Other Names

Huma Collagen, type I, Alpha 1 ELISA Kit

COL1A1; COL-1A1; COL1-A1; COL1A-1; OI4; Collagen Alpha-1(I)chain

Background

Type I collagen is a structural protein that is abundant in skin, bone and other tissues. It is synthesized as a procollagen molecule which is shown as a 300 nm triple helical domain flanked by globular N- and C-terminal propeptides. When the non-helical propeptides are removed by procollagen N-terminal and C-terminal proteinase activities, the mature triple helices are able to self-assemble into collagen fibrils that enhance tensile strength to tissues.

Type I collagen is a heterotrimer in structure, which consists of two alpha 1 chains and one alpha 2 chain. As a heterotrimer in structure, although Type I collagen is also described as homotrimers consisting of three identical alpha 1 chains. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene.