Recombinant Human LGALS13, N-GST

Description of Recombinant Human LGALS13, N-GST

Introduction to Recombinant Human LGALS13

Recombinant Human LGALS13, also known as Galectin-13, is a protein that is produced through genetic engineering techniques. It is a member of the galectin family of proteins, which are characterized by their ability to bind to specific sugar molecules on the surface of cells. LGALS13 is a small protein, consisting of 135 amino acids, and is highly conserved among different species.

Structure of Recombinant Human LGALS13

The structure of Recombinant Human LGALS13 is composed of two distinct domains: a carbohydrate recognition domain (CRD) and a non-carbohydrate recognition domain (NCRD). The CRD is responsible for binding to specific sugar molecules, while the NCRD is involved in protein-protein interactions. The two domains are connected by a flexible linker region, which allows for conformational changes and flexibility in binding.

The CRD of LGALS13 is composed of two subdomains, each containing a conserved carbohydrate-binding site. These sites are responsible for the binding of LGALS13 to specific sugar molecules, such as galactose and lactose. The NCRD, on the other hand, is composed of a single subdomain and is involved in binding to other proteins, such as integrins and extracellular matrix proteins.

Activity of Recombinant Human LGALS13

The main activity of Recombinant Human LGALS13 is its ability to bind to specific sugar molecules present on the surface of cells. This binding is mediated by the CRD of LGALS13 and is important for various cellular processes, including cell adhesion, migration, and signaling. LGALS13 has been shown to bind to a variety of cell types, including immune cells, endothelial cells, and cancer cells.

In addition to its role in sugar binding, LGALS13 also has anti-inflammatory properties. It has been shown to inhibit the production of pro-inflammatory cytokines and chemokines, as well as the activation of immune cells. This anti-inflammatory activity is mediated by the NCRD of LGALS13, which interacts with specific receptors on immune cells.

Application of Recombinant Human LGALS13

Recombinant Human LGALS13 has a wide range of potential applications in both research and clinical settings. Its ability to bind to specific sugar molecules makes it a valuable tool for studying cell-surface interactions and signaling pathways. LGALS13 can also be used as a diagnostic tool for certain diseases, as its expression has been linked to various cancers and inflammatory disorders.

Furthermore, LGALS13 has therapeutic potential in the treatment of various diseases. Its anti-inflammatory properties make it a promising candidate for the treatment of inflammatory disorders, such as rheumatoid arthritis and inflammatory bowel disease. Additionally, LGALS13 has been shown to inhibit tumor growth and metastasis, making it a potential target for cancer therapy.

Conclusion

In summary, Recombinant Human LGALS13 is a small protein with a unique structure and multiple functions. Its ability to bind to specific sugar molecules and inhibit inflammation makes it a valuable tool in research and a potential therapeutic agent for various diseases. As research on LGALS13 continues, its potential applications in medicine and biotechnology are likely to expand, making it an important protein in the field of molecular biology.

Keywords: Recombinant protein, antigen, LGALS13, galectin, sugar binding, anti-inflammatory, therapeutic, research, clinical, cancer, immune cells.