TNFSF12-TNFSF13: A Potential Drug Target for Cell Death and Inflammation

Target Name: TNFSF12-TNFSF13

NCBI ID: G407977

TNFSF12-TNFSF13: A Potential Drug Target for Cell Death and Inflammation

TNFSF12-TNFSF13, also known as tumor necrosis factor (ligand) superfamily member 12-member 13, is a protein that plays a crucial role in various cellular processes in the body. It is a member of the TNFSF family, which is known for its ability to induce cell death, repair, and inflammation. The TNFSF12-TNFSF13 protein is expressed in various tissues and cells throughout the body, including the immune system, and has been implicated in a number of diseases, including cancer. As a result, it is a potential drug target or biomarker for a variety of therapeutic approaches.

The TNFSF12-TNFSF13 protein is composed of 118 amino acid residues and has a calculated molecular mass of 13.9 kDa. It is characterized by a long extracellular domain that includes a region of 11 amino acids known as the N-terminal hypervariable region (HVR1), as well as a variable region that includes several conserved amino acids known as HVR2-HVR7. The variable region includes a unique feature known as a variable region in the middle of the protein, which is composed of four conserved amino acids that are involved in the formation of a distinct alpha-helices.

The TNFSF12-TNFSF13 protein is involved in a variety of cellular processes, including inflammation, cell adhesion, and signaling. One of its most well-known functions is its role in the regulation of cell death. When cells are exposed to TNFSF12-TNFSF13, the protein can induce cell death through a variety of mechanisms, including the production of reactive oxygen species (ROS) and the formation of autophagy. This is thought to be an important mechanism by which TNFSF12-TNFSF13 contributes to tumor development and progression.

In addition to its role in cell death, TNFSF12-TNFSF13 is also involved in the regulation of cell adhesion. The protein is known to play a role in the formation of tight junctions, which are a type of cell-cell adhesion that helps to maintain tissue structure and prevent the excessive migration of cells. TNFSF12-TNFSF13 is also involved in the regulation of cell-cell adhesion through its ability to interact with the protein known as cadherin, which is a major adhesion molecule.

Another function of TNFSF12-TNFSF13 is its role in cell signaling. The protein is involved in a variety of signaling pathways, including the TGF-β pathway and the NF-kappa-B pathway. These pathways are involved in the regulation of cellular processes such as cell growth, differentiation, and inflammation. TNFSF12-TNFSF13 is thought to play a role in the regulation of these processes by its ability to interact with the protein known as transforming growth factor (TGF-β1).

TNFSF12-TNFSF13 is also involved in the regulation of inflammation. The protein is known to play a role in the regulation of immune responses, including the regulation of T cell proliferation and the production of antibodies. In addition, TNFSF12-TNFSF13 is thought to contribute to the regulation of inflammation through its ability to interact with the protein known as nuclear factor kappa B (NFKB).

Due to its involvement in a variety of cellular processes, TNFSF12-TNFSF13 is a potential drug target or biomarker for a variety of therapeutic approaches. For example, because the protein is involved in the regulation of cell death, it may be a good candidate for drugs that are designed to

Protein Name: TNFSF12-TNFSF13 Readthrough

Functions: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion

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