You searched for: Enzymes

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Cystathionine Gamma-Lyase (CTH) belongs to the trans-sulfuration enzymes family. CTH exists as a homotetramer and interacts with CALM in a calcium-dependent manner. CTH breaks down cystathionine into cysteine, ammonia and 2-oxobutanoate. CTH catalyses the last step in the trans-sulfuration pathway from methionine to cysteine and has broad substrate specificity. Defects in CTH will lead to cystathioninuria, which is an autosomal recessive phenotype characterised by abnormal accumulation of plasma cystathionine.

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Aldo-Keto Reductase 1C4/AKR1C4 is a member of the aldo/keto reductase family that consists of more than 40 known enzymes and proteins. AKR1C4 has highly expressed in Liver. It can catalyses the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver. AKR1C4 catalyses the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5- alpha-Androstan-3- alpha,17- beta -diol (3- alpha-diol). In addition, AKR1C4 also has some 20- alpha-Hydroxysteroid Dehydrogenase activity.

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Protein disulfide-isomerase A5 is a 519 amino acids protein that belongs to the protein disulfide isomerase family.It contains 3 thioredoxin domains.It can catalyse the rearrangement of -S-S- bonds in proteins.

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Kidney-Type Arginase (ARG2) is a member of the arginase family. Arginase is a manganese-containing enzyme which catalyses the hydrolysis of arginine to ornithine and urea. ARG2 is highly expressed in kidney and prostate, not founded in the liver, heart and pancreas. ARG2 has been implicated in the regulation of the arginine/ornithine concentrations in the cell. ARG2 may take part in the regulation of extra-urea cycle arginine metabolism and in down-regulation of nitric oxide synthesis. The extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase.

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Malate Dehydrogenase, Cytoplasmic (MDH1) is an enzyme which belongs to the MDH Type 2 sub-family of LDH/MDH superfamily. MDH1 is involved in the Citric Acid Cycle that catalyses the conversion of Malate into Oxaloacetate (using NAD+) and vice versa. MDH1 should not be confused with Malic Enzyme, which catalyses the conversion of Malate to Pyruvate, producing NADPH. MDH1 also participates in Gluconeogenesis, the synthesis of Glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by Pyruvate Carboxylase to form Pxaloacetate, a Citric Acid Cycle intermediate. In order to transport the Oxaloacetate out of the Mitochondria, Malate Dehydrogenase reduces it to Malate, and it then traverses the inner Mitochondrial membrane. Once in the cytosol, the Malate is oxidised back to Oxaloacetate by MDH1. Finally, Phosphoenol-Pyruvate Carboxy Kinase (PEPCK) converts Oxaloacetate to Phosphoenol Pyruvate.

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Triose-phosphate isomerase, also named Triose-phosphate isomerase, TPI and TIM, is an enzyme that catalyses the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI deficiency is an autosomal recessive disorder and the most severe clinical disorder of glycolysis. Triose phosphate isomerase deficiency is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection and characterised by chronic hemolytic anemia.

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Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyse the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.

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D-Amino-Acid Oxidase (DAO) belongs to the DAMOX/DASOX family. DAO is a peroxisomal enzyme which founctions as a homodimer to oxidises D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. D-amino-acid oxidase regulates the level of the neuromodulator D-serine in the brain, has a high activity towards D-DOPA and contributes to dopamine synthesis. D-amino-acid oxidase could act as a detoxifying agent which removes D-amino acids accumulated during aging. It also acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups.

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Cysteine Dioxygenase Type 1 (CDO1) is a mammalian non-heme iron enzyme that belongs to the cysteine dioxygenase family. CDO1 is highly expressed in the liver and placenta, and has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells. CDO1 catalyses the conversion of L-cysteine to cysteine sulfinic acid by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels.

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Human Biliverdin reductase A (BLVRA) is belonged to the Gfo/Idh/MocA family and Biliverdin reductase subfamily. BLVRA is an enzyme that in humans is encoded by the BLVRA gene. BLVRA plays an important role in reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. BLVRA acts on biliverdin by reducing its double-bond between the pyrrole rings into a single-bond. It accomplishes this using NADPH + H+ as an electron donor, forming bilirubin and NADP+ as products.

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L-Xylulose Reductase is an enzyme that belongs to the Short-Chain Dehydrogenases/Reductases (SDR) family. L-Xylulose Reductase is responsible for the metabolism of Xylulose, converting it into Xylitol. L-Xylulose Reductase catalyses the NADPH-dependent reduction of several Pentoses, Tetroses, Trioses, alpha-Dicarbonyl compounds and L-Xylulose. L-Xylulose Reductase participates in the Uronate Cycle of Glucose metabolism. It may play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing Xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.

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Butyrylcholine Esterase (BCHE) is a secreted protein that belongs to the type-B carboxylesterase/lipase family. BCHE is a major acetylcholine hydrolyzing enzyme in the circulation. It is detected in blood plasma and present in most cells except erythrocytes. BCHE is an esterase with broad substrate specificity. BCHE can contribute to the inactivation of the neurotransmitter acetylcholine. BCHE can degrade a large number of neurotoxic organophosphate esters. Thus, it plays important pharmacological and toxicological roles and is thought to be involved in the pathological progression. Defects in BCHE are the cause of butyrylcholinesterase deficiency (BChE deficiency) which is a metabolic disorder characterised by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine and other ester local anesthetics.

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Kynurenine aminotransferases (KATs) are pyridoxal-5’-phosphate-dependent enzymes that catalyse the conversion of L-kynurenine into kynurenic acid, a neuroactive metabolite whose unbalancing is associated with a number of brain disorders. Biochemical and structural investigations revealed that L-kynurenine (L-KYN) recognition by hKAT II is achieved by exploiting structural features that are peculiar of this isoform, thus offering the possibility to select/design inhibitor molecules specifically targeting hKAT II to be used as modulators of kynurenic acid synthesis in the CNS. hKAT II is one of the aminotransferases involved in the pyridoxal 5'-phosphate (PLP)-dependent irreversible transamination of L-kynurenine (L-KYN) to kynurenic acid (KYNA) in the central nervous system. When assayed in vitro the protein also displays beta-elimination activity.

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Tryptophan synthase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an alpha- beta beta - alpha complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H₂O.The beta subunits catalyse the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.

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Tryptophan synthase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an alpha- beta beta - alpha complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H₂O.The beta subunits catalyse the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.

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MDP1, which is short for nesium-dependent phosphatase 1, is a 176 aa. protein. It has 3 forms by different alternative splicing. This protein belongs to the HAD-like hydrolase superfamily, and usually takes its function with Magnesium. It can be inhibited by vanadate and zinc, and slightly by calcium. MDP1 is a Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.

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PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesised glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

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Carbonic Anhydrase 13 (CA13) belongs to the carbonic anhydrase family which can catalyses the reversible hydration recation of carbon dioxide. Carbonic anhydrases participate in many biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA13 is a cytosolic enzyme and is widely expressed in human, such as thymus, small intestine, spleen, prostate, ovary, colon and testis, indicating that it may play a key role in several organs. CA13 is inhibited by acetazolamide.

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Thymidine kinase 1(TK1) belongs to the thymidine kinase family. It is located in the cytoplasm, and phosphorylated on Ser-13 in mitosis during post-translational modification. Two forms of this protein have been identified in animal cells, one in cytosol TK1 and one in mitochondria TK2. Thymidine kinases have a key function in the synthesis of DNA and thereby in cell division, as they are part of the unique reaction chain to introduce deoxythymidine into the DNA. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle, while it is very low in resting cells. TK1 acts as a homotetramer, and can transform thymidime to thymidine 5'-phosphate with the help of ATP.

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Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.

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Mouse CD73 is a glycosyl phosphatidylinositol (GPI) anchored membrane protein that belongs to the 5'-nucleotidase family. CD73 is an ecto 5'Nucleotidase expressed by most cell types. CD73 hydrolyses extracellular nucleotides into membrane permeable nucleosides. CD73 is one of several enzymes responsible for the production of extracellular adenosine, a signalling molecule that is involved in responses to inflammation and tissue injury. CD73 is a lymphocyte maturation marker that has functions independent of its catalytic activity. CD73 is also a regulator of leukocyte extravasation, a function that requires its 5'Nucleotidase activity.CD73 has also been reported to regulate expression of pro-inflammatory molecules in mouse endothelium.

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PAPSS1 is a bifunctional enzyme with both ATP sulfurylase and APS kinase activity. In the N-terminal section, it belongs to the APS kinase family; while the C-terminal section belongs to the sulfate adenylyltransferase family. PAPSS1 can be inhibited by chlorate, and is expressed in many tissues, such as high endothelial venules (HEV) cells and in cartilage. PAPSS1 mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate. In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. PAPSS1 also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells.

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Sentrin-Specific Protease 8 (SENP8) mediates the reversible covalent modification of proteins by NEDD8. SENP8 catalyses the full-length NEDD8 to generate its mature form and deconjugation of NEDD8 from targeted proteins such as CUL2 , CUL4A in vivo, or p53. but it does not show activity against ubiquitin or SUMO proteins.

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Benzonase® nuclease degrades all forms of DNA and RNA while having no proteolytic activity. Benzonase® is compatible with BugBuster® and PopCulture® protein extraction reagents and therefore can be added to these reagents to eliminate viscosity and remove nucleic acids from E. coli extracts.

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AKR1C3, is an enzyme which belongs to the aldo/keto reductase family. It is expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. AKR1C3 catalyses the conversion of aldehydes and ketones to alcohols. It catalyses the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2,which functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. It can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites.

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Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyses the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

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ALPP is a membrane protein and exits as a homodimer. ALPP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It has been shown to play a role in a number of processes including cell signaling, long-term potentiation, and cell adhesion, however, the best known and most commonly studied role is implicated in Alzheimer's research.

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Human Esterase D is a serine hydrolase that is involved in the detoxification of formaldehyde. Esterase D plays a part in a variety of substrates, including O-acetylated sialic acids, which may involves in the recycling of sialic acids. Esterase D can be used as a genetic marker for retinoblastoma and Wilson’s disease.

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NAD kinase catalyses the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis.

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Nicotinate Phosphoribosyltransferase (NAPRTase) is involved in the biological processes of pyridine nucleotide biosynthesis and nicotinate nucleotide salvage and functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). It is a crucial factor in the NAD+ biosynthesis pathway. Catalytic activity: Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.