Anti-TNF-alpha (Ms) aus Kaninchen (Klon: pAk) – unkonj.

Tumor necrosis factor alpha (TNFa), also known as cachectin and TNFSF1A, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, apoptosis, and immune system development. TNFa is produced by a wide variety of immune and epithelial cell types. Mouse TNFa consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, mouse TNFa shares 94% aa sequence identity with rat and 70%-77% with bovine, canine, cotton rat, equine, feline, human, porcine, rat, and rhesus TNFa. The 26 kDa type 2 transmembrane protein is assembled intracellularly to form a noncovalently linked homotrimer. Ligation of this complex induces reverse signaling that promotes lymphocyte costimulation but diminishes monocyte responsiveness. Cleavage of membrane bound TNFa by TACE/ADAM17 releases a 55 kDa soluble trimeric form of TNFa. TNFa trimers bind the ubiquitous TNF RI and the hematopoietic cell restricted TNF RII, both of which are also expressed as homotrimers. TNFa regulates lymphoid tissue development through control of apoptosis. It also promotes inflammatory responses by inducing the activation of vascular endothelial cells and macrophages. TNFa is a key cytokine in the development of several inflammatory disorders. It contributes to the development of type 2 diabetes through its effects on insulin resistance and fatty acid metabolism.