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tRNA-splicing endonuclease subunit Sen15 (TSEN15) is a member of the SEN15 family. tRNA splicing is an essential process required for cell growth and division. TSEN15 is a subunit of the tRNA splicing endonuclease. TSEN15 cleaves pre-tRNA at the 5' and 3' splice sites to release the intron.

Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

TXNL4B is a member of the DIM1 family which has a vital role in pro-mRNA splicing. TXNL4B is required in cell cycle progression for S/G2 transition and interacts with PRPF6 subunit of the spliceosome.

HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

HAAO is a monomeric cytosolic protein which is a member of intramolecular dioxygenases family containing nonheme ferrous iron. The HAAO protein catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is facilitated by its ability to activate glutamate N-methyl-D-aspartate receptors. Amplified cerebral levels of QUIN may contribute to the pathogenesis of neurologic and inflammatory disorders. HAAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low amounts in the central nervous system.

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.

Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

60S ribosomal protein L8 (RPL8) is a member of the ribosomal protein L2P family. Ribosomes consist of a small 40S subunit and a large 60S subunit. RPL8 is found in the cytoplasm and exists as a component of the 60S subunit where it is assumed to have role in aminoacyl-tRNA binding, specifically at the ribosomal subunit interface. In rats, the RPL8 protein connects with the 5.8S rRNA, and possibly participates in the binding of aminoacyl-tRNA, and is a component of the elongation factor 2-binding site at the ribosomal subunit interface.

The ribosomal phosphoproteins, also called P protein antigens, are associated with the large ribosomal subunit and therefore are antigenic targets with a cytoplasmic localization. Three P proteins have been described: P0 with a molecular weight of 35 kDa, P1 (19 kDa) and P2 (17 kDa). RPLP0 is a ribosomal protein that is a component of the 60S subunit. RPLP0 belongs to the L10P family of ribosomal proteins. RPLP0 is a neutral phosphoprotein having a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 & P2. The P0 protein interacts with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of RPLP0 scattered throughout the genome.
Autoantibodies against ribosomal P proteins are present in 10 % of SLE patients. If anti-ribosomal P antibodies were to occur in the absence of other typical SLE associated autoantibodies, they may account for some patients with so-called ANA-negative lupus. It has been reported that lupus patients positive for anti-ribosomal P autoantibodies have a high frequency of CNS involvement, suggesting a marker use for these antibodies.

Heparanase is an endo ß-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).

Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

S100P is a Ca2+ binding protein that is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are found in the cytoplasm and/or nucleus of a large range of cells, and participates in the regulation of a number of cellular function such as cell cycle progression and differentiation. S100P participates in numerous biological functions but the exact functions or mechanism of its action is still mostly unknown. Once S100P binds calcium ions it goes through a conformational change that results in an exposure of a hydrophobic surface which permits the interaction with specific target proteins.

HES7 belongs to the Hairy and enhancer of split family of bHLH transcription factors. The mouse ortholog of the HES7 is set by Notch signaling. The protein serves as a transcriptional repressor, and is involved in correct patterning of the axial skeleton. A mutation in HES7 has been shown to result in spondylocostal dysostosis. Multiple transcript variants encoding different isoforms have been discovered for HES7.

Modulator of apoptosis 1 (MOAP1), is a member of the PNMA family and contains one BH3-like domain and one RASSF1-binding domain. MOAP1 was recognized by its interaction with apoptosis regulator BAX protein. MOAP1 includes a Bcl-2 homology 3 (BH3)-like motif, which is essential for the association with BAX. In addition, once over expressed MOAP1 mediates caspase-dependent apoptosis.

HMGB1 is an abundant chromatin-binding protein found in eukaryotic cell nucleus and acts in the assembly of nucleoprotein complexes. Inside the cell, HMGB1 binds to DNA and is involved in transcriptional regulation. Outside the cell, HMGB1 acts as a cytokine with activities that resemble those of tumor necrosis factor (TNF). HMGB1 is elevated significantly in chronic kidney disease patients and correlates with glomerular filtration rate as well as with markers of inflammation and malnutrition. HMGB1 is involved in Gram-negative sepsis by catalyzing movement of LPS monomers from LPS aggregates to CD14 to initiate a TLR4-mediated proinflammatory response. HMGB1 plays an important role in the relationship between necrosis and malignancy in glioma tumours. HMG1 protein is induced by Mycobacterium bovis BCG. Overexpression of HMGB1 is common in gastrointestinal stromal tumors and is related to the KIT mutation. HMG1 induces growth inhibition and apoptosis in macrophages through RAGE intracellular signaling pathway. The increase of extracellular HMGB1 observed in salivary glands of Sjogren's syndrome patients indicates that HMGB-1 is involved in the inflammatory process of the disease. HMGB-1 together with estrogen increase cell cycle progression in tumor cell lines.

Homeobox A9 (HOXA9) is a member of the Abd-B homeobox family. The HOXA9 protein is a transcription factor with a key role in both haemopoiesis and leukaemia. High levels of HOXA9 expression in haemopoietic cells is a distinctive feature of acute myeloid leukaemia (AML), and may be sufficient to cause this disease. HOXA9 overexpression noticeably expands hematopoietic stem cells. The HOXA9 gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which regulates gene expression, morphogenesis, and differentiation. HOXA9 is a sequence-specific transcription factor which is part of a developmental regulatory system, which provides cells with specific positional identities on the anterior-posterior axis. HOXA9 is essential for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.

DHPS is vital for the first step of hypusine biosynthesis. DHPS catalyzes the NAD-dependent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the EIF5A precursor protein to form the intermediate deoxyhypusine residue.

Adipocyte plasma membrane-associated protein, also known as APMAP, is a member of the strictosidine synthase family. APMAP exhibits strong arylesterase activity with beta-naphthyl acetate in addition to phenyl acetate and takes part in adipocyte differentiation.

NCBP2 is a part of the nuclear cap-binding protein complex (CBC) that binds to the monomethylated 5'' cap of nascent pre-mRNA in the nucleoplasm. NCBP2 protein has an RNP domain usually located in RNA binding proteins, and contains the cap-binding activity. CBC promotes pre-mRNA splicing, 3''-end processing, RNA nuclear export, and nonsense-mediated mRNA decay.

HSPA6 is a distinctive member of the human Hsp70 chaperone that takes part in cellular processes such as protein trafficking, folding, and prevention of aggregation. HSPA6 is strictly stress-inducible, having little or no basal expression levels in most cells. HSPA6 and HSP72 are are involved in cell survival of proteotoxic stress.

DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.
DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques.