Description

• 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]
• 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.
• 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.