Recombinant Human CILP, N-GST

Description of Recombinant Human CILP, N-GST

Introduction to Recombinant Human CILP, N-GST

Recombinant Human CILP, N-GST is a fusion protein that has been developed for use as a drug target in various diseases. CILP, or cartilage intermediate layer protein, is a protein found in the extracellular matrix of cartilage tissue. It is known to play a role in the maintenance and repair of cartilage, making it a potential therapeutic target for conditions such as osteoarthritis. The addition of the N-terminal glutathione-S-transferase (N-GST) tag to CILP allows for easier purification and detection of the protein, making it a valuable tool in both research and clinical settings.

Structure of Recombinant Human CILP, N-GST

Recombinant Human CILP, N-GST is a fusion protein made up of two distinct components: CILP and the N-GST tag. CILP is a 354 amino acid protein with a molecular weight of approximately 40 kDa. It contains multiple domains, including a von Willebrand factor type C domain, a thrombospondin type 1 repeat, and a C-terminal cysteine-rich domain. These domains are thought to be important for the interaction of CILP with other proteins in the extracellular matrix.

The N-GST tag, on the other hand, is a 26 amino acid sequence that is added to the N-terminus of CILP. This tag is derived from the glutathione-S-transferase enzyme, which is known for its ability to bind to and purify proteins. The addition of this tag allows for easy purification of Recombinant Human CILP, N-GST using standard affinity chromatography techniques.

Activity of this protein

Recombinant Human CILP, N-GST has been shown to have multiple activities, making it a versatile tool in both research and clinical applications. Firstly, CILP has been shown to interact with other proteins in the extracellular matrix, including collagen and aggrecan. This interaction is thought to play a role in the maintenance and repair of cartilage tissue. Additionally, CILP has been shown to have anti-angiogenic properties, meaning it can inhibit the formation of new blood vessels. This activity has potential therapeutic implications in diseases where abnormal blood vessel growth is a contributing factor.

The N-GST tag also contributes to the activity of Recombinant Human CILP, N-GST. As mentioned earlier, the tag allows for easy purification of the protein, making it a valuable tool for researchers studying the role of CILP in various diseases. Additionally, the tag can be used for detection of CILP in biological samples, providing a convenient way to monitor the levels of this protein in different conditions.

Application of Recombinant Human CILP, N-GST

Recombinant Human CILP, N-GST has a wide range of potential applications, particularly in the field of osteoarthritis research. The ability of CILP to interact with other proteins in the extracellular matrix makes it a promising target for the development of therapies that can promote cartilage repair and regeneration. Additionally, the anti-angiogenic activity of CILP may be useful in treating diseases such as cancer, where abnormal blood vessel growth is a contributing factor.

In addition to its potential therapeutic applications, Recombinant Human CILP, N-GST can also be used as a research tool. The easy purification and detection of this protein make it a valuable tool for studying the role of CILP in different biological processes. It can also be used to screen for potential drugs that may interact with CILP and modulate its activity.

Conclusion

In summary, Recombinant Human CILP, N-GST is a fusion protein that combines the activities of CILP and the N-GST tag.