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Carbonic Anhydrase 1 (CA1) is a cytosolic enzyme, belonging to the alpha-carbonic anhydrase family. It is highly expressed in erythrocytes and acts as an early marker for erythroid differentiation. Carbonic anhydrase 1 plays a improtant role in many biological processes such as calcification, cellular respiration, bone resorption, acid-base balance. It is activated by imidazole, histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. At the same time, It is inhibited by sulfonamide derivatives and coumarins. In addition, CA1 is a zinc metalloenzyme that has reversible hydration of carbon dioxide. It can hydrate cyanamide to urea.

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Protein-glutamine gamma-glutamyltransferase 2 (TGM2) is a 78-kDa, calcium dependent enzyme,It belongs to the transglutaminase superfamily and transglutaminase family. The protein encoded by this TGM2 gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. TGM2 is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene.

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Thymidylate kinase (DTYMK) is a ubiquitous enzyme of about 25 kD which belongs to thymidylate kinase family. DTYMK is important in the dTTP synthesis pathway for DNA synthesis. It participated in the pyrimidine metabolism pathway and dTTP biosynthesis pathway. DTYMK catalyses the conversion of dTMP to dTDP and catalyses the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium. Structural and functional analyses suggest that the cDNA codes for authentic human dTMP kinase. The mRNA levels and enzyme activities corresponded to cell cycle progression and cell growth stages.

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Bile Salt Sulfotransferase (SULT2A1( is a cytosolic enzyme that belongs to the Sulfotransferase 1 family. SULT2A1 is primarily expressed in the liver and adrenal tissues, and to a lesser extent in the kidney. SULT2A1 utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor, and it catalyse the sulfonation of steroids and bile acids in the liver and adrenal glands. SULT2A1 may have a role in the inherited adrenal androgen excess.

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Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene, belongs to the aldehyde dehydrogenase family. ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidises aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.

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Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.

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Mouse Carboxylesterases 3 (CES3) is a member of five families of mammalian carboxylesterases that plays a role in catalysing hydrolytic and transesterification reactions with xenobiotics, anticancer pro-drugs and narcotics, and detoxifying organophosphates and insecticides. Mammalian carboxylesterases are enzymes with broad substrate specificities ranging from small molecule esters to longchain fatty acid esters. It is shown that CESs has key roles in the metabolism of a wide variety of clinical drugs, illicit narcotics and chemical nerve agents. CES3 is broadly expressed in liver, colon and brain.

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Selenocysteine Lyase belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Selenocysteine Lyase exists as a homodimer in the cytosol. In the brain, Selenocysteine Lyase is as an enzyme that putatively salvages Sec and recycles the selenium for selenoprotein translation. Selenocysteine Lyase catalyses the decomposition of L-selenocysteine to L-alanine and elemental selenium. Selenocysteine Lyase can be up-regulated In acute glomerulonephritis, it can also be regulated by JUN/AP-1.

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Sialic Acid Synthase (NANS) is an enzyme that contains one AFP-like domain. NANS is ubiquitous and plays a role in the biosynthetic pathways of sialic acids. NANS produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). It also can use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

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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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Human N-Glycosylase/DNA Lyase is a DNA repair enzyme, which incises DNA at 8-oxoG residues, and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damage DNA. DGG1 has a beta -lyase activity that nicks DNA 3’ to the lesion.

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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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5-formyltetrahydrofolate cyclo-ligase (MTHFS) belongs to the 5-formyltetrahydrofolate cyclo-ligase family. It is an enzyme that catalyses the conversion of 5-formyltetrahydrofolate to 5,10-methenyltetrahydrofolate, contributes to tetrahydrofolate metabolism. MTHFS helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. An increased activity of the encoded protein can result in an increased folate turnover rate and folate depletion.

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Ribonuclease Pancreatic is a secreted enzyme that belongs to the pancreatic ribonuclease family. RNASE1 is an endonuclease that cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. RNASE1 prefers poly(C) as a substrate and hydrolyses 2',3'-cyclic nucleotides, with a pH optimum near 8.0. RNASE1 acts on single stranded and double stranded RNA.

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ACAT2 is a cytoplasmic enzyme which belongs to the thiolase family. ACAT2 takes part in lipid metabolism, lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. It is responsible for the synthesis of cholesteryl esters which are part of lipoproteins containing apoB. ACAT2 deficiency contributes to severe mental retardation and hypotonus.

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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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Caspase 14 (CASP14) is an enzyme that belongs to the peptidase C14A family. The Caspase 14 protein is complexed of unprocessed caspase-14 and processed 19 kDa (p19) and 10 kDa (p10) subunits. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes, which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerise to form the active enzyme. CASP14 has been shown to be processed and activated by Caspase 8 and Caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier. It is believed to be a non-apoptotic caspase which is involved in epidermal differentiation, keratinocyte differentiation and cornification. CASP14 probably regulates maturation of the epidermis by proteolytically processing filaggrin.

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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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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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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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Phosphomannomutase 2 (PMM2) is an enzyme that is a member of the highly variable methyltransferase superfamily. PMM2 is a cytoplasmic protein and catalyses the isomerisaion of mannose 6-phosphate to mannose 1-phosphate.In addition, PMM2 involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose that required for a number of critical mannosyl transfer reactions. Defects in PMM2 can results in congenital disorder of glycosylation type 1A (CDG1A). Congenital disorders of glycosylation are metabolic deficiencies in glycoprotein biosynthesis that usually cause severe mental and psychomotor retardation.

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Carboxypeptidase B1 is an exopeptidase which specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. Expressed mainly in pancreas, CPB1 is a useful serum marker for acute pancreatitis and pancreatic graft rejection.Human CPB1 consists of a signal peptide, a pro region, and a mature chain. The purified rhCPB1 corresponds to the pro form, which can be activated by trypsin, the only pancreatic protease capable of generating active enzyme from the zymogen in vitro.

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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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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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For enzyme digestion during DNA and RNA preparation. Both OB Protease and Proteinase K offer broad substrate specificity with high activity for a wide range of salts, denaturant and detergent, pH, and temperature conditions. Proteinase K is a subtilisin-type protease isolated from the saprophytic fungus Tritirachiumalbum and is particularly suitable for short digestion times. It possesses a high specific activity which remains stable over a wide range of temperatures and pH values with substantially increased activity at higher temperature.

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Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyses 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.

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Argininosuccinate Synthase (ASS1) is an urea cycle enzyme with a tetrameric structure composed of identical subunits. ASS1 is involved in the synthesis of arginine and catalyses that condensation of citrulline and aspartate to argininosuccinate using ATP. ASS1 is important to the urea cycle as it catalyses the important second last step in the arginine biosynthetic pathway. ASS1 mainly expressed in periportal hepatocytes, but also in most other body tissues. A deficiency of ASS1 causes citrullinemia (CTLN1), an autosomal recessive disease which is characterised by severe vomiting spells and mental retardation.

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Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.

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Methylmalonyl-CoA epimerase, mitochondrial（MCEE）is an enzyme which belongs to the glyoxalase I family. It converts (S)-methylmalonyl-CoA to the (R) form, catalyses the following chemical reaction: (R)-methylmalonyl-CoA (S)-methylmalonyl-CoA. It plays an important role in the catabolism of fatty acids with odd-length carbon chains. This protein deficiency is an autosomal recessive inborn error of AA metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.

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Alkaline Phosphatase, Tissue-Nonspecific Isozyme (ALPL) is a cell membrane protein which belongs to the alkaline phosphatase family. There are at least four distinct but related alkaline phosphatases in humans: intestinal AP (IAP), placental AP(PLAP), germ cell AP (GCAP) and their genes are clustered on chromosome 2, tissue-nonspecific isozyme (TNAP) which gene is located on chromosome 1. Alkaline phosphatases (APs) are dimeric enzymes, it catalyse the hydrolysis of phosphomonoesters with release of inorganic phosphate. The native ALPL is a glycosylated homodimer attached to the membrane through a GPI-anchor. This isozyme may play a role in skeletal mineralisation. Mutations in ALPL gene have been linked directly to different forms of hypophosphatasia,characterised by poorly mineralised cartilage and bones, and this disorder can vary depending on the specific mutation since this determines age of onset and severity of symptoms.