Human Collagen Type II

Description

• General description: Type II collagen, a fibrillar collagen, is the main component of hyaline cartilage and constitutes 95% of the collagens and approximately 60% of cartilage’s dry weight.[1] It is a homotrimer protein encoded by the gene COL2A1, mapped to human chromosome 12q13. Type two Collagen is also found in the nucleous pulposo of the intervertebral disc and the retina, sclera, and lens of the eye.[2] Type IIA, is localized mainly to the vitreous body of the eye. Type IIB, is preferentially produced in adult cartilage tissue.  Collagen type II was purified by using differential salt precipitation, alcohol precipitation and DEAE chromatography. Multiple purification steps provide final preparations of collagen types in the native triple-helical form, free of any non-collagenous protein. Contamination of other collagen types in a standard preparation is lower than five percent.
• Application: Human Collagen Type II has been used:as an extracellular matrix (ECM) protein in microarray analysis, to coat on nitrocellulose film slides for probing and detection experiments[3]to study the role of Col2a1a in the neural crest during early eye development in zebrafish model of Stickler syndrome[4]as a calibration standard in the quantification of collagen II levels in scaffolds using an enzyme-linked immunosorbent assay (ELISA)-based assay[5]
• Biochem/physiol Actions: Type II collagen is commonly co-assembled with collagen XI, forming a complex that is covalently crosslinked to collagen IX and interacts with small leucine-rich proteoglycans. Collagen 2 imparts stability and strength to the tissue and maintains integrity and resilience under stress. Cleavage of Type II collagen occurs mainly through the action of matrix metalloproteinase collagenases, leading to the generation of well-known biomarkers such as the C-terminal telopeptide of Type II collagen and C2C. Mutations in type II collagen cause chondrodysplasia, leading to premature osteoarthritis.[1]
• Physical form: Purified protein. Liquid in 0.5M acetic acid. No preservative.
• Storage and Stability: Aliquot and freeze. Maintain at -20°C up to 12 months. Avoid repeated freeze/thaw cycles.
• Legal Information: CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
• Disclaimer: RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.