Recombinant Human Collagen XI alpha 2/COL11A2 protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Collagen XI alpha 2 (COL11A2) also known as alpha-2 chain of type XI collagen plays a mechanical role in the formation of collagen fibrils found in cartilage. This protein has a mass of approximately 178 kDa. COL11A2 is expressed in cartilaginous tissues including articular cartilage and intervertebral discs. Its structural properties help in maintaining the tensile strength and integrity of extracellular matrices in these tissues contributing to skeletal development and joint function.

Biological function summary

Collagen XI alpha 2 is integral to the development and maintenance of cartilage tissue. It is a component of the collagen type XI complex which includes collagen fibers composed of three polypeptide chains: alpha-1 alpha-2 and alpha-3. These fibers regulate the size and spacing of collagen fibrils during cartilage formation ensuring proper bone growth and maintenance. COL11A2 works in coordination with other collagen types such as collagen II and IX to ensure stability and structural cohesion within the cartilage matrix.

Pathways

Collagen XI alpha 2 is essential in the assembly and organization of collagen fibrils within the extracellular matrix which plays a vital role in the bone morphogenetic protein (BMP) signaling pathway and the TGF-beta (transforming growth factor-beta) pathway. These pathways facilitate various cellular processes including cell proliferation and differentiation. COL11A2 interacts with proteins like collagen type II (COL2A1) to modulate these pathways ensuring proper cartilage and skeletal tissue development.

COL11A2 mutations can lead to conditions such as Stickler syndrome and Otospondylomegapiphyseal Dysplasia (OSMED). Stickler syndrome affects connective tissues leading to abnormalities in the eyes bones and ears while OSMED results in skeletal dysplasia. Both disorders relate to structural anomalies in cartilage. The protein shares a linkage with collagen type II in these conditions as alterations in the COL11A2 gene can disrupt the normal interaction between these collagen molecules further impacting skeletal growth and function.