Collagen, Type I solution from rat tail

General description

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.

When C3867 is first removed from the cooler it will appear gelled. When it is allowed to come fully to ambient room temperature it will appear as a liquid.

Application

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.

Biochem/physiol Actions

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.

Preparation Note

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%.

Other Notes

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.