Recombinant Human SPARC/Osteonectin Protein, N-His-SUMO

Description of Recombinant Human SPARC/Osteonectin Protein, N-His-SUMO

Introduction to Recombinant Human SPARC/Osteonectin Protein

Recombinant Human SPARC/Osteonectin Protein, also known as Secreted Protein Acidic and Rich in Cysteine, is a multifunctional glycoprotein that is encoded by the SPARC gene. It is a member of the matricellular protein family, which plays a crucial role in the regulation of cell-matrix interactions and tissue remodeling. SPARC is expressed in various tissues and has been found to be involved in a wide range of physiological processes, such as cell proliferation, differentiation, adhesion, and migration.

Structure of Recombinant Human SPARC/Osteonectin Protein

The SPARC protein is composed of 303 amino acids and has a molecular weight of approximately 43 kDa. It contains an N-terminal acidic domain, a follistatin-like domain, a calcium-binding EF-hand motif, and a C-terminal extracellular calcium-binding (EC) domain. The follistatin-like domain is responsible for the interaction with various growth factors, while the EC domain mediates the binding of SPARC to extracellular matrix proteins, such as collagen and fibronectin.

The recombinant form of SPARC is produced by cloning the SPARC gene into an expression vector and then expressing it in a suitable host cell, such as E. coli or Chinese hamster ovary (CHO) cells. This allows for the production of large quantities of pure and biologically active SPARC protein.

Activity of Recombinant Human SPARC/Osteonectin Protein

SPARC has been shown to have a wide range of activities, including both intracellular and extracellular functions. Inside the cell, SPARC can regulate gene expression, cell cycle progression, and cytoskeletal organization. Extracellularly, it can modulate cell-matrix interactions and affect the activity of growth factors and cytokines.

One of the key functions of SPARC is its role in tissue remodeling and wound healing. It has been found to promote the migration and adhesion of various cell types, such as fibroblasts, endothelial cells, and immune cells, to the site of injury. Additionally, SPARC can stimulate the production of extracellular matrix proteins, such as collagen and fibronectin, which are essential for tissue repair and regeneration.

Moreover, SPARC has been shown to have anti-angiogenic properties, meaning it can inhibit the formation of new blood vessels. This is important in the context of cancer, as tumors require a blood supply in order to grow and metastasize. By inhibiting angiogenesis, SPARC can potentially slow down tumor growth and metastasis.

Application of Recombinant Human SPARC/Osteonectin Protein

Due to its diverse functions, SPARC has been studied for its potential therapeutic applications in various diseases. One of the main areas of interest is in cancer treatment. As mentioned earlier, SPARC has anti-angiogenic properties, making it a potential target for anti-cancer therapies. Additionally, SPARC has been found to be downregulated in many cancers, and its reintroduction has been shown to inhibit tumor growth and metastasis in preclinical studies.

SPARC has also been studied for its potential in tissue engineering and regenerative medicine. Its ability to promote cell adhesion and extracellular matrix production makes it a promising candidate for enhancing tissue repair and regeneration. It has been used in combination with other growth factors and biomaterials to improve the healing of bone, cartilage, and skin injuries.

Furthermore, SPARC has been investigated for its role in various other diseases, such as fibrosis, cardiovascular disorders, and neurodegenerative diseases. Its involvement in tissue remodeling and cell-matrix interactions makes it a potential target for therapeutic interventions in these conditions.

Conclusion

In summary, Recombinant Human SPARC/Osteonectin