COL1A1, Recombinant, Human (Collagen alpha-1(I) Chain, Alpha-1 Type I Collagen)
Description
Purity ~80% (SDS-PAGE). Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a procollagen molecule which is characterized by a 300nm triple helical domain flanked by globular N- and C-terminal propeptides. The triple helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues. Type I collagen is a heterotrimer that consists of two alpha1(I) chains and one alpha2(I) chain, although homotrimers consisting of three identical alpha1 (I) chains have also been described. This recombinant mini pro-alpha1(I) collagen is a homotrimer of three shortened alpha1(I) chains with following domain structure from N-to C-terminus: N-propeptide, N-telopeptide, the 33 most