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GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.

GPD1 enzyme catalyzes the reduction of dihydroxyacetone phosphate to sn-glycerol 3-phosphate. (sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH) previous names for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase and glycerolphosphate dehydrogenase. However, GPD1 differs from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

CTSC has an important role in the activation of granule serine proteases in inflammatory cells.CTSC catalyses excision of dipeptides from the N-terminus of protein and peptide substrates. Once activated by CTSC, proteases are capable of degrading extracellular matrix components, which can result in tissue damage and chronic inflammation. CTSCcomprises of 4 subunits, each composed of the N-terminal proregion fragment, heavy chain and light chains. Defects in the CTSC protein have been demonstratedto result in Papillon-Lefevre disease which is an autosomal recessive disorder.

AICDA is an RNA-editing deaminase which belongs to the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. Defects in the AICDA gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2).

PAPPA is a large zinc binding protein, which acts as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A can also act as a regulator of IGF bioactivity in a number of biological systems, including the human ovary and cardiovascular systems. It was shown that PAPP A levels are elevated in patients with unstable angina or acute myocardial infarction. Furthermore, PAPPA is believed to be involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.
Lower levels of PAPPA are found in an array of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow, colon, fibroblasts and osteoblasts. PAPP-A is present in serum and placenta during pregnancy; with levels increasing throughout pregnancy. Low levels of PAPP A are associated with a number of foetal chromosomal abnormalities, as well as pre-eclampsia and stillbirth.
PAPPA levels may be a potentially highly specific marker for heart disease.
PAPP-A proteolytic activity is inhibited by targeting substrate exosite binding.

GSTO1 belongs to the theta class glutathione S-transferase-like (GSTTL) protein family. GSTO1 is expressed in a broad array of human tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities as well as catalyzing the reduction of monomethylarsonate which is an intermediate in the pathway of arsenic biotransformation. Furthermore, GSTO1 shields from oxidative stress which is a risk factor for Alzheimer disease, vascular dementia and stroke. GSTO1 is abundant in alveolar macrophages and airway secretions, with the levels reduced in chronic obstructive pulmonary disease patients. In mouse, the GSTO1 protein acts as a small stress response protein, probably involved in cellular redox homeostasis.

6PGD is the second dehydrogenase in the pentose phosphate shunt. Pentose is neccesary for nucleic acid biosynthesis. The pentose phosphate cycle is a major source of NADPH 6PGD deficiency is usually asymptomatic, and the inheritance of this disorder is autosomal dominant. PGD deficiency raises the erythrocyte pyruvate kinase levels of activity and decreases glutathione synthetase, resulting in hemolysis.

ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.

Platelet-activating Factor Acetylhydrolase 1b Catalytic Subunit 3 (PAFAH1B3) is a member of the 'GDSL' lipolytic enzyme family. Acetylhydrolase catalyzes the elimination of an acetyl group from the glycerol backbone of platelet-activating factor. PAFAH1B3, which is a subunit of the platelet-activating factor cetylhydrolase isoform 1B complex, is comprised of the catalytic beta and gamma subunits and the regulatory alpha subunit. The PAFAH1B3 complex has an imperative role during the development of brain.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

FKBP2 is part of the immunophilin protein family, which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.

TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

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.

UPRT is a uracil phosphoribosyltransferase, that catalyzes the alteration of uracil and 5-phosphoribosyl-1-R-diphosphate to uridine monophosphate (UMP). This reaction is a significant part of nucleotide metabolism, specifically the pyrimidine salvage pathway. UPRT is restricted to the nucleus and cytoplasm and is a possible target for rational design of drugs to cure cancer and parasitic infections.

ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

Aldo-keto reductase family 1 member C4 or AKR1C4 is a part of the aldo/keto reductase superfamily that has more then 40 known proteins & enzymes. AKR1C4 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols with NADH and/or NADPH as cofactors. AKR1C4 takes place in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in the liver tissue.

Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

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.