You searched for: Enzymes

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Sulfotransferase 1A2 (SULT1A2) is a member of the Sulfotransferase 1 family. Sulfotransferase enzymes catalyse the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. SULT1A2 is a cytoplasmic protein and exists as a homodimer. SULT1A2 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and might thus participate as a modulating factor of cancer risk.

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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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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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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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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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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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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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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.

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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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Inositol monophosphatase 2, also known as Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2 and IMPA2, is an enzyme which belongs to the inositol monophosphatase family. IMPA2 catalyses the dephosphoylration of inositol monophosphate with cofactor Magnesium and Inhibited by high Li+ and restricted Mg2+ concentrations. IMPA2 plays an important role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain, it is considered to have a role in schizophrenia and bipolar disorder.

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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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These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. CPM is widely distributed in a variety of tissues and cells. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.

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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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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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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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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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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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Elastase substrate V

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Trypsin is used to enzymatically release adherent cells from tissue culture plates for passaging

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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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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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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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Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyses the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.

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Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

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Protein Disulfide-Isomerase A4 (PDIA4) is an endoplasmic reticulum luminal protein that belongs to the protein disulfide isomerase family. Human PDIA4 is synthesised as a 625 amino acid precursor that contains a 20 amino acid signal sequence, and a 625 amino acid mature chain, including three thioredoxin domains. PDIA4 catalyses the rearrangement of -S-S- bonds in proteins and is thought to be a deoxycytidine kinase. In addition, PDIA4 serves as a proteases protein disulfide isomerase, phospholipase or an arrangement of these.

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Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily. PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.

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Tripeptidyl-Peptidase 1 (TPP1) belongs to the peptidase S53 family. TPP1 is detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues. TPP1 is lysosomal serine protease with tripeptidyl-peptidase I activity. TPP1 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. TPP1 requires substrates with an unsubstituted N-terminus. TPP1 mutations have also been shown to cause neuronal ceroid lipofuscinosis type 2 (CLN2).