TNFR Human

Tumor Necrosis Factor Receptors (TNFRs) are a group of receptors that play a crucial role in the regulation of immune responses, inflammation, and cell survival. These receptors are part of the larger Tumor Necrosis Factor (TNF) superfamily, which includes various ligands and receptors involved in cell signaling. The human recombinant form of these receptors is used extensively in research and therapeutic applications.

TNFRs are transmembrane proteins that bind to Tumor Necrosis Factor (TNF) ligands. There are two main types of TNFRs: TNFR1 and TNFR2. TNFR1 is ubiquitously expressed in most tissues, while TNFR2 is primarily found in immune cells. Both receptors have distinct but overlapping roles in mediating the effects of TNF.

• TNFR1: This receptor is involved in the induction of apoptosis (programmed cell death) and inflammation. It contains a death domain that initiates signaling pathways leading to cell death.
• TNFR2: This receptor primarily promotes cell survival and proliferation. It activates pathways that lead to the expression of anti-apoptotic proteins and the proliferation of immune cells.

Upon binding to their respective ligands, TNFRs initiate a cascade of intracellular signaling events. These pathways include:

1. NF-κB Pathway: Activation of TNFRs leads to the activation of the NF-κB pathway, which is crucial for the expression of genes involved in inflammation, immune response, and cell survival.
2. MAPK Pathway: TNFRs also activate the Mitogen-Activated Protein Kinase (MAPK) pathway, which regulates cell proliferation, differentiation, and apoptosis.
3. Caspase Activation: In the case of TNFR1, the death domain recruits adaptor proteins that activate caspases, leading to apoptosis.

Human recombinant TNFRs are produced using recombinant DNA technology. These receptors are expressed in various host cells, such as bacteria, yeast, or mammalian cells, and are purified for use in research and therapeutic applications. Recombinant TNFRs are used to study the mechanisms of TNF signaling and to develop treatments for diseases involving excessive inflammation and immune responses.

Recombinant TNFRs have been developed as therapeutic agents for various inflammatory and autoimmune diseases. One of the most well-known examples is Etanercept, a fusion protein that combines the extracellular domain of TNFR2 with the Fc portion of IgG1. Etanercept acts as a decoy receptor, binding to TNF and preventing it from interacting with its natural receptors, thereby reducing inflammation.