Recombinant type III humanized collagen, biochemical grade, Collagen III Protein, has abundant integrin recognition sites, such as GPAGEK, GAPGER and GPAGFR, which can interact with receptors on the surface of fibroblasts to enhance integrin binding. and further regulates cell recognition, adhesion and migration. At the same time, the flexibility and curvature of recombinant humanized type III collagen facilitates better binding with cell receptor proteins.
A total of 28 collagen types have been identified thus far, with types I, II, and III collectively constituting over 90% of the overall collagen. Notably, skin collagen predominantly comprises types I and III.
Origin of Collagen:
Recombinant Collagen-Like Protein: This variant is produced through genetic recombination and bioengineering, closely resembling human collagen in structure and characteristics. Despite modifications in structure that may affect efficacy, there is a certain risk of sensitization.
Recombinant Humanized Collagen: This collagen variant aligns its gene sequence with that of human collagen, boasting excellent tissue compatibility. Recognized as a substance native to the body by the immune system, it can seamlessly penetrate the skin barrier, getting absorbed directly and actively participating in collagen construction at the muscle base, ensuring high utilization and potency.
Type I collagen is predominantly present in the skin, tendons, and various tissues, constituting a significant portion of aquatic product processing waste (skin, bone, and scales) at 80-90% of the total collagen content. Notably, it finds extensive application in medicine. A distinctive characteristic of fish collagen's type I is its relatively low thermal stability, coupled with specificity to fish species.
