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.

CN122189092APending Publication Date: 2026-06-12CANTONBIO CO LTD +2
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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

Technical Problem

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.

Method used

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.

Benefits of technology

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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Abstract

The application belongs to the technical field of bioengineering and particularly relates to a preparation method of recombinant collagen type III. The application provides a vector, which comprises a gene encoding collagen and a gene encoding hydroxylase, and a backbone of the vector comprises a first expression cassette, wherein the first expression cassette comprises EF1a-intron A; the collagen is collagen type III; a cell comprising the vector can improve the expression amount of the collagen, and meanwhile, ensures the stable formation of the triple helix structure of the collagen.
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