Bovine Collagen Type I

General description
In mammals, collagen type 1 is a widely expressed fibrous protein.[1] It constitutes to one-third of the total protein in humans.[2] Collagen fibril is the basic component of the tissues containing collagen. It is predominantly expressed in the extracellular matrix,[2] and is also found in arterial walls,[3] tendons, ligaments, skin, cornea, bone and dentin.[1] Collagen structure possesses a triple helix polypeptide strand.[2] Application
Collagen solution from bovine skin has been used as a substrate in cell adhesion assay.[4] This highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals
Biochem/physiol Actions
Collagen type 1 is a versatile building material required for tissue elasticity and maintains the stability and strength in a variety of tissues.[1] Collagen is also present in byssus thread of invertebrates, which helps in surface attachment.[1] Defective collagen affects the biomechanical property of arterial tissue.[3] In 3D environments, cell extensions can use integrins on cell surfaces to activate specific signaling pathways and integran-independent mechanical interactions resulting from the entanglement of matrix fibrils is possible.
Preparation Note
This product is prepared from type I bovine collagen purified and extracted from skin and contains a high monomer content. The raw collagen used to prepare this product has been isolated from a closed herd and purified with a GMP manufacturing process that includes inactivation of any possible prion or viral contamination. As supplied, it is a 6 mg/mL aqueous solution in 0.01 M HCl at a pH of 2.0.
Other Notes
Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.
Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.