix-assisted laser desorption/ionization (Alexandra et al, 2011).

We Provide but Not Limited to:

  • Molecular weight determination
  • Characterization of monoclonal antibodies (mAb)
  • Qualitative characterization of the covalent interaction of proteins and peptide drugs with polymers
  • Analysis of physical and chemical stability of protein drug samples
  • Analysis of protein / peptide-polymer conjugates in biopharmaceutical formulations
MALDI-TOF-MS Intact Protein Analysis

Characteristics of MALDI-TOF-MS Intact Protein Analysis Service:

  • High throughput and high selectivity. High resolution: ~ 20000. High sensitivity: ~ fmol, amol. High quality accuracy: <500 ppm.
  • High tolerance to buffer solutions, detergents and contaminants.
  • Not suitable for reliable detection of low molecular weight compounds (less than 500 m / z).
  • The ions generated by MALDI contain less charge, so it is easy to obtain and interpret data, and the analysis speed is fast.

Sample Requirements

  • Purity: >90%.
  • Range: 1 kDa~100 kD.
  • Quantity: >40ug.
  • Acceptable buffers: ammonium acetate, ammonium bicarbonate, and ammonium formate.
  • Avoiding buffer: HEPES, PBS, MES, MOPS, and Tris.
  • Avoiding detergents: SDS, PEG, PPG, Tween, CHAPS, Triton, and urea.
  • Avoiding salts: alkylammonium salts, guanidinium salt, metal cations and inorganic anions such as phosphate, sulfate, and halides.

Creative Proteomics' analytical scientists can provide customers with MALDI-TOF-MS intact protein analysis service. We will deliver raw data, concise and clear results report, detailed bioinformatics analysis reports.


  • Kafka A P, Kleffmann T, et al. The application of MALDI TOF MS in biopharmaceutical research. International journal of pharmaceutics, 2011, 417(1-2): 70-82.
  • Staub A, Guillarme D, et al. Intact protein analysis in the biopharmaceutical field. Journal of pharmaceutical and biomedical analysis, 2011, 55(4): 810-822.
  • Shubhakar A, Kozak R P, et al. Automated high-throughput permethylation for glycosylation analysis of biologics using MALDI-TOF-MS. Analytical chemistry, 2016, 88(17): 8562-8569./

*For Research Use Only. Not for use in the treatment or diagnosis of disease.

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