Thymopentin is a member of the LEM family. Thymopentin is expressed in many tissues, highly in the adult thymus and fetal liver. The N-terminal contains two structurally independent domains, LEM domain and LEM-like domain. The C-terminal domain forms a four-stranded coiled coil. Thymopentin may be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. It is associated with T-cell development and function. Meantime, Thymopentin plays an important role, together with LMNA, in the nuclear anchorage of RB1. Thymopoietin is participated in the induction of CD90 in the thymus.
Transmembrane Protease Serine 11B (TMPRSS11B) is a single-pass type II membrane protein member of the peptidase S1 family. TMPRSS11B contains one peptidase S1 domain and one SEA domain. TMPRSS11B is a serine protease that may play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions.
STC2 is a secreted, homodimeric glycoprotein which expressed in a wide variety of tissues. STC2 has an anti-hypocalcemic action on calcium and phosphate homeostasis. It may have autocrine or paracrine functions. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. STC2 has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. It may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis.
TMX2 is a single-pass type I membrane protein and contains 1 thioredoxin domain. Thioredoxin plays an important role in various cellular processes through redox regulation. The molecular cloning and characterization of one member of the thioredoxin superfamily, designated as TMX2.The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail.
TNFα is a homotrimer with a subunit molecular mass of 17 kD cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It plays a major role in growth regulation; differentiation; inflammation; viral replication; tumorigenesis; autoimmune diseases and in viral; bacterial; fungal; and parasitic infections. Besides inducing hemorrhagic necrosis of tumors; TNF was found to be involved in tumorigenesis; tumor metastasis; viral replication; septic shock; fever; inflammation; and autoimmune diseases including Crohn’s disease; and rheumatoid arthritis as well as graft-versus-host disease.
Tumor Necrosis Factor-α (TNF-α) is secreted by macrophages; monocytes; neutrophils; T-cells; and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-α while cells that express CD8 secrete little or no TNF-α. Synthesis of TNF-α can be induced by many different stimuli including interferons; IL2; and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-α has been limited by the proinflammatory side effects such as fever; dose-limiting hypotension; hepatotoxicity; intravascular thrombosis; and hemorrhage. Designing clinically applicable TNF-α mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-α that binds to murine TNF-R55 but not murine TNF-R7; exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-α; which binds to both murine TNF receptors. Based on these results; many TNF-α mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF-α High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8; Lys9; Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo.
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