描述：
Tumor necrosis factor alpha (TNF-α, 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. TNF-α is produced by a wide
variety of immune and epithelial cell types. Bovine TNFα consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 178 aa extracellular domain
(ECD). Within the ECD, bovine TNF-α shares 64% 83% sequence identity with canine, cotton
rat, equine, feline, human, mouse, porcine, rat, and rhesus TNF-α. 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 TNF-α by TACE
/ADAM17 releases a 55 kDa soluble trimeric form of TNF-α. TNF-α trimers bind the ubiquitous
TNF RI and the hematopoietic cellrestricted TNF RII, both of which are also expressed as
homotrimers. TNF-α regulates lymphoid tissue development through control of apoptosis.
It also promotes inflammatory responses by inducing the activation of vascular endothelial
cells and macrophages. TNF-α is a key cytokine in several inflammatory disorders. It contributes
to the development of type 2 diabetes through its effects on insulin resistance and fatty acid
metabolism.
原厂资料：
Tumor necrosis factor alpha (TNF-α, 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. TNF-α is produced by a wide
variety of immune and epithelial cell types. Bovine TNFα consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 178 aa extracellular domain
(ECD). Within the ECD, bovine TNF-α shares 64% 83% sequence identity with canine, cotton
rat, equine, feline, human, mouse, porcine, rat, and rhesus TNF-α. 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 TNF-α by TACE
/ADAM17 releases a 55 kDa soluble trimeric form of TNF-α. TNF-α trimers bind the ubiquitous
TNF RI and the hematopoietic cellrestricted TNF RII, both of which are also expressed as
homotrimers. TNF-α regulates lymphoid tissue development through control of apoptosis.
It also promotes inflammatory responses by inducing the activation of vascular endothelial
cells and macrophages. TNF-α is a key cytokine in several inflammatory disorders. It contributes
to the development of type 2 diabetes through its effects on insulin resistance and fatty acid
metabolism.
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