Services We Provide

Agile BioScience: Ensuring quality and confidence in your protein characterization.

Agile BioScience specializes in comprehensive protein and biotherapeutic analysis. Their expertise spans amino acid analysis, glycosylation profiling, peptide mapping, and intricate structural characterization. They employ cutting-edge techniques like mass spectrometry and chromatography to ensure accurate results. Agile BioScience partners with clients to deliver the data essential for confident drug development.

What We Do

N-terminal Sequencing

Showing that the N-terminus of your protein is intact and as expected. Demonstrating batch-to-batch consistency. Unambiguously defining the Isoleucine and Leucine residues within the protein sequence

C-terminal sequencing

C-terminus or the presence of ragged ends can be assessed using data obtained from a peptide map.

Peptide Mapping

Enabling you to meet the structural characterization requirements of the ICH Q6B guidelines, understand the primary structure of your protein, assess post translational modifications (PTMs)

N-Linked and O-Linked Glycosylation

N-glycans and O-glycans from a glycoprotein using mass spectrometry and chromatographic analytical processes.

Protein Disulfide Bond identification

Determined through peptide mapping and LC MS

Oligosaccharide profiling

Chromatography analysis of 2-AB labelled oligosaccharides covering the analysis of total N-glycans

Intact molecular weight analysis

By LC MS Intac mass Reduced mass Post N-Glycan Removal Both Reduced and N-Glycan removal

icIEF

Charge Differences Due To Post Translational Modifications Charge Differences Due To C-terminal Lysine Charge Differences Due to Glycosylation Isoform fraction collection and analysis by LC MS/chromatography

CE-SDS

Non reducing and reducing

RP-HPLC with PDA detection

Analysis of Proteins, Peptides and Monoclonal antibody

Ion Exchange Chromatography

Isoform Characterization

DSC

Assess thermal transitions of biopharmaceuticals, such as unfolding. This technique can be utilized to assess conformational stability and also provide the melting temperature of the protein.

CD

For far-UV (for secondary structure) and near UV (for tertiary structure) α-helices and β-sheets have specific CD profiles and use changes in these spectra to assess samples and determine if there are any structural changes.

FT-IR

Provide qualitative and quantitative information on the secondary structure of proteins such as α helices, β sheets, β turns and disordered structures.

SEC-MALS

Multimers and aggregates using a combination of methods. Regulatory authorities commonly request data obtained from SEC-MALS

SV-AUC

Orthogonal aggregation determination, particularly to assess soluble antibody aggregates with diameters less than 100nm

Mico Flow Imaging (MFI)

Sizing, Quantifying, Visualizing and Identifying (Sub-)Visible Particles.

Amino Acid Analysis

Estimate the protein concentration and extinction coefficient.