Human Galectin-1 (GAL1) recombinant protein

Description of Human Galectin-1 (GAL1) recombinant protein

The Structure of Human Galectin-1 (GAL1) Recombinant Protein

Human Galectin-1 (GAL1) is a recombinant protein that plays an important role in various biological processes. It is a member of the galectin family, which is a group of proteins that bind specifically to carbohydrates on the surface of cells. GAL1 is a small protein, consisting of 135 amino acids and has a molecular weight of approximately 14.5 kDa. It is composed of two domains, a carbohydrate recognition domain (CRD) and a non-lectin domain. The CRD is responsible for binding to specific carbohydrates, while the non-lectin domain is involved in protein-protein interactions.

The crystal structure of GAL1 has been determined, revealing a unique dimeric structure. The two monomers are held together by a disulfide bond and form a head-to-tail arrangement. The CRD of each monomer is composed of two beta-sheets and a short alpha-helix, which form a pocket for carbohydrate binding. The non-lectin domain is composed of a beta-sheet and a long alpha-helix, which is involved in dimerization. This unique structure allows GAL1 to bind to multiple carbohydrates simultaneously, making it a versatile protein with diverse functions.

The Activity of Human Galectin-1 (GAL1) Recombinant Protein

GAL1 is a multifunctional protein that is involved in various biological processes, including cell adhesion, migration, proliferation, and apoptosis. Its activity is dependent on its binding to specific carbohydrates, which are present on the surface of cells and in the extracellular matrix. GAL1 has a high affinity for beta-galactosides, such as lactose and N-acetyllactosamine, and can also bind to glycoproteins and glycolipids.

One of the key functions of GAL1 is its role in cell adhesion. It can bind to carbohydrates on the surface of cells, promoting cell-cell and cell-matrix interactions. This is important for processes such as wound healing and tissue regeneration. GAL1 also plays a role in cell migration, as it can bind to carbohydrates on the surface of migrating cells, facilitating their movement.

In addition, GAL1 has been shown to modulate cell proliferation and apoptosis. It can promote cell growth in some cell types, while inducing apoptosis in others. This is due to its ability to interact with different signaling molecules and modulate their activity. GAL1 has also been implicated in immune response regulation, as it can bind to carbohydrates on the surface of immune cells and modulate their function.

The Application of Human Galectin-1 (GAL1) Recombinant Protein

Due to its diverse functions, GAL1 has been studied extensively for its potential therapeutic applications. One of the main areas of interest is its role as a drug target. GAL1 has been shown to be overexpressed in various types of cancer, including breast, lung, and colon cancer. It has also been associated with tumor growth, metastasis, and resistance to chemotherapy. Therefore, targeting GAL1 with specific inhibitors could potentially be an effective treatment strategy for these types of cancer.

In addition, GAL1 has also been investigated for its potential in tissue engineering and regenerative medicine. Its ability to promote cell adhesion and migration makes it a promising candidate for promoting tissue repair and regeneration. GAL1 has been used in combination with biomaterials to enhance their properties and promote tissue regeneration in various preclinical studies.

Furthermore, GAL1 has been studied for its potential as a biomarker for various diseases. Its overexpression has been linked to several inflammatory and autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis. GAL1 levels have also been found to be elevated in patients with cardiovascular diseases, making it a potential biomarker for these conditions.

In conclusion, Human Galectin-1 (GAL1) recombinant protein is a versatile protein with a unique structure and diverse functions.