Description

• General description: Collagen is made of three polypeptide chains.[1] Type 2 collagen is ubiquitously present in the hyaline cartilage. It is a homotrimer made of three α1[2] chains.[1] Type 2 collagen is also predominant in nucleus pulposus of the vertebral disc and vitreous body of the eye.[2] The proteoglycan obtained from the chicken sternal cartilage is similar to type nine collagen structure.[3]
• Application: Collagen from chicken sternal cartilage has been used: in enzyme–linked immunosorbent assay (ELISA).[4]chondrocyte-mediated tissue production in vitro.[5]induction, treatment and assessment of collagenα induced arthritis (CIA). [6][7] cell proliferation assay.[8]as a coating for cell culture surfaces.[8]
• Biochem/physiol Actions: Collagen breaks down metabolically in the body to release N-telopeptide, which is the N-terminus of collagen. There is also C-telopeptide, which is presumably the C-terminus. N-telopeptide is released in urine, and its detection in diagnostic tests is used to screen for osteoporosis.
• Features and Benefits: This collagen has been tested in culture with mammalian cells to verify it is low in endotoxin content.
• Other Notes: Major component of articular cartilage.
• Preparation Note: Prepared by a modification of the method of Trentham, D.E., et al.