Prokaryotic expression and functional study of a novel recombinant human-derived collagen
新型促细胞粘附重组人源性胶原的原核表达及功能性研究

The DNA sequences, which originated from gene COL1A1, optimized for E.coli codon usage and contained cell adhesion domains of GER units, was amplified by RT-PCR technology from human tissue. The recombinant expression vector pET28a( )-COL encoded the recombinant human-derived collagen (RHDC) was constructed and transformed host E.coli strain BL21(DE3)pLysS. The RHDC production was induced by the addition of IPTG and approximately 40% of the total strain proteins. RHDC could form a triple-helical structure suggested by the SDS-PAGE and Western blot analysis. Cell adhesion assay indicated that RHDC had high cell adhesive character, which makes it suitable for use as biomaterials.