Lactoferrin Characterization

Detailed profiling of N-glycans and site-specific glycosylation

• Identification of glycosylation sites and occupancy
• Structural characterization of glycans (e.g. fucosylation, sialylation)
• Comparison of glycoform distributions between samples

Why it matters:

Glycosylation patterns vary significantly between sources and directly influence biological activity and functionality.

Holistic analysis of lactoferrin heterogeneity

• Intact mass determination (Top‑down MS)
• Proteoform distribution (combined PTMs, glycoforms)
• Batch-to-batch comparability

Why it matters:

Lactoferrin exists as multiple coexisting molecular variants (proteoforms), which are critical for quality and reproducibility

Characterization of iron occupancy states

• Differentiation between apo-, mono- and holo-lactoferrin
• Quantification of iron-loaded fractions

Why it matters:

Iron-binding is central to lactoferrin’s antimicrobial and nutritional functionality

Quality control for industrial and regulatory requirements

• Detection of protein impurities and degradation products
• Assessment of sample purity and homogeneity

Why it matters:

High purity levels are essential for food and pharmaceutical applications (>95% typical requirement).

Verification of product origin and integrity

• Differentiation between bovine, human and recombinant lactoferrin
• Detection of adulteration or compositional inconsistencies

Why it matters:

Lactoferrin profiles provide valuable information for authentication and product quality assessment.

Benchmarking recombinant vs. native lactoferrin

• Structural comparability analysis
• Glycosylation matching
• Functional-relevant differences

Ideal for:

• Precision fermentation companies
• Alternative protein developers