Recombinant Human COL1A1 protein

**Background of COL1A1 Recombinant Protein**

COL1A1 (Collagen Type I Alpha 1 Chain) is a critical gene encoding the α1 chain of type I collagen, the most abundant structural protein in vertebrates. Type I collagen, a fibrillar collagen, forms a triple helix composed of two α1 chains and one α2 chain (α1[I]₂α2[I]). It is a major component of the extracellular matrix (ECM) in connective tissues, providing tensile strength to organs such as skin, bones, tendons, and blood vessels. COL1A1 mutations are linked to osteogenesis imperfecta (brittle bone disease), Ehlers-Danlos syndrome, and fibrosis.

Recombinant COL1A1 protein is produced using biotechnological systems (e.g., mammalian, insect, or bacterial cells) to express the engineered gene, enabling controlled synthesis without animal-derived impurities. This approach ensures high purity, reproducibility, and reduced immunogenicity, addressing limitations of traditional collagen extraction from animal tissues. The recombinant protein retains key functional domains, including the N-terminal propeptide, central triple-helical region rich in Gly-X-Y repeats, and C-terminal propeptide, which mediate fibril assembly and cellular interactions.

Research applications include studying collagen biosynthesis, ECM remodeling, and disease mechanisms. Recombinant COL1A1 is also used in tissue engineering (e.g., scaffolds for bone or skin regeneration), drug delivery systems, and 3D cell culture models. Its role in modulating cell adhesion, migration, and differentiation makes it valuable for regenerative medicine. Additionally, engineered variants help investigate structure-function relationships or develop therapeutic strategies targeting collagen-related disorders.

Overall, COL1A1 recombinant protein bridges fundamental research and translational innovation, offering insights into connective tissue biology and advancing biomedical applications.