Collagen is an extracellular matrix protein comprising triple helical structure. Homotrimetric collagens have three identical α-chains. Type I collagen have one α-chain different in sequence among the three. Type I collagen was first isolated from rat-tail tendon, has two main α chains (α and α ) and one β chain.
Collagen, Type I solution from rat tail has been used for coating culture plates and dishes for human hepatocyte HepG2 cell line and podocytes. It has also been used as a standard for total collagen content calibration curve generation for the quantification of liver extracellular matrix pre-gel.
Used as a coating material to support adherent cells growth and differentiation.
Collagen is essential for the mechanical integrity of tendons and bone. Rat tail tendon collagen is used in tissue engineering especially in the generation of 3-D scaffolds based gels. It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.
Recommended for use as a cell culture substratum. May not be suitable for 3-D gel formation.
Sterile solution prepared from rat tail tendons by a modification of the published extraction method 1. It is supplied as an aqueous solution in 20mM acetic acid with a protein concentration as stated on the bottle. (approx.100mg protein per vial). Protein concentration was estimated by the Biuret method 2.
SDS polyacrylamide gel electrophoresis analysis shows the typical band pattern for Type I collagen, with a doublet at apparent molecular weights of 115 and 130kDa and another doublet at 215 and 235kDa. Based on this analysis, the purity of the collagen sample is >95%.
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.