Recombinant Human LGALS9B, N-His

Description of Recombinant Human LGALS9B, N-His

Introduction

Recombinant Human LGALS9B, also known as Galectin-9B, is a protein that is produced through the process of recombinant DNA technology. This technology involves inserting the gene for LGALS9B into a host cell, such as bacteria or yeast, and allowing the host cell to produce the protein. Recombinant Human LGALS9B has been extensively studied for its structure, activity, and potential applications in various fields.

Structure of Recombinant Human LGALS9B

Recombinant Human LGALS9B is a member of the galectin protein family, which are characterized by their ability to bind to specific sugar molecules. It is composed of 353 amino acids and has a molecular weight of approximately 39 kDa. The protein has a conserved carbohydrate recognition domain (CRD) at its N-terminus, which is responsible for its binding to specific sugar moieties. It also has a C-terminal domain that is responsible for its multimerization and interaction with other proteins.

Studies have shown that the structure of Recombinant Human LGALS9B is similar to that of its naturally occurring counterpart. This is important as it ensures that the protein is able to perform its functions effectively. Additionally, the recombinant production of LGALS9B allows for modifications to be made to the protein, such as the addition of tags for purification or the introduction of mutations to study the protein’s function.

Activity of Recombinant Human LGALS9B

Recombinant Human LGALS9B has been found to have various activities, including its ability to bind to specific sugar molecules, interact with other proteins, and modulate immune responses. The CRD of LGALS9B allows it to bind to glycosylated proteins, such as integrins and CD44, which are involved in cell adhesion and migration. This interaction can affect various cellular processes, such as cell signaling and proliferation.

Furthermore, Recombinant Human LGALS9B has been shown to interact with various immune cells, such as T cells, natural killer cells, and dendritic cells. This interaction can modulate immune responses, including cell activation, proliferation, and cytokine production. Studies have also shown that LGALS9B has anti-inflammatory properties and can induce immune tolerance, making it a promising molecule for the treatment of autoimmune diseases and organ transplantation.

Applications of Recombinant Human LGALS9B

Due to its various activities, Recombinant Human LGALS9B has potential applications in different fields, including immunology, cancer research, and drug development. In immunology, LGALS9B has been studied for its role in regulating immune responses and its potential as a therapeutic target for various diseases. In cancer research, LGALS9B has been found to play a role in tumor progression and metastasis, making it a potential target for cancer therapy.

Moreover, Recombinant Human LGALS9B has been investigated for its potential use as a biomarker for various diseases, such as autoimmune diseases and cancer. Its ability to bind to specific sugar molecules on the surface of cells makes it a useful tool for identifying and studying these diseases.

Furthermore, the recombinant production of LGALS9B allows for large-scale production of the protein, making it more accessible for research and potential therapeutic use. It also allows for modifications to be made to the protein, such as the addition of drug-binding domains, to enhance its potential as a therapeutic agent.

Conclusion

In conclusion, Recombinant Human LGALS9B is a protein that has been extensively studied for its structure, activity, and potential applications in various fields. Its ability to bind to specific sugar molecules and modulate immune responses make it a promising molecule for the treatment of various diseases. With further research and development, Recombinant Human LGALS9B has the potential to contribute to the