Bovine Collagen Type I

Collagen type I is a component of skin, bone, tendon, and other fibrous connective tissues. It consists of repeating triplet amino acids glycine, proline and hydroxyproline. Collagen is a left handed helix with three polypeptide chains. It is a component of extracellular matrix and as close to 28 types are present in bovine.

Collagen from calf skin has been used:

• for pre-coting glass slides for immunofluorescence studies
• as a cell adhesion factor and modification of poly(vinylidene fluoride-trifluoroethylene) (P(VDF-TrFE)) films for neuron culture
• for coating culture dishes for murine embryonic fibroblasts culture

This product is intended to produce thin layer coatings on tissue culture plates to facilitate attachment of anchorage-dependent cells, recommended for use at 6-10 μg/cm². It is NOT intended for production of 3-D gels. Type I collagen is often used in cell culture as an attachment substratum with myoblasts, spinal ganglia, hepatocytes, embryonic lung, heart explants, fibroblasts, endothelial cells, and islet cells have all been cultured successfully on films or gels of type I collagen. Collagen type I may also be used in research of Idiopathic pulmonary fibrosis (IPF), studies on the effect of ER stress IPF on lung fibroblasts. Collagen in acidic solution can produce three dimensional scaffolding with use in bioengineering and cell culture applications.

Collagen type I on heat denaturation results in disruption of triple helix to a randomly coil. Mutations in the collagen gene are implicated in a variety of cattle diseases. It has applications in food and cosmetics. Collagen is used as a biomaterial and as a tissue scaffold in tissue engineering. Collagen type I fiber assembly is very crucial for physiological processes and cellular signaling.

This product is a 0.1% (1mg/ml) solution of calf skin collagen 0.1 M acetic acid. The product′s appearance is turbid, milky white solution. It is recommended that dilutions of product are prepared in sterile water. Please refer to information given on the product information sheet prior to introduction of product to cells and media.

All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition.

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.