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Enteropeptidase or enterokinase is an enzyme involved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen (a zymogen) to trypsin, indirectly activating a number of pancreatic digestive enzymes. Enteropeptidase is a serine protease enzyme (EC 3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.

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.

Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture.

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.

NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.

Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.

TSTA3 is a NADP(H)-binding protein. TSTA3 catalyzes the two-step epimerase and the reductase reactions in GDP-D-mannose metabolism, converting GDP-4-keto-6-D-deoxymannose to GDP-L-fucose. GDP-L-fucose is the substrate of numerous fucosyltransferases that take part in the expression of several glycoconjugates, including blood group ABH antigens and developmental adhesion antigens.
Mutations in TSTA3 result in leukocyte adhesion deficiency, type II.

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.

Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.

GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

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.

PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

TEV protease is the common name for the 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein encoded by the tobacco etch virus (TEV). Because its sequence specificity is far more stringent than that of factor Xa, thrombin, or enterokinase, TEV protease is a very useful reagent for cleaving fusion proteins. TEV protease recognizes a linear epitope of the general form E-Xaa-Xaa-Y -Xaa-Q-(G/S), with cleavage occurring between Q and G or Q and S. The most commonly used sequence is ENLYFQG.

IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.

MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

ALDH1A1 is part of the aldehyde dehydrogenases family.
Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
(Retinal + NAD+ + H2O = retinoate + NADH).

KGF-2 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.

GLRX5 is small redox enzyme of approximately 100 amino acids which uses glutathione as a cofactor. GLRX5 is a mitochondrial protein, which is evolutionarily conserved. GLRX5 is oxidized by substrates, and reduced non-enzymatically by glutathione. GLRX5 is involved in the biogenesis of iron-sulfur clusters that are required for normal iron homeostasis. GLRX5 is necessary for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. Defects in the GLRX5 gene are a cause of anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA).

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.