Human Collagen Type I

Description

• General description: Collagen constitutes to one-third of the total protein in humans.[1] Collagen fibril is the basic component of the tissues containing collagen. It is predominantly expressed in the extracellular matrix.[1]Type I collagen is a major structural component of skin, bone, tendon, and other fibrous connective tissues. It differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. Type I collagen is a heterotrimer composed of two α1(I) chains and one alpha2(I) chain, which spontaneously form a triple helix scaffold at neutral pH and 37 °C. Purified human collagen solution is produced from neo-natal human fibroblasts that have secreted human extracellular matrix (hECM) using a propriety cell culture production system. This product contains a high monomer content. In vitro cultures were prepared using intensively tested human fibroblast cells and purified using a manufacturing process following applicable aspects of cGMP. The human fibroblast cells have undergone significant testing demonstrating safety from viruses and other adventitious agents. This process contains built-in, validated steps to ensure the inactivation of possible prion and/or viral contaminants.
• Application: Collagen Solution from human fibroblasts has been used as a component of coating solution for human bone marrow chip fabrication.[2] in fibroblast-like synoviocytes culturing.[3]as a coating solution for microchannels for organ chip culture[4]
• Biochem/physiol Actions: Collagen is an essential ingredient of connective tissue. Studies in a Chinese family show that mutation in COL1A1 (collagenase type I) is linked with type I osteogenesis imperfecta.[5][6] Collagen is linked with subchondral turnover of bone, and might have potential as marker to determine the state of joint space narrowing and osteophytes in osteoarthritis.[7]