Hai cercato: Enzimi

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Sulfotransferase 1A1 (SULT1A1) is a cytosolic sulfotransferases that is expressed in the liver, lung, adrenal, brain, platelets, and skin. SULT1A1 is a phenol sulfotransferases with thermostable enzyme activity. SULT1A1 utilises 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyse the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. It is responsible for the sulfonation and activation of minoxidil. SULT1A1 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.

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SENP2 is an enzyme that belongs to the peptidase C48 family. SENP2 is a protease that catalyses two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. SUMO1 is a small ubiquitin-like protein that can be covalently conjugated to other proteins. It has been implicated as a down-regulator of CTNNB1 levels and may therefore be a modulator of the Wnt pathway.

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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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Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, alpha1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Glucose-6-phosphate dehydrogenase (from Yeast)

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Horseradish peroxidase

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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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Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family. PPIases can accelerate the folding of proteins and catalyze the cis-trans isomerisaion of proline imidic peptide bonds in oligopeptides. PPIase is a ubiquitous protein and has highly expression in heart ,skeletal and muscle. PPIase contains a PPIase cyclophilin-type domain and four Cyclosporin A binding regions. PPIase might play an important role in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is suggested that PPIase can act as as a novel molecular target for colon-cancer therapy.

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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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PGK1 is called phosphoglycerate kinase that involved in a critical energy-producing process known as glycolysis. Phosphoglycerate kinase helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 The encoded protein may also act as a cofactor for polymerase alpha.. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.

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D-tyrosyl-tRNA(Tyr) deacylase 1(DTD1) belongs to the DTD family, and expressed in many adult and fetal tissues such as testis, ovary, spleen in adult and fetal brain. It is a nucleus and cytoplasm located protein, and is preferentially phosphorylated in cells arrested early in S phase. DTD1 is an ATPase involved in DNA replication, it may facilitate loading of CDC45 onto pre-replication complexes. The protein may hydrolyse D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine.

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Selenophosphate synthetase 1 (SEPHS1) belongs to the selenophosphate synthase 1 family, Class II subfamily. It has four different isoforms by alternative splicing. Isoform 1 and isoform 2 are gradually expressed during the cell cycle until G2/M phase and then decreased, which Isoform 3 is gradually expressed during the cell cycle until S phase and then decreased. SEPHS1 can be activated by phosphate ions and by potassium ions. It can synthesise synthesises selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesise selenocysteine, which is co-translationally incorporated into selenoproteins at in-frame UGA codons.

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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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Phosphoserine phosphatase (PSP) is an enzyme that belongs to the serB family. PSPH catalyses magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Deficiency of this protein is thought to be linked to Williams syndrome. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.

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N-acetylgalactosaminyltransferase 7(GALNT7) is expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.It belongs to the glycosyltransferase 2 family and galNAc-T subfamily. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation.

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Human Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3) is an enzyme that in humans is encoded by the B3GAT3 gene, belongs to the glycosyltransferase 43 family. B3GAT3 is involved in a number of biological processes such as catalyzing the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans, forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate, gGlycosaminoglycans biosynthesis, transfering a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.It also plays a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins , hows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc and stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation.

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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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Mouse Ca14,also known as Carbonic anhydrase 14,is a member of large family of zinc metalloenzymes. It could catalyse reversible hydration of carbon dioxide. The reaction is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. Fifteen CA isoforms have been reported so far. They have different patterns of tissue-specific expression and physiologic roles. Some CAs may serve as markers for tumours and hypoxia. CA XIV is a polypeptide consisting of an extracellular N-terminal catalytic domain, a membrane-spanning segment and a short intracellular C- terminal segment with several potential phosphorylation sites. A subset of CAs lack CA activity due to point mutations but retain esterase function. CA14 is widely expressed in the central nervous system.

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Aldo-Keto Reductase Family 1 Member C2 (AKR1C2) plays a role in concert with the 5- alpha/5- beta -Steroid Reductases to convert Steroid hormones into the 3- alpha/5- alpha and 3- alpha/5- beta -Tetrahydrosteroids. AKR1C2 catalyses the inactivation of the most potent androgen 5- alpha-Dihydrotestosterone (5- alpha-DHT) to 5- alpha-Androstane-3- alpha, 17- beta -diol (3- alpha-diol).

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Carbonic Anhydrase X (CA10) belongs to CA family of zinc metalloenzymes, which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. While CA10 is a secreted protein without Carbonic Anhydrase activity (i.e., the reversible hydration of CO2) due to point mutations in the zinc binding site, it has esterase activity. The human and mouse CA10 are expressed in the brain, indicating that they may play a role in brain development.

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Fructose Bisphosphate Aldolase A (ALDOA) belongs to the class I fructose-bisphosphate aldolase family. ALDOA is a glycolytic enzyme that catalyses the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, Aldolase A in muscle, Aldolase B in liver and aldolase C in brain. Aldolase A Interacts with SNX9 and WAS. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. In addition, Aldolase A plays an important role in glycolysis and gluconeogenesis; it may also act as a scaffolding protein.

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Cyclin-dependent kinase 2 (CDK2) belongs to the cyclin-dependent kinase of Ser/Thr protein kinase. CDK2 acts as a catalytic subunit of the cyclin dependent kinase complex, whose activity is restricted to the G1-S phage of the cell cycle, it is essential for the G1/S transition. The kinase activity of CDK2 can be regulated by the association with a cyclin subunit, its phosphorylation state and CDK inhibitors. The activation of the CDK2/cyclin complex requires the phosphorylation of Thr160 and the dephosphorylation of Try14 and Tyr15. The inhibition of CDK2-cyclin complex can also be attributed to association with p27Kip1 and p21Waf1/Cip1. The activation of CDK2 has been shown to be necessary for apoptosis of quiescent cells, such as neurons, thymocytes and endothelial cells.

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Prostaglandin-H2 D-Isomerase (PTGDS) belongs to the Lipocalin family of calycin superfamily. PTGDS is preferentially expressed in the brain. PTGDS catalyses the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. PTGDS is involved in a variety of CNS functions, such as sedation, REM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. PTGDS binds small non-substrate lipophilic molecules and may act as a scavenger for harmful hydrophopic molecules and a secretory retinoid and thyroid hormone transporter. It possibly participates in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor, blood-testis barrier, the central nervous system and male reproductive system.

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Carboxylesterase 5 (CES5), also called cauxin or CES7, is a member of carboxylesterases family which plays an important role in the hydrolysis of ester and amide bonds. Carboxylesterase is a type of enzyme that capable of hydrolysing a variety of carboxylic acid esters and it's widely distributed in cells especially in mammalian liver. CES5 is with broad substrate specificity ranging from small molecule esters to longchain fatty acid esters and thioesters. It has been previously reported CES5 was in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones, catalysing lipid transfer reactions within mammalian male reproductive fluids, and protecting neural tissue from drugs and xenobiotics.

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Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyses the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.

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NadN (NAD nucleotidase) is a periplasmic enzyme from Haemophilus influenzae, a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. NadN plays a central role by degrading NAD into adenosine and NR (nicotinamide riboside), NMN to nicotinamide riboside and AMP to adenosine. It shows a broad substrate specificity, recognising either mono- or di-nucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. It can be used as an economically alternative to produce NR (nicotinamide riboside). Catalytic activity: NAD=AMP + NMN=Ade+NR+PPi | AMP=Ade+Pi | NMN=NR+Pi.

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Xaa-Pro aminopeptidase 2 (XPNPEP2) belongs to the peptidase M24B family of metalloproteases. Human XPNPEP2 is widely expressed in various tissues, such as kidney, lung, heart, placenta, liver, small intestine and colon. However, it doesn’t express in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary. XPNPEP2 is a Homotrimer which binds 2 manganese ions per subunit. The metalloprotease XPNPEP2 may play a role in the inflammatory process and other reactions produced in response to injury or infection and the metabolism of the vasodilator bradykinin.

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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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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.