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10 ug, 50ug, 100ug
ProteoGenix
Recombinant Proteins
Escherichia coli (E. coli)
Elisa, WB
Human CD27 is a transmembrane glycoprotein that belongs to the tumor necrosis factor receptor superfamily. It is primarily expressed on the surface of T cells, B cells, and natural killer cells, and plays a crucial role in regulating immune responses. The recombinant form of human CD27 protein has gained significant attention in recent years due to its potential as a drug target for various diseases. In this article, we will delve into the structure, activity, and applications of human CD27 recombinant protein.
The human CD27 protein is composed of 236 amino acids and has a molecular weight of approximately 55 kDa. It consists of a signal peptide, an extracellular domain, a transmembrane domain, and a cytoplasmic tail. The extracellular domain of CD27 contains four cysteine-rich domains, which are important for ligand binding and receptor activation. The cytoplasmic tail of CD27 contains a conserved sequence known as the TNF receptor-associated factor (TRAF) binding motif, which is responsible for downstream signaling. The recombinant form of human CD27 protein is produced by cloning the cDNA sequence into a suitable expression vector and expressing it in a host cell. The purified recombinant protein is a homodimer, with each monomer consisting of the extracellular domain and a portion of the transmembrane domain. The recombinant protein retains its native structure and possesses similar biological activity to the endogenous protein.
Human CD27 protein is primarily known for its role in regulating immune responses. Upon binding to its ligand, CD70, CD27 triggers a series of signaling events that lead to the activation of T cells, B cells, and natural killer cells. This activation results in the production of pro-inflammatory cytokines, proliferation of immune cells, and enhancement of cytotoxicity. In addition to its role in immune regulation, CD27 has also been implicated in the development and maintenance of memory T cells. It has been shown that CD27 plays a critical role in the survival and differentiation of memory T cells, which are crucial for long-term protection against pathogens. Furthermore, CD27 has been linked to the pathogenesis of various diseases, including autoimmune disorders, infectious diseases, and cancer. Dysregulation of CD27 signaling has been observed in these conditions, highlighting the potential of CD27 as a therapeutic target.
The recombinant form of human CD27 protein has been widely used in research and drug development. Due to its ability to activate immune responses, it has been investigated as a potential adjuvant in vaccine development. Studies have shown that co-administration of CD27 protein with antigens can enhance the immune response and improve vaccine efficacy. Moreover, the potential of CD27 as a drug target has led to the development of CD27 agonists and antagonists. CD27 agonists, which activate the receptor, have shown promising results in preclinical studies for the treatment of cancer and infectious diseases. On the other hand, CD27 antagonists, which block the receptor, have been explored as potential treatments for autoimmune disorders. In addition to its therapeutic applications, human CD27 recombinant protein has also been used in diagnostic assays for the detection of CD27 expression on immune cells. This can aid in the diagnosis and monitoring of certain diseases, such as lymphomas and autoimmune disorders.
In summary, human CD27 recombinant protein is a promising drug target with diverse applications in research and medicine. Its well-defined structure and activity make it an ideal candidate for drug development, particularly in the field of immunotherapy. Further research and clinical trials are needed to fully explore the potential of CD27 as a therapeutic target and to bring new treatments to patients in need.”
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