Collagen is a fibrous protein that consists of three α-chains that can combine to form a rope-like triple helix, providing tensile strength to the extracellular matrix (ECM) where it plays a key role in cell growth, differentiation, attachment, and cell migration. The α-chains contain GXY repeats. Glycine (G) is a small amino acid that fits well in the triple helix. X and Y are typically proline and hydroxyproline, which is critical for collagen stability. Type I is the most common fibrillar collagen (90%) and is mostly found in skin, bone, tendons, and other connective tissues.
Bovine tail collagen I can be prepared as a clear gel providing a 3D matrix or surface coated on tissue culture plates as a substrate for culturing primary cells such as keratinocytes and hepatocytes. The bovine tail collagen I offered here is supplied at a concentration of 5 mg/mL, providing the flexibility to dilute to lower concentrations.