Bioanalytical Characterization

Characterization and quantification of acetylation as a post-translational modification (PTM). This analysis evaluates its impact on protein structure, stability, and biological function, supporting CQA assessment and product consistency.

Comprehensive analysis of protein aggregation, including detection, characterization, and quantification of soluble and insoluble aggregates. We assess size distribution, structural properties, and formation pathways to support stability studies and manufacturing process optimization.

Quantitative determination of amino acid composition for protein therapeutics. This method supports protein concentration determination, identity confirmation, and lot-to-lot consistency.

Forced degradation and stress studies to evaluate protein stability under thermal, oxidative, pH, and mechanical conditions. This testing helps identify degradation pathways and supports formulation development and stability-indicating methods.

Analysis of C-terminal lysine variants in monoclonal antibodies to assess heterogeneity and enzymatic processing. This characterization supports product consistency and comparability studies.

Separation and characterization of charge variants arising from sequence modifications or PTMs (e.g., deamidation, sialylation, C-terminal lysine). These studies are critical for understanding heterogeneity, stability, and biological activity.

Characterization and quantification of deamidation at asparagine (Asn) residues, a critical post-translational modification that can impact protein stability, charge heterogeneity, and biological activity. This analysis supports CQA assessment and stability studies.

Comprehensive analysis of protein glycosylation, including glycan identification, quantification, and site-specific mapping. We characterize glycoform distribution, structure, and heterogeneity to support product quality, efficacy, and regulatory requirements.

Detection and characterization of residual host cell proteins using orthogonal methods such as ELISA and LC-MS/MS. This analysis supports process development, impurity profiling, and regulatory compliance.

Identification and characterization of protein isomers, including isoaspartate formation and other structural variants. This analysis helps assess structural integrity, degradation pathways, and potential impact on function and stability.

Characterization of terminal variants to identify truncation sites, sequence integrity, and relative abundance. This analysis supports assessment of product heterogeneity, stability, and process-related modifications.

Quantification and site-specific characterization of oxidative modifications (e.g., methionine, tryptophan oxidation). This analysis evaluates the impact of oxidation on protein stability, structure, and biological activity.

Comprehensive characterization of proteins using LC-MS/MS-based peptide mapping. This analysis confirms amino acid sequence, identifies and quantifies post-translational modifications (PTMs), and assesses structural integrity to support CQA evaluation and regulatory submissions.

Identification and site-specific characterization of phosphorylation as a critical post-translational modification. This analysis evaluates its impact on protein structure, function, and biological activity.

Comprehensive profiling of PTMs, including identification, site localization, and relative quantification. This analysis provides insights into protein heterogeneity, stability, and functional impact.

Accurate identification of proteins and peptides using high-resolution LC-MS/MS. This analysis confirms molecular identity through peptide sequencing and mass analysis, supporting product characterization and impurity assessment.

This determines the percentage of a protein’s amino acid sequence identified through peptide fragment analysis. This represents the distribution of detected peptides across the protein, providing insight into sequence coverage.

This measures the extent to which a product retains, within specified limits, and throughout its period of storage and use, the same properties and characteristics that it possessed at the time of manufacturing.

This characterizes protein structure modifications by breaking down the antibody into smaller subunits to determine structural quality attributes such as deamidation, oxidation, glycation, aggregation, and glycosylation patterns.

This breaks down proteins into subunits to characterize their structure, integrity, and post-translational modifications (PTMs).

This detects and characterizes how a protein maintains its structure and function at different temperatures.