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. Equine TNF-α consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 178 aa extracellular domain
(ECD). Within the ECD, equine TNF-α shares 69% -88% aa sequence identity with bovine,
canine, cotton rat, 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 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.
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. Equine TNF-α consisits of a 35 amino acid (aa)
cytoplasmic domain, a 21 aa transmembrane segment, and a 178 aa extracellular domain
(ECD). Within the ECD, equine TNF-α shares 69% -88% aa sequence identity with bovine,
canine, cotton rat, 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 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.
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