Bovine Collagen Type I

Collagen solution is derived by dissolving collagen molecules in an aqueous solution. Collagen type Iα1 (COL1A1) is encoded by the gene that is located on human chromosome 17q21.33. It is the most abundant extracellular matrix (ECM) protein in humans. Type 1 collagen is the major structural protein of bone, tendon, skin and cornea. The encoded protein is a heterotrimer consisting of two α1-chains and one α2-chain.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.

Collagen solution from bovine skin has been used

• in the preparation of collagen gels.
• to coat cell culture dishes for HeLa cell line culture.
• to construct hydrogels laden for HepG2 cell culture.

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

Collagen solution from bovine skin is a 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. Collagen, type I (COL1A1) participates in fibrosis. COL1A1 is an important component of the connective tissue matrix. It plays a vital role in the growth and maintenance of organ and tissue integrity. This protein also participates in the process of tissue repair.

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.

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.

This product ships on wet ice and with recommended storage at 2-8°C, the product will last for 2 years.

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 3 mg/mL aqueous solution in 0.01 M HCl with a pH of 2.0. Collagen denatures when exposed to high temperatures or irradiation. Prior to a pH adjustment, store stock or diluted solutions refrigerated. Following a pH adjustment to 7, solutions should not exceed 40°C and should not be frozen.

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.