- Primary Structure Analysis
- High-resolution mass spectrometry molecular weight
- MALDI TOF mass spectrometry analysis
- N-terminal sequence analysis
- C-terminal sequence analysis
- N/C terminal sequence analysis
- Analysis of the K deletion ratio at the C-terminus of antibodies
- LC-MS/MS protein full sequence validation
- Peptide coverage / Peptide spectrum analysis
- Protein peptide profile determination
- Amino Acid Composition Analysis
- Extinction coefficient analysis
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- Advanced Structural Analysis
- Charge Heterogeneity Analysis
- Impurity Analysis
- Native Mass Spectrometry
- SDS-PAGE protein purity analysis
- Protein purity analysis (size exclusion/reverse phase chromatography)
- Host Cell Protein Residue (HCP) Analysis Service
- Antibody-Drug Conjugates (ADCs) Analysis
- Protein content analysis
- Product-related impurity analysis
- Analysis of other process-related impurities
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- Special Analysis
- Primary Structure Analysis
How are proteins separated on isoelectric focusing (IEF) gels?
Isoelectric focusing electrophoresis (IEF) is an electrophoretic technique for separating proteins based on their isoelectric points (pI). The pI is the pH at which a protein carries no net charge and does not move in an electric field. IEF gels effectively create a pH gradient, allowing proteins to be separated according to their unique pI.
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