We offer comprehensive analyses of extracellular matrix proteins as service to biomedical, pharmaceutical, cosmetics and food companies or as part of research collaborations. Our key competence is a detailed collagen analysis in tissues or cell culture material (e.g. Tissue engineering products). We assess the collagen, elastin and total protein content in a given specimen. In addition, we analyse the cross-link pattern of both collagen and elastin. The cross-link pattern of any specimen is not only a marker for its biomechanical capacity but also for newly synthesized collagen, activated fibroblasts or fibrotic tissue. Various degradation tests serve to analyse the biochemical stability of the tissue specimen.

The analyses in detail

Analysis of collagen

• collagen content (hydroxyproline content; amino acid analysis)
• collagen types (collagen types I, II, II, V; SDS gel electrophoresis)
• collagen cross-links (HP, LP, HHL, DHLNL, HLNL, HHMD; amino acid analysis and HPLC)
• collagen glycosylation (galactosylhydroxylysine, glucosyl-galactosylhydroxylysine; amino acid analysis)
• collagen glycation (advanced glycation end products – pentosidine; HPLC)
• collagen stability (denaturation by DSC – differential scanning calorimetry)
• degree of hydroxylation (hydroxyproline/proline, hydroxylysine/lysine; amino acid analysis)
• purity of collagen (amino acid composition / 1000 amino acids)
• content of denatured collagen (chymotrypsin assay)
• degradability (MMP-assay)

Anaylsis of elastin

• elastin content (amino acid anaylsis)
• elastin cross-links (desmosine, isodesmosine; amino acid analysis)
• elastin purity (amino acid composition / 1000 amino acids) 

Analysis of recombinant proteins

• Protein content / protein purity (amino acid composition)
• Glycosylation by amino acid analysis (N-acetylglucosamine, N-acetylgalactosamine; amino acid analysis)