You searched for: Enzymes

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Carbonic Anhydrase (CA) XII, also known as Car12 and CA12, is an extracellular enzyme involved in the regulation of the microenvironment acidity and tumour malignant phenotype, was originally identified as a protein overexpressed in some types of cancers. It has showed that CA XII is induced by hypoxia and oestrogen and expressed at high levels on various types of cancer. The enzyme is directly involved in tumour progression, and its inhibition has an anti-tumour effect. Apart from its role in carcinogenesis, the enzyme contributes to various other diseases like glaucoma and arteriosclerotic plaques, among others. CA XII is therefore regarded as promising target for specific therapies, and may be used as a novel prognostic marker in combination with histologic grade of the tumours.

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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.

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Thymidine kinase 1(TK1) belongs to the thymidine kinase family. It is located in the cytoplasm, and phosphorylated on Ser-13 in mitosis during post-translational modification. Two forms of this protein have been identified in animal cells, one in cytosol TK1 and one in mitochondria TK2. Thymidine kinases have a key function in the synthesis of DNA and thereby in cell division, as they are part of the unique reaction chain to introduce deoxythymidine into the DNA. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle, while it is very low in resting cells. TK1 acts as a homotetramer, and can transform thymidime to thymidine 5'-phosphate with the help of ATP.

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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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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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Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyses the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.

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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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The 3-hydroxykynurenine transaminase (3-HKT) gene plays a vital role in the development of malaria parasites by participating in the synthesis of xanthurenic acid, which is involved in the exflagellation of microgametocytes in the midgut of malaria vector species. The 3-HKT enzyme is involved in the tryptophan metabolism of Anophelines. The gene had been studied in the important global malaria vector, Anopheles gambiae.

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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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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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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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Lipase family. The gene encoding this protein is expressed mainly in brain, liver and testes,followed by secreting into plasma and cerebral spinal fluid. The esterification of cholesterol is required for cholesterol transport. LCAT is a central enzyme in the extracellular metabolism of plasma lipoproteins. Defects in LCAT are the cause of lecithin-cholesterol acyltransferase deficiency (LCATD) and a cause of fish-eye disease (FED).

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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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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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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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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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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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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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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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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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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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Elastase substrate V

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

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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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NAD Kinase (NADK) is an enzyme that belongs to the NAD Kinase family. It is a widely expressed enzyme, but it is not detected in skeletal muscle. NADK converts Nicotinamide Adenine Dinucleotide (NAD+) into NADP+, through phosphorylating the NAD+ coenzyme. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined.