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| Product | Description | |
|---|---|---|
| alditol oxidase | The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly. Belongs in the vanillyl-alcohol-oxidase family of enzymes. Group: Enzymes. Synonyms: xylitol oxidase; xylitol:oxygen oxidoreductase; AldO. Enzyme Commission Number: EC 1.1.3.41. CAS No. 177322-52-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0414; alditol oxidase; EC 1.1.3.41; 177322-52-0; xylitol oxidase; xylitol:oxygen oxidoreductase; AldO. Cat No: EXWM-0414. |  |
| benzoyl-CoA 2,3-epoxidase | The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii. BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of monooxygenation. BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein (FAD), BoxB is a monomeric iron-protein. Group: Enzymes. Synonyms: benzoyl-CoA dioxygenase/reductase (incorrect); BoxBA; BoxA/BoxB system; benzoyl-CoA 2,3-dioxygenase (incorrect). Enzyme Commission Number: EC 1.14.13.208. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0809; benzoyl-CoA 2,3-epoxidase; EC 1.14.13.208; benzoyl-CoA dioxygenase/reductase (incorrect); BoxBA; BoxA/BoxB system; benzoyl-CoA 2,3-dioxygenase (incorrect). Cat No: EXWM-0809. | |
| cAMP-dependent protein kinase | cAMP is required to activate this enzyme. The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits [i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C]. Group: Enzymes. Synonyms: PKA; PKA C; protein kinase A; STK22. Enzyme Commission Number: EC 2.7.11.11. CAS No. 142008-29-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3130; cAMP-dependent protein kinase; EC 2.7.11.11; 142008-29-5; PKA; PKA C; protein kinase A; STK22. Cat No: EXWM-3130. | |
| Cholesterol Oxidase from Microorganism | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. Activity: 12U/mg-solid or more. Form: Freeze dried powder. Source: Microorganism. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-138. | |
| Cholesterol oxidase from Nocardia sp., Recombinant | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Activity: > 20 Units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Nocardia sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-1033. | |
| Cholesterol Oxidase from Streptomyces sp. | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. Activity: 15U/mg-solid or more. Storage: -20°C. Form: Freeze dried powder. Source: Streptomyces sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0128. | |
| exoribonuclease II | Preference for single-stranded RNA. The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5 ribonuclease P. Group: Enzymes. Synonyms: ribonuclease II; ribonuclease Q; BN ribonuclease; Escherichia coli exo-RNase II; RNase II; exoribonuclease (misleading); 5'-exoribonuclease (misleading). Enzyme Commission Number: EC 3.1.13.1. CAS No. 37288-24-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3536; exoribonuclease II; EC 3.1.13.1; 37288-24-7; ribonuclease II; ribonuclease Q; BN ribonuclease; Escherichia coli exo-RNase II; RNase II; exoribonuclease (misleading); 5'-exoribonuclease (misleading). Cat No: EXWM-3536. | |
| Native Bacillus sp. Sarcosine Oxidase | Sarcosine oxidase is an enzyme (EC 1.5.3.1) that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy. Monomeric sarcosine oxidase (msox) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (n-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. monomeric sarcosine oxidase can oxidize other secondary amino acids such as n-methyl-l-alanine, n-ethylglycine, and l-proline. Applications: Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins. Group: Enzymes. Synonyms: Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Activity: 25-50 units/mg solid. Storage: -20°C. Form: lyophilized powder; No stabilizers added. Source: Bacillus sp. Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Cat No: NATE-0664. | |
| Native Bovine Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Protein determined by biuret. Applications: Cholesterol esterase bound to membrane-associated heparin on b...terase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 200 units/g protein. Storage: -20°C. Form: Lyophilized powder. This product is partially purified from bovine pancreas and is supplied as an off-white to tan lyophilized powder containing 30-65% protein (biuret), potassium phosphate. Source: Bovine pancreas. Species: Bovine. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrol | |
| Native Candida cylindracea Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Hydrolase that splits fatty acids from sterols. rely on the proven diagnostic quality of this product. Applications: Use cholesterol esterase in diagnostic tests for the determination of cholesterol in combination with cholesterol oxidase. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester s. Cholesterol Esterase. Activity: >10.5 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Almost white lyophilizate. Source: Candida cylindracea. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0984. | |
| Native Microorganisms Pyruvate Oxidase | Pyruvate Oxidase consists of four subunits with identical molecular weights. PoxB reacts with certain aldehydes and phosphate can be replaced by arsenate. Oxygen as well as several artificial compounds can function as electron acceptors. Pyruvate Oxidase is activated by phospholipids as well as monomeric and micellar amphiphiles. Applications: Pyruvate oxidase (poxb) converts pyruvate directly to acetate and co2. it is used to study pyruvate metabolism. it is used to study aerobic metabolism of bacterium, such as lactobacillus plantarumand strept oc occus pneumoniae. pyruvate oxidase is used for enzymatic determination of pyruvate, got, and gpt in clinical analysis. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: mol wt ~260 kDa. Activity: > 1.5 units/mg; > 35 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing FAD and sugar as stabilizer. Source: Microorganisms. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: NATE-0613. | |
| Native Nocardia erythropolis Cholesterol Oxidase | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6; CHOD; cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Activity: > 15 U/mL. Stability: Stable at -20°C for at least one year. Storage: 2-8°C. Form: in 1 M ammonium sulfate solution, pH 6, solution (slightly hazy). Source: Nocardia erythropolis. EC 1.1.3.6; CHOD; cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0127. | |
| Native Porcine Apo D-Amino Acid Oxidase | Apo-D-amino acid oxidase is entirely present as a monomeric protein, while the reconstituted holoenzyme is a dimer of 79 kDa. Group: Enzymes. Synonyms: Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. Purity: 0.9. DAAO. Activity: 25-30 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Porcine Kidney. Species: Porcine. Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Cat No: NATE-1872. | |
| Native Pseudomonas fluorescens Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Protein determined by biuret. Applications: Cholesterol esterase from pseudomonas fluorescens has...iterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 10,000 units/g protein. Storage: -20°C. Form: lyophilized powder. Source: Pseudomonas fluorescens. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0116. | |
| Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase | Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria. Applications: Ferredoxin-nadp+ reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. it was also used to regulate glyceraldehyde-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reducta. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Activity: > 15 units/mg solid, secondary activity: > 10 units/mg solid NADPH diaphorase. Storage: -20°C. Form: lyophilized powder. Source: Spinacia oleracea (Spinach). EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase; 9029-33-8; FNR. Cat No: NATE-0256. | |
| Native Staphylococcus aureus α-Hemolysin | α-Hemolysin is a 33 kDa extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is selectively hemolytic and has a marked preference for rabbit red blood cells. It induces dermonecrosis, spastic muscle paralysis, and it is lethal for laboratory animals. The toxin must be in the monomeric form to initially bind to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites. Group: Enzymes. Synonyms: α-Hemolysin; 94716-94-6; α-Toxin. α-Hemolysin. Activity: > 10,000 units/mg protein. Storage: 2-8°C. Source: Staphylococcus aureus. α-Hemolysin; 94716-94-6; α-Toxin. Cat No: NATE-0753. | |
| Native Streptomyces griseus Aminopeptidase I | Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070. | |
| Native Streptomyces sp. Cholesterol Oxidase | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Applications: Cholesterol oxidase from streptomyces has been used in a study to assess the relationship between the micellar structure of model bile and the activity of esterase. cholesterol oxidase from streptomyces has also been used in a study to investigate the effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell ...ton boll weevil. chod has also been used as a molecular probe to elucidate cellular membrane structures. Group: Enzymes. Synonyms: EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Mole weight: mol wt ~34 kDa. Activity: > 20 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing bovine serum albumin and sugars as stabilizers. Source: Streptomyces sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0128. | |
| Protein Kinase A Catalytic Subunit β, Active human, Recombinant | cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the protein kinase A (PKA), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of PKA is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of PKA have ...e crebtide substrate peptide per minute per mg protein at 30°c using a final concentration of 50 μm [32p] atp. Group: Enzymes. Synonyms: PKA Catalytic Subunit β, Active human; PKA-Cβ; cAMP-dependent protein kinase; PKACB; PRKACB; PKA C-beta; Protein Kinase A Catalytic Subunit &beta. Purity: > 85% (SDS-PAGE). PKAC. Mole weight: protein apparent mol wt ~65 kDa. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected Sf9 cells. Species: Human. PKA Catalytic Subunit β, Active human; PKA-Cβ; cAMP-dependent protein kinase; PKACB; PRKACB; PKA C-beta; Protein Kinase A Catalytic Subunit &beta. Cat No: NATE-0572. | |
| small monomeric GTPase | A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the α-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies). Group: Enzymes. Enzyme Commission Number: EC 3.6.5.2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4713; small monomeric GTPase; EC 3.6.5.2. Cat No: EXWM-4713. | |
| Native Bovine Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Bovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. at least three isoforms exist, which typically possess two n-linked and one or more o-linked glycans per monomer.2 the enzyme requires zinc, and magnesium or calcium divalen...r proteins for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein labeling when high sensitivity is required. alkaline phosphatase may be also be used to dephosphorylate the 5?-termini of dna or rna to prevent self-ligation. dna or rna can also be tagged with radiolabeled phosphate (via t4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase. this product has been used to study the mon oclonal alkaline phosphatase-anti-alkaline phosphatase (apaap) complex. high specific activity grade recommended for antibody and protein conjugation. Group: Enzymes. Synonyms | |
| Native Bovine intestinal mucosa Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Bovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. at least three isoforms exist, which typically possess two n-linked and one or more o-linked glycans per monomer.2 the enzyme requires zinc, and magnesium or calciu...s for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein labeling when high sensitivity is required. alkaline phosphatase may be also be used to dephosphorylate the 5?-termini of dna or rna to prevent self-ligation. dna or rna can also be tagged with radiolabeled phosphate (via t4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase. this product has been used to study the mon oclonal alkaline phosphatase-anti-alkaline phosphatase (apaap) complex. high specific activity grade recommended for antibody and protein conjugation. Group: Enzymes. Synonyms | |
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