Rat Collagen Type I

General description
Collagen is an extracellular matrix protein comprising triple helical structure. The structure of collagen type I, in particular, is characterized by the presence of three identical α-chains in its homotrimetric form. Among these three α-chains, one exhibits slight sequence variation.[1] Type I collagen was first isolated from rat-tail tendon, has two main α chains (α and α ) and one β chain.[2] Application
Collagen, Type I solution from rat tail has been used for coating culture plates and dishes for human hepatocyte HepG2 cell line[3] and podocytes.[4] It has also been used as a standard for total collagen content calibration curve generation for the quantification of liver extracellular matrix pre-gel.[5] Used as a coating material to support adherent cells growth and differentiation.
Biochem/physiol Actions
Collagen protein 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.[6] It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.[2] Features and Benefits
Sourced from rat tail.
Sterile-filtered to minimize contamination risks.
Suitable for a wide range of cell culture applications.
Provides optimal surface coverage (6-10 μg/cm2) for promoting cell adhesion and proliferation.
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
When C3867 is first removed from the cooler it will appear gelled. When it is allowed to come fully to 37°C it will appear as a liquid.
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.