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Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

Recombinant Hirudin is a potent thrombin inhibitor originally derived from the medicinal leech. Hirudin acts directly on thrombin rather than through other clotting factors. The mechanism of Hirudin-thrombin appears to be unique. The conversion of fibrinogen into fibrin by the serine protease enzyme thrombin is a major event in the final stages of blood coagulation. In the final stages of coagulation prothrombinase converts prothrombin into thrombin. Fibrin is subsequently cross linked by factor XIII to form a blood clot. The primary inhibitor of thrombin in normal blood circulation is antithrombin III. The anticoagulatant activity of hirudin is derived from its ability to inhibit the pro-coagulant activity of thrombin (similar to antithrombin III activity). Hirudin is the strongest natural inhibitor of thrombin. Hirudin binds to and inhibits only the activity of thrombin forms with a specific activity on fibrinogen contrasting to antithrombin III activity. Therefore, hirudin has a thrombolytic activity since it prevents or dissolves the formation of clots and thrombi. Hirudin also has therapeutic significance in blood coagulation disorders, in the treatment of skin hematomas and of superficial varicose veins. Hirudin does not hinder with the biological activity of other serum proteins and can also act on complexed thrombin, thus having an advantage over more common anticoagulants and thrombolytics. It is complicated to extract large quantities of hirudin from natural sources; therefore a method for producing and purifying hirudin using recombinant biotechnology has been developed.

BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

Human Cu/Zn Superoxide Dismutase (SOD) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. SOD protects the cell against dangerous levels of superoxide. SOD binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled.

Protein Tyrosine Phosphatase Non Receptor Type-11 or PTPN11 has 2 Src homology 2 domains and part of the tyrosine phosphatase group of proteins. PTPN11 is responsible for the catalyzation of tyrosine residues dephosphorylation in proteins and takes part in the stimulation and activation of Erk/MAP kinase transduction via signals from tyrosine kinase. Noonan syndrome and acute myeloid leukemia can be caused from mutations in PTPN11.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

Thiosulfate Sulfurtransferase Like Domain Containing 3, also known as TSTD3 contains 1 rhodanese domain which is characterized by an active site cysteine residue that has the ability to bind sulfane sulfur and catalyse sulfur transfer.

Threonyl-tRNA synthetase, cytoplasmic (TARS) is a member of the class-II aminoacyl-tRNA synthetase family. The main role of TARS is in tRNA aminoacylation. The N-terminal domain of the TARS enzyme is responsible for the competition with the ribosome whereas the catalytic and the C-terminal domain are involved in binding the 2 anticodon arm-like structures in the operator.

Tyrosyl-DNA phosphodiesterase 1 ( TDP1) is required for repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 also detach glycolate from single-stranded DNA having 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks.

TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

Threonyl-tRNA Synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 83 kDa protein is an autoantigen recognized by PL-7 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that PL-7 antibodies (similar to Jo-1 antibodies) indicate an increased risk for lung involvement, but this needs to be confirmed for a larger number of cases.

Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.

Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.

Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.