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ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.

NEDD8 is part of the ubiquitin family. Human NEDD8 shares 60% amino acid sequence homology to ubiquitin. The NEDD8 system is essential for the regulation of protein degradation pathways involved in cell cycle progression, morphogenesis and tumorigenesis. NEDD8 is involved in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E-1 complex UbE1c- appbp1 and linkage to the E-2 enzyme UbE2m. Attachment of NEDD8 to cullins activates their associated E-3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

DTNBP1 is involved in organelle biogenesis connected with melanosomes, platelet dense granules, and lysosomes. An analogous protein in murine is a part of a protein complex called BLOC-1, and connects to alpha- and beta-dystrobrevins, which are factors of the dystrophin-associated protein complex (DPC). Mutations in DTNBP1 gene are associated with Hermansky-Pudlak syndrome type 7. DTNBP1 gene may also be associated with schizophrenia.

IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

NUDT5 is part of the nudix hydrolase family which remove toxic nucleotide derivatives from the cell. NUDT5 hydrolyzes ADP-ribose and ADP-mannose in the presence of magnesium, and in addition hydrolyzes nucleotide sugars with decreasing activity such as ADP-glucose and diadenosine diphosphate. As a nudix hydrolase, NUDT5 holds a central nudix motif and functions to eliminate toxic nucleotide metabolites from the cell while maintaining the levels of signaling nucleotides.
NUDT5 is broadly expressed but is most abundant in liver as a homodimer.

Programmed cell death 1 ligand 2 (PDCD1LG2) which takes part in the costimulatory signal, is necessary for T-cell proliferation. PDCD1LG2 is also involved in IFNG production in a PDCD1-independent way. The interaction with PDCD1 inhibits T-cell proliferation by preventing cytokine production and cell cycle progression.

CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

CDC34 is important in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, has been shown to target many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include I?B, B-Myb, Wee1, MyoD, ICERII?, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as ?-catenin, p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 has been demonstrated to self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. This protein is useful for in vitro ubiquitinylation reactions.

CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.

Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). The GldA protein allows microorganisms to use glycerol as a source of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.

CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

Ubiquitin-conjugating enzyme E2 F (UBE2F) is a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily. Ubiquitin-conjugating enzymes or sometimes as ubiquitin-carrier enzymes, run the second step in the ubiquitination reaction which targets a protein for degradation using the proteasome. The UBE2F receives the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins.
RBX2-UBE2F complex neddylates specific target proteins, for example CUL5 as can be seen from the specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1.

The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.

Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.

DNAJC15 which is expressed ubiquitously and located on the membrane contains 1 J domain. In many advanced cases of ovarian adenocarcinoma DNAJC15 is absent or down-regulated, due to hypermethylation and allelic loss. Loss of expression correlates with increased resistance to antineoplastic drugs, such as cisplatin. DNAJC15is a crucial component of the TIM23 translocase complex and stimulates the ATPase activity of HSPA9.

NAD (P) Dependent Steroid Dehydrogenase-Like (NSDHL) takes part in synthesis of cholesterol. NSDHL is involved in one of a few steps which convert lanosterol to cholesterol by removing a carbon atom and three hydrogen atoms (a methyl group). NSDHL is also a vital element of cell membranes and myelin, the fatty covering that insulates nerve cells.

BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.

CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.