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ProteoGenix
Recombinant Proteins
Escherichia coli (E. coli)
Elisa, WB
Human Hepatitis A virus cellular receptor 2 (HAVCR2), also known as T cell immunoglobulin and mucin domain-containing protein 3 (TIM-3), is a transmembrane protein that is encoded by the HAVCR2 gene. The protein is composed of 301 amino acids and has a molecular weight of approximately 33 kDa. It is primarily expressed on the surface of immune cells, such as T cells, natural killer cells, and dendritic cells.
The structure of HAVCR2 is characterized by an extracellular region, a transmembrane domain, and a cytoplasmic tail. The extracellular region contains an immunoglobulin variable (IgV)-like domain and a mucin-like domain. The IgV domain is responsible for binding to its ligand, galectin-9, while the mucin-like domain is involved in cell adhesion and signaling. The transmembrane domain anchors the protein to the cell membrane, while the cytoplasmic tail contains signaling motifs that are important for downstream signaling.
The primary function of HAVCR2 is to regulate immune responses. It is a negative regulator of T cell responses, and its activation leads to suppression of T cell proliferation and cytokine production. This is achieved through the binding of galectin-9 to the IgV domain of HAVCR2, which triggers downstream signaling events that inhibit T cell activation. Additionally, HAVCR2 has been shown to play a role in the regulation of immune cell death and tolerance.
Apart from its role in immune regulation, HAVCR2 has also been implicated in other biological processes. It has been shown to play a role in the maintenance of immune homeostasis in the gut, as well as in the regulation of allergic responses. Furthermore, HAVCR2 has been linked to the progression of certain autoimmune diseases, such as multiple sclerosis and rheumatoid arthritis.
Given its role in immune regulation, HAVCR2 has emerged as a potential drug target for various diseases. One potential application of HAVCR2 is in the treatment of autoimmune diseases. By targeting HAVCR2, it may be possible to modulate immune responses and reduce inflammation in these conditions. In fact, several clinical trials are currently underway to investigate the efficacy of HAVCR2-targeting drugs in autoimmune diseases.
Another potential application of HAVCR2 is in cancer therapy. HAVCR2 has been shown to be overexpressed in certain types of cancer, and its activation has been linked to tumor progression and immune evasion. By targeting HAVCR2, it may be possible to enhance anti-tumor immune responses and improve the efficacy of cancer immunotherapy.
In addition, HAVCR2 has also been explored as a biomarker for various diseases. Its expression has been correlated with disease severity and progression in certain autoimmune diseases and cancers. Therefore, measuring HAVCR2 levels may be useful for disease diagnosis, prognosis, and monitoring of treatment response.
In conclusion, Human Hepatitis A virus cellular receptor 2 recombinant protein CD366 is a structurally and functionally diverse protein with important roles in immune regulation and disease pathogenesis. Its potential as a drug target and biomarker makes it an intriguing candidate for further research and development in various disease contexts.
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