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ProteoGenix
Recombinant Proteins
Mammalian cells
Elisa, WB
Human Baff, also known as TNFSF13B, is a protein that plays a crucial role in the immune system. It belongs to the tumor necrosis factor (TNF) superfamily and is involved in regulating B cell survival and maturation. In this article, we will discuss the structure, activity, and potential applications of human Baff as a drug target.
Human Baff is a type II transmembrane protein that is expressed on the surface of various immune cells, including B cells, T cells, and dendritic cells. It is composed of 285 amino acids and has a molecular weight of approximately 32 kDa. The protein consists of a cytoplasmic domain, a transmembrane domain, and an extracellular domain. The extracellular domain is further divided into a stalk region and a TNF homology domain.
The TNF homology domain of human Baff is responsible for its biological activity and is highly conserved among different species. It contains a beta-sheet sandwich structure and a trimerization motif, which allows the protein to form homotrimers. These homotrimers are essential for the binding of human Baff to its receptor, B cell maturation antigen (BCMA), and other receptors such as transmembrane activator and calcium-modulating cyclophilin ligand interactor (TACI) and B cell-activating factor receptor (BAFF-R).
Human Baff is primarily involved in regulating B cell survival and maturation. It does so by binding to its receptors on B cells and promoting their proliferation and differentiation. In addition to its role in B cell development, human Baff also plays a crucial role in the maintenance of peripheral B cell populations and the production of antibodies.
Furthermore, human Baff has been found to be involved in the pathogenesis of various autoimmune diseases, including systemic lupus erythematosus, rheumatoid arthritis, and Sjogren’s syndrome. In these diseases, the dysregulation of human Baff leads to an increase in B cell survival and activation, resulting in the production of autoantibodies and tissue damage.
Given its critical role in the immune system and its involvement in autoimmune diseases, human Baff has emerged as a potential drug target for the treatment of these disorders. Several strategies have been developed to target human Baff, including monoclonal antibodies, soluble receptors, and small molecule inhibitors.
Monoclonal antibodies against human Baff, such as belimumab, have been approved for the treatment of systemic lupus erythematosus. These antibodies bind to human Baff and prevent it from interacting with its receptors, thereby reducing B cell survival and activation. Similarly, soluble receptors, such as atacicept, have been shown to be effective in reducing disease activity in patients with rheumatoid arthritis and systemic lupus erythematosus.
Small molecule inhibitors of human Baff, such as tabalumab and blisibimod, have also been developed and are currently in clinical trials for the treatment of autoimmune diseases. These inhibitors target the interaction between human Baff and its receptors, thereby reducing B cell survival and activation.
Human Baff is a crucial protein in the immune system, involved in regulating B cell survival and maturation. Its dysregulation has been linked to the pathogenesis of various autoimmune diseases, making it a potential drug target for the treatment of these disorders. With the development of new therapies targeting human Baff, it is hoped that these treatments will provide more effective and targeted options for patients with autoimmune diseases.
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