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Thymine-DNA glycosylase (TDG) is a member of the TDG/mug DNA glycosylase family.
TDG is a nuclear protein that fixes G/T mismatches to G/C pairs by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired thymin. In addition, TDG removes uracil and 5-bromouracil from mispairings with guanine. The TDG enzyme has an essential role in cellular defense against genetic mutation triggered by the spontaneous deamination of 5-methylcytosine and cytosine.

Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.

KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.

Phosphoserine aminotransferase (PSAT1) catalyzes the conversion of 3-phosphohydroxypyruvate into 3-phosphoserine which is dephosphorylated consequently by phosphoserine phosphatase to form L-serine. PSAT1 is probably a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila. PSAT1 is expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon. Defects in the PSAT1 gene are the cause of phosphoserine aminotransferase deficiency (PSATD). PSATD is distinguished biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.

Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).

Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.

Killer Cell Lectin-Like Receptor Subfamily C, Member 1 (KLRC1) is a part of the killer cell lectin-like receptor family. KLRC1 functions as a receptor for the detection of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRC1 is also connects with CD94 and is expressed on NK cells and some activated T cell.

Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.

The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.

DUSP10 is a member of the protein-tyrosine phosphatase family. DUSPs inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residuesb and negatively regulate members of the MAPK superfamily which is linked with cellular proliferation and differentiation. DUSP10 interacts with MAPK14 and MAPK8. DUSP10 blocks in mammalian cells the enzymatic activation of MAP kinases with the selectivity p38 approximately JNK/SAPK >> ERK.

N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.

ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.

PRDX5 belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides with reducing equivalents supplied through the thioredoxin system. PRDX5 has an antioxidant protective function in different tissues under normal conditions and during inflammatory processes. Peroxiredoxin-5 interacts with peroxisome receptor 1 and is involved in intracellular redox signaling. PRDX5 is involved in intracellular redox signaling. Peroxiredoxin-5 is a significant antioxidant protein of lung epithelial cells for its expression in the human lung increases during inflammation. PRDX5 expression is upregulated in osteoarthritis. PRDX5 may be significant in mitochondrial genome stability. Peroxiredoxin-5 has a protective role in human tendon cells against oxidative stress by reducing apoptosis and upholding collagen synthesis.

Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.

GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

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.

FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.