Hledali jste: Enzymy

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Human DNA polymerase beta is constitutively expressed in cells. It fills in gaps in DNA that are formed following base excision repair. The activity cannot be affected by Aphidicolin, which is an inhibitor of DNA polymerase beta .

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ACYP1, also known as Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1 and ACYPE, is a small cytosolic enzyme which catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates. ACYP1 is a protein which belongs to the acylphosphatase family and contains 1 fibrinogen C-terminal domain. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase, on the basis of their tissue localisation. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis. Recombinant human ACYP1 protein was expressed in E. coli fused with HIS-tag at N-terminus.

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SWSAP1 is a nucleus ATPase protein, interacts with ZSWIM7 and forms a functional complex. The complexs involved in homologous recombination repair and stabilises each other. SWS1AP1 also interacts with RAD51, RAD51B, RAD51C, RAD51D and XRCC3. It involves in homologous recombination repair. ATPase is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). SWSAP1 has a DNA-binding activity which is independent of its ATPase activity.

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Arginase-1 (ARG1) is also known as Liver-type arginase, Type I arginase, which belongs to the arginase family. Arginase-1 / ARG1 is a manganese-containing enzyme. The reaction catalysed by this enzyme is: arginine + H2O → ornithine + urea. It is the final enzyme of the urea cycle. Defects in Arginase-1 / ARG1 are the cause of argininemia (ARGIN).

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Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults.

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Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH/MDH superfamily. MDH type 1 family. MDH2 catalyses the reversible oxidation of malate to oxaloacetate, utilising the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localised to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.

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Hog Acylase (from Kidney)

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Aspergillus niger Pectinase

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Human nicotinate phosphoribosyltransferase (NAPRTase) is localised in the cytoplasm and is involved in biological processes such as NAD biosynthetic and metabolic processes, nicotinamide metabolic process, nicotinate nucleotide salvage, response to oxidative stress and water-soluble vitamin metabolic process. It functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN) and is essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. 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.

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Chymotrypsin-Like Protease CTRL-1 is a protease that belongs to the peptidase S1 family. Human CTRL-1 is synthesised as a 264 amino acid (aa) precursor that contains an 18 aa signal sequence, 15 aa activation peptide and a 231 aa mature chain. CTRL-1 Contains 1 peptidase S1 domain. It has many molecular functions, such as hydrolase, protease, and serine protease. CTRL-1 plays a role in digest and hydrolyse proteins in biological process.

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Carbonic Anhydrase 3 (CA3) belongs to the Alpha-Carbonic Anhydrase family that encodes carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyse the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and it is present at high levels in skeletal muscle with much lower levels found in cardiac and smooth muscle. CA3 is activated by proton donors such as imidazole and the dipeptide histidylhistidine. CA3 is inhibited by coumarins and sulfonamide derivatives such as acetazolamide.

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GMP Reductase 1 (GMPR) is a member of the IMPDH/GMPR family. GMPR exists as a homotetramer and catalyses the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. GMP reductase gene expression may be regulated by MITF. At least two different alleles are known.

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Carbonic Anhydrase 7 (CA7) is a member of the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Furthermore, Alpha-carbonic anhydrase is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA7 is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine, but it is inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA) by saccharin and Foscarnet.

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Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localisation, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerisation and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyses the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

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Endoplasmic Reticulum Mannosyl-Oligosaccharide 1,2- alpha-Mannosidase (MAN1B1) belongs to the glycosyl hydrolase 47 family. MAB1B1 is a single-pass type II membrane protein and widely expressed in many tissues. MAB1B1 is involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. MAB1B1 can be inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine. Defects in MAN1B1 are the cause of mental retardation autosomal recessive type 15 (MRT15). Mental retardation is characterised by significantly below average general intellectual functioning, it is also associated with impairments in adaptative behavior and manifested during the developmental period.

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N-Sulphoglucosamine Sulphohydrolase (SGSH) is an important member of the sulphatase family which is involved in the degradation of heparin sulphate. SGSH binds one calcium ion per subunit as a cofactor. SGSH catalyses N-sulfo-D-glucosamine and H₂O to D-glucosamine and sulphate. SGSH deficiency is result in mucopolysaccharidosis type 3A (MPS3A), a recessive lysosomal storage disease characterised by neurological dysfunction but relatively mild somatic manifestations.

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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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N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family. N-Acetylglucosamine-6-Sulfatase is required for the lysosomal degradation of the Glycosaminoglycans (GAG) Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase hydrolyses the 6-Sulfate groups of the N-Acetyl-D-Glucosamine 6-Sulfate units of Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase binds 1 Calcium ion per subunit. N-Acetylglucosamine-6-Sulfatase deficiency are the cause of Mucopolysaccharidosis Type 3D (MPS3D), an inborn error leading to lysosomal accumulation of heparan sulfate. MPS3D has profound mental deterioration, hyperactivity, and relatively mild somatic manifestations.

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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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Horseradish peroxidase

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Ketohexokinase, also known as Hepatic fructokinase, is a member of the carbohydrate kinase PfkB family. It exits as a homodimer and most abundant in liver, kidney, gut, spleen and pancreas. Low levels also found in adrenal, muscle, brain and eye.This enzyme catalyses conversion of fructose to fructose-1-phosphate. It is the first enzyme with a specialised pathway that catabolises dietary fructose. Defects in KHK are the cause of fructosuria.

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6-phosphogluconate dehydrogenase(PGD) is a cytoplasm-located protein, and belongs to the 6-phosphogluconate dehydrogenase family. 6PGD is the second dehydrogenase in the pentose phosphate shunt. It catalyses the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO₂, with concomitant reduction of NADP to NADPH. Mutations within the gene coding this enzyme result in 6-phosphogluconate dehydrogenase deficiency, an autosomal hereditary disease effecting the red blood cells.

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Galactose Mutarotase (GALM) is a cytoplasmic enzyme that belongs to the Aldose Epimerase family. GALM is a Mutarotase that converts alpha-Aldose to the beta -Anomer. GALM is active on D-Glucose, L-Arabinose, D-Xylose, D-Galactose, Maltose and Lactose. GALM may be required for normal Galactose metabolism by maintaining the equilibrium of alpha- and beta - anomers of Galactose.

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X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyses the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.

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Hyaluronidase-1 (HYAL1) is a secreted lysosomal hyaluronidase that belongs to the glycosyl hydrolase 56 family. HYAL1 contains one EGF-like domain and is highly expressed in the liver, kidney, and heart, but it is weakly expressed in the lung, placenta, and skeletal muscle. HYAL1 is thought to be involved in cell proliferation, migration, and differentiation. It may play a role in promoting tumor progression and blocking the TGFB1-enhanced cell growth. Mutations in HYAL1 are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency.

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Pancreatic Lipase-Related Protein 2 (PNLIPRP2) is a secreted protein that belongs to the Lipase family of AB hydrolase superfamily. PNLIPRP2 is a lipase with broad substrate specificity that contains one PLAT domain. PNLIPRP2 is expressed mainly in pancreas. PNLIPRP2 can hydrolyse both phospholipids and galactolipids. PNLIPRP2 acts preferentially on monoglycerides, phospholipids and galactolipids. PNLIPRP2 also contributes to milk fat hydrolysis.

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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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Phosphomevalonate kinase (PMVK) is a cytosolic enzyme. PMVK can be highly expressed in the heart,skeletal muscle, liver, pancreas, and kidney; it is expressed at lower levels in the brain, lung, and placenta. Induced by sterol, PMVK takes part in isopentenyl diphosphate biosynthesis through the mevalonate pathway. PMVK catalyses the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway.

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Carbonic Anhydrase 5B (CA5B) is a member of alpha-carbonic anhydrase family (CAs) that catalyze the reversible hydration of carbon dioxide. CAs is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA5B is highly expressed in heart, pancreas, kidney, placenta, lung, and skeletal muscle, but it is restricted to the liver. CA5B is localised in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA-VA. CA5B is inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin, and Foscarnet.

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Fumarase is an enzyme that catalyze the reversible hydration/dehydration of fumarate to S-malate and is involved in the tricarboxylic acid or Krebs cycle. Fumarase exists in both form, cytosolic formand N-terminal extend mitochondrial form. The N-terminal extended form is targeted to the mitochondrion, where the removal of the extension is the same form as in the cytoplasm. Fumarase is thought to act as a tumour suppressor, which deficiency can lead to progressive encephalopathy, cerebral atrophy and development delay.