Tumor necrosis factor (also known as TNF-α, TNF-a, Tumor necrosis factor ligand superfamily member 2 or Cachectin) is a transmembrane protein with a molecular weight of 26 kDa, found in the phagocytic cup, integral component of plasma membrane and recycling endosome of cells. In humans, TNF-α has been thought to be involved with important functions like cytokine activity. It is the subject of extensive research because of the fact that it acts in the lipopolysaccharide-mediated signaling pathway, intrinsic apoptotic signaling pathway in response to DNA damage and extrinsic apoptotic signaling pathway via death domain receptors. Sequencing of TNF-α has exemplified it contains 2 types of conserved structural units: extracellular and cytoplasmic domain. TNF-α is a suppressor of fat cell differentiation, myosin-light-chain-phosphatase activity and interleukin-6 production while also is a positive regulator of interleukin-8 production, ERK1 and ERK2 cascade and protein catabolic process. It is an integral part of organismal processes, in particular, microglial cell activation, JNK cascade and cortical actin cytoskeleton organization. TNF-α binds to protease, transcription regulatory region sequence-specific DNA and identical protein. It has been found to be involved in establishment of endothelial barrier, endothelial cell apoptotic process and transcription by RNA polymerase II. TNF-α is clinically significant because abnormalities in its function have been closely linked to diseases such as psoriatic arthritis.
We provide custom conjugation services for this antibody (e.g. labeling of TNF α antibody with HRP). A list of available labels can be found in the table below: