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Carboxymethylenebutenolidase homolog (CMBL) is a cysteine hydrolase of the dienelactone hydrolase family which is highly expressed in the liver cytosol. CMBL is the human homolog of Pseudomonas dienelactone hydrolase, which is a protein that participates in the bacterial halocatechol degradation pathway. CMBL which preferentially cleaves cyclic esters activates medoxomil-ester prodrugs in which the medoxomil moiety is coupled with an oxygen atom. CMBL is inhibited by PCMB (p-chloromercuribenzoate) and is encoded by a gene which maps to human chromosome 5p15.2. CMBL can also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. CMBL is widely expressed, with the highest levels in the liver, followed by the kidney, small intestine and the colon.

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.

Coproporphyrinogen Oxidase (CPOX) which is localized to the internal membrane space of erythrocytes takes part in the 6th phase of heme biosynthesis. CPOX catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III. Mutations in human CPOX gene forecast the clinical result of the disease, with either hepatic hereditary coproporphyria or hematological manifestations of erythropoietic harderoporphyria.

ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

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.

Ecto-ADP-Ribosyltransferase 4 or ART4 is typed as a glycosylphosphatidylinositol (GPI)-linked membrane protein which carries Dombrock blood group antigens. The development of this protein takes place at the highest levels in the fetal liver. the process of the ART4 development is regulated while the erythroid differentiation process occurs. ART4 is a is part of the Ribosyltransferase family.

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.

Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.

Enteropeptidase or enterokinase is an enzymeinvolved 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 pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

Ornithine aminotransferase is a key enzyme in the pathway that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine aminotransferase (OAT) is a 49kDa nucleus-encoded protein imported into mitochondria to give the mature 48kDa OAT polypeptide. It is found in humans, animals, insects, plants and microorganisms. The OAT has a sex-differential expression in the mouse kidney. OAT plays central physiological roles in amino acid metabolism. OAT shows a large structural and mechanistic similarity to other enzymes from the subgroup III of aminotransferases that transfer an amino group from a carbon atom which doesn’t carry a carboxyl function. OAT is vital for nitrogen recycling from arginine but not for the stress-induced proline accumulation. OAT enzyme deficiency causes the autosomal recessive eye disease Gyrate Atrophy.

Enteropeptidase or enterokinase is an enzymeinvolved 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 pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

TAF10 is a small subunit of TFIID which is related to a subdivision of TFIID complexes. Studies with human and mammalian cells verified that this subunit is mandatory for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and is essential for several cellular differentiation programs.

GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.

Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.

Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.

BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.

P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.

Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.

BPNT1 belongs to the magnesium-dependent, lithium-sensitive phosphomono-esterase superfamily. BPNT1 catalyzes the conversion of PAPS (adenosine 3'-phosphate 5' phosphosulfate) to APS (adenosine 5'-phosphosulfate) and the conversion of PAP (3'(2')-phosphoadenosine 5' phosphate) to AMP (adenosine 5'-phosphate) using magnesium as a cofactor. BPNT1 is expressed everywhere but at maximum levels in brain and kidney. BPNT1 is potently inhibited by lithium, a drug used for the treatment of manic depression and bipolar affective disorder, which suggests that BPNT1 has a possible role in the etiology of mood disorders.