You searched for: Enzymes

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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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Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesised as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER , the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis.PCSK9 also plays a role in neural development.

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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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Geranylgeranyl pyrophosphate synthase (GGPS1) is a member of the FPP/GGPP synthase family. GGPS1 is highly expressed in testis, heart and skeletal muscle. GGPS1 is localised in the cytoplasm and has geranylgeranyl diphosphate (GGPP) synthase activity. It catalyses the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. Other transcriptional splice variants have been found.

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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 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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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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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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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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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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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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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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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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Collagenases are enzymes that break the peptide bonds in collagen.

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Collagenases are enzymes that break the peptide bonds in collagen.

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Papain, powder, purified, is a cysteine protease enzyme the is present in the papaya fruit.

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Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).

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Zymolyase-20T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells. The primary enzyme in this preparation responsible for lysis of viable yeast cells is ß-1,3-glucan laminaripentaohydrolase. It hydrolyzes glucose polymers at the ß-1,3-glucan linkages releasing laminaripentaose as the principal product.

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One bacterial amylase unit is defined as that quantity of enzyme which will dextrinise one milligram of starch per minute at pH 6,6 and 30 °C.

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Pepsin is an acid protease, contains a proteolytic enzyme. It contains the "cathepsin" component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.

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Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid +¹/₂ O₂ ascorbate oxidase → Dehydroascorbic acid +H₂O.

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For typical assay, dissolve enzyme at a concentration of 1 mg/ml in 0,05 M TES with 0,36 mM calcium chloride, pH 7,5. Dilutions run are 1/10 and 1/20 in the above buffer.

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The hyaluronidase is purified from Streptomyces hyalurolyticus. This enzyme belongs to the endo-beta-hexosaminidase and endo-eliminase type enzyme that produces oligo-saccharide (unsaturated tetraose and pentose) by hydrolysing the beta-1,4-linkage of hyaluronic acid. It is stable in both high temperature and acid or alkaline range. It has high substrate specificity and hydrolyzes hyaluronic acid only in mucopolysaccharide.

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Alkaline phosphatase is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids.

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Cellulase refers to a group of enzymes which, acting together, hydrolyse cellulose. The b-glucosidases, including cellobiose, are primarily active on the smaller molecular weight cellulose hydrolysates. During cellulose breakdown they are active on the dimers and oligomers of cellulose.

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Unit Definition: Enzyme activity is determined by a change in optical density in a solution of hyaluronic acid. Activity is compared to a hyaluronidase International Standard and is expressed as an International Unit (U).

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HRP is a plant glycohemoprotein belongs to the ferroprotoporphyrin group of peroxidases. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens.

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Pancreatin are natural chemicals that help break down fats, proteins, and carbohydrates. Pancreatin is a digestive enzyme produced by the pancreas and delivered to the small intestine for the hydrolysis of complex nutrients.

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Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.

Supplier: MP Biomedicals

Activity: Each vial contains 500 units β-Lactamase I and 50 units β-Lactamase II Unit Definition: One unit is defined as the amount of enzyme which will hydrolyse 1,0 micromole of benzyl penicillin and 1,0 micromole of cephalosporin C per minute at 25 °C in the presence of EDTA pH 7,0.