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Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.

Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.

FKBP1A is a 12kDa protein initially discovered on an immune cells on the basis of its capability to bind as well as mediate the intracellular effect of the immunosuppressant FK506. FKBP1A is also known to mediate the action of Rapamycin-immunosuppressive agent. FKBP1A is part of the family of immunophilins, which have in common high affinity for immunosuppressant drugs and a peptidyl-prolyl cis-trans isomerase (PPIase). Activity which participates in folding of proline-containing protein. In the absence of immunosuppressive ligands, FKBP1A is involved in intracellular calcium regulation by associating with 3 types of Ca2+ release channel complexes: skeletal ryanodine receptors, cardiac ryanodine receptors and the inositol 1,4,5-triphosphate receptor. FKBP1A also interact with TGF-beta type I receptor exerting an inhibitory effect on the TGF-beta signaling pathway. FKBP12 plays a role in modulation of ryanodine receptor isoform-1 (ryr-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. FKBP1A increase the folding of proteins and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

Alanyl-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 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.

CBR4 is a member of the short-chain dehydrogenase/reductase family. CBR4 has a role in biosynthesis of fatty acids in the mitochondria and a broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and a range of other o-quinones and p-quinones (in vitro). CBR4 formation of a heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity for o- and p-quinones.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.

Conglutin, also known as Ara h 6.0101 is a part of the 2S albumin protein family. Conglutin along with Ara h 2.0201 are considered as some of the most potent elicitors of anaphylaxis. Both proteins hold multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure. Conglutin causes an allergic reaction in human and binds to IgE.

The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

HSD17B10 functions in mitochondrial tRNA maturation. HSD17B10 is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5''-ends. HSD17B10 interacts with intracellular amyloid-beta, and contributes to the neuronal dysfunction associated with Alzheimer disease.

IYD is an enzyme that catalyzes the oxidative NADPH-dependent deiodination of both mono- and diiodotyrosine although acts more efficiently on monoiodotyrosine. The N-terminus of Iodotyrosine Deiodinase , also known as IYD, plays a role as a membrane anchor. IYD acts during the hydrolysis of thyroglobulin to liberate iodide, which then reenter the hormone-producing pathways.

QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.

Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.