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ADP-ribosylhydrolase like 2 (ADPRHL2) belongs to the ADP-ribosylglycohydrolase family. ADPRHL2 catalyzes the removal of ADP-ribose from ADP-ribosylated proteins. ADPRHL2, which is ubiquitously expressed, uses magnesium as a cofactor to catalyze the hydrolysis of poly (ADP-ribose) that is synthesized after DNA damage. Furthermore, ADPRHL2 has an essential role in the maintenance of normal neuronal cell function. The ADPRHL2 enzyme localizes to the mitochondria, in addition to the nucleus and cytoplasm.

Aldolase A (ALDOA) is a glycolytic enzyme, which catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ALDOA is found in the developing embryo and is produced in even greater amounts in adult muscle. ALDOA expression is repressed in the adult liver, kidney and intestine and similar to ALDOC levels in the brain and other nervous tissue. ALDOA deficiency has been linked with myopathy and hemolytic anemia.

NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.

TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMPfamily members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP.

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.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.

Norrie Disease (NDP) is a secreted regulatory protein which activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. NDP takes part in retinal vascularization by acting as a ligand for FZD4 which signals through stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. NDP is involved in a pathway that regulates neural cell differentiation and proliferation and also in neuroectodermal cell-cell interaction.

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 (CEACAM1) belongs to the carcinoembryonic antigen (CEA) gene family which is a part of the immunoglobulin superfamily. CEACAM1 is a cell adhesion protein which mediates homophilic cell adhesion in a calcium-independent way. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. CEACAM1 functions as coinhibitory receptor in immune response, and plays a role also as an activator during angiogenesis.

DNA Cytosine-5--Methyltransferase 3-Like (DNMT3L) is a nuclear protein with similarity to DNA methyltransferases, but is not believed to act as a DNA methyltransferase since it doesn’t contain the amino acid residues needed for methyltransferase activity. Nevertheless, DNMT3L stimulates de novo methylation by DNA cytosine methyltransferase 3 alpha and is assumed to be required for the formation of maternal genomic imprints. DNMT3L also mediates transcriptional repression as a result of interaction with histone deacetylase 1. DNMT3L is a catalytically inactive regulatory factor of DNA methyltransferases, which is vital for the function of DNMT3A and DNMT3B. DNMT3L activates DNMT3A and DNMT3B by binding to their catalytic domain. Furthermore, DNMT3L accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases.

AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.

Glucosidase Beta Acid 3, also known as GBA3, hydrolyzes various types of glycosides. GBA3 takes part in a nonlysosomal catabolic pathway of glycosylceramide. GBA3 is a protein coding gene which acts as beta-glycosylceramidase.

Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.

Heparan Sulfate 3-O-Sulfotransferase 1 (HS3ST1), is sulfotransferase which uses 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. HS3ST1 catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a vital part in the biosynthesis of anticoagulant heparan sulfate since it concludes the structure of the antithrombin pentasaccharide binding site.