A method for the production of a recombinant collagen type III
By expressing the collagen in CHO cells and purifying it using salting-out chromatography, the challenges of expressing and purifying full-length recombinant human collagen were solved, enabling the efficient and stable preparation of triple-helix collagen and promoting its application in the medical and aesthetic fields.
Patent Information
- Authority / Receiving Office
- CN Β· China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2025-03-25
- Publication Date
- 2026-06-12
AI Technical Summary
Existing technologies struggle to efficiently express and purify full-length recombinant human collagen with a triple helix structure, resulting in its stability and biological properties being far inferior to those of animal-extracted collagen, thus limiting its application in the medical and aesthetic fields.
A vector containing genes encoding collagen and hydroxylase was used for expression in CHO cells, followed by purification using salting-out chromatography to ensure the stability and high purity of the triple helix structure of collagen.
This study achieved efficient expression and purification of recombinant human collagen with a triple helix structure, enhancing its biological activity and purity. It solved the expression and purification challenges in existing technologies, which is conducive to promoting its commercial application.
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