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| Product | Description | |
|---|---|---|
| 4-hydroxybenzoate polyprenyltransferase | This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound. The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency. Group: Enzymes. Synonyms: nonaprenyl-4-hydroxybenzoate transferase; 4-hydroxybenzoate transferase; p-hydroxybenzoate dimethylallyltransferase; p-hydroxybenzoate polyprenyltransferase; p-hydroxybenzoic acid-polyprenyl transferase; p-hydroxybenzoic-polyprenyl transferase; 4-hydroxybenzoate nonaprenyltransferase. Enzyme Commission Number: EC 2.5.1.39. CAS No. 9030-77-7. 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-2775; 4-hydroxybenzoate polyprenyltransferase; EC 2.5.1.39; 9030-77-7; nonaprenyl-4-hydroxybenzoate transferase; 4-hydroxybenzoate transferase; p-hydroxybenzoate dimethylallyltransferase; p-hydroxybenzoate polyprenyltransferase; p-hydroxybenzoic acid-polyprenyl transferase; p-hydroxybenzoic-polyprenyl transferase; 4-hydroxybenzoate nonaprenyltransferase. Cat No: EXWM-2775. |  |
| 8-dimethylallylnaringenin 2'-hydroxylase | A membrane-bound cytochrome P-450 heme-thiolate monooxygenase that is associated with the endoplasmic reticulum. This enzyme is specific for sophoraflavanone B as substrate. NADPH cannot be replaced by NADH, FAD or FMN. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2''-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. Group: Enzymes. Synonyms: 8-DMAN 2'-hydroxylase. Enzyme Commission Number: EC 1.14.13.103. 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-0702; 8-dimethylallylnaringenin 2'-hydroxylase; EC 1.14.13.103; 8-DMAN 2'-hydroxylase. Cat No: EXWM-0702. | |
| acetylalkylglycerol acetylhydrolase | Hydrolysis of the acetyl group from the 1-alkyl-2-acetyl and 1-alkyl-3-acetyl substrates occurs at apparently identical rates. The enzyme from Erlich ascites cells is membrane-bound. It differs from lipoprotein lipase (EC 3.1.1.34) since 1,2-diacetyl-sn-glycerols are not substrates. It also differs from EC 3.1.1.47, 1-acetyl-2-alkyl-glycerophosphocholine esterase. Group: Enzymes. Synonyms: alkylacetylglycerol acetylhydrolase. Enzyme Commission Number: EC 3.1.1.71. 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-3499; acetylalkylglycerol acetylhydrolase; EC 3.1.1.71; alkylacetylglycerol acetylhydrolase. Cat No: EXWM-3499. | |
| acyl-CoA 11-(Z)-desaturase | The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0), that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0), while that from the moth Spodoptera littoralis accepts both substrates. The enzyme contains three histidine boxes that are conserved in all desaturases. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase. Group: Enzymes. Synonyms: Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11. Enzyme Commission Number: EC 1.14.19.5. 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-1013; acyl-CoA 11-(Z)-desaturase; EC 1.14.19.5; Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase; Δ11-fatty-acid desaturase. Cat No: EXWM-1013. | |
| alcohol dehydrogenase (quinone) | Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed propeller structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide. Group: Enzymes. Synonyms: type III ADH; membrane associated quinohaemoprotein alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.5.5. 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-0433; alcohol dehydrogenase (quinone); EC 1.1.5.5; type III ADH; membrane associated quinohaemoprotein alcohol dehydrogenase. Cat No: EXWM-0433. | |
| Alkaline phosphatase, Bovine intestine | Alkaline phosphatase, Bovine intestine (Apase) is a membrane-bound glycoprotein that catalyzes the hydrolysis of phosphate monoesters at alkaline pH. Alkaline phosphatase can be used in molecular biology and enzyme-free analysis. Inhibition of tissue nonspecific alkaline phosphatase can block intracellular lipid accumulation [1] [2]. Uses: Scientific research. Group: Natural products. Alternative Names: Apase. CAS No. 9001-78-9. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P2818. |  |
| ammonia monooxygenase | The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper, iron and possibly zinc. The enzymes require two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor. Group: Enzymes. Synonyms: AMO. Enzyme Commission Number: EC 1.14.99.39. 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-1050; ammonia monooxygenase; EC 1.14.99.39; AMO. Cat No: EXWM-1050. | |
| betaine-aldehyde dehydrogenase | In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Synonyms: betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Enzyme Commission Number: EC 1.2.1.8. CAS No. 9028-90-4. 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-1182; betaine-aldehyde dehydrogenase; EC 1.2.1.8; 9028-90-4; betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Cat No: EXWM-1182. | |
| biotin-dependent malonate decarboxylase | Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. The enzyme described here is a biotin-dependent, Na+-translocating enzyme that includes both soluble and membrane-bound components. The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88, biotin-independent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. Both enzymes achieve this by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-bound form of the enzyme. The ACP su...nyl-S-ACP:biotin-protein carboxyltransferase) and MadH (EC 6.2.1.35, ACP-SH:acetate ligase). Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein. The carboxy group is lost with retention of configuration. Group: Enzymes. Synonyms: malonate decarboxylase (with biotin); malonate decarboxylase (ambiguous). Enzyme Commission Number: EC 4.1.1.89. 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-4838; biotin-dependent malonate decarboxylase; EC 4.1.1.89; malonate decarboxylase (with biotin); malonate decarboxylase (ambiguous). Cat No: EXWM-4838. | |
| biotin-independent malonate decarboxylase | Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. This enzyme is a cytosolic protein that is biotin-independent. The other type is a biotin-dependent, Na+-translocating enzyme that includes both soluble and membrane-bound components (cf. EC 4.1.1.89, biotin-dependent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. In both enzymes, this is achieved by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-ACP. The ACP subunit of both enzyme...enzyme complex are EC 2.3.1.187 (acetyl-S-ACP:malonate ACP transferase), EC 2.3.1.39 ([acyl-carrier-protein] S-malonyltransferase) and EC 4.1.1.87 (malonyl-S-ACP decarboxylase). The carboxy group is lost with retention of configuration. Group: Enzymes. Synonyms: malonate decarboxylase (without biotin); malonate decarboxylase (ambiguous); MDC. Enzyme Commission Number: EC 4.1.1.88. 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-4837; biotin-independent malonate decarboxylase; EC 4.1.1.88; malonate decarboxylase (without biotin); malonate decarboxylase (ambiguous); MDC. Cat No: EXWM-4837. | |
| carboxypeptidase E | A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Enzyme Commission Number: EC 3.4.17.10. CAS No. 81876-95-1. 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-4062; carboxypeptidase E; EC 3.4.17.10; 81876-95-1; carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Cat No: EXWM-4062. | |
| carboxypeptidase M | A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: CPM. Enzyme Commission Number: EC 3.4.17.12. CAS No. 120038-28-0. 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-4064; carboxypeptidase M; EC 3.4.17.12; 120038-28-0; CPM. Cat No: EXWM-4064. | |
| catechol O-methyltransferase | The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols. Group: Enzymes. Synonyms: COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. 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-1961; catechol O-methyltransferase; EC 2.1.1.6; 9012-25-3; COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Cat No: EXWM-1961. | |
| cholate-CoA ligase | Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway. Group: Enzymes. Synonyms: BAL; bile acid CoA ligase; bile acid co. Enzyme Commission Number: EC 6.2.1.7. CAS No. 9027-90-1. 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-5709; cholate-CoA ligase; EC 6.2.1.7; 9027-90-1; BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase. Cat No: EXWM-5709. | |
| choline dehydrogenase | A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. Group: Enzymes. Synonyms: choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase. Enzyme Commission Number: EC 1.1.99.1. CAS No. 9028-67-5. 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-0443; choline dehydrogenase; EC 1.1.99.1; 9028-67-5; choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase. Cat No: EXWM-0443. | |
| choline monooxygenase | The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 1.14.15.7. CAS No. 118390-76-4. 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-0950; choline monooxygenase; EC 1.14.15.7; 118390-76-4. Cat No: EXWM-0950. | |
| choline oxidase | A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes. Group: Enzymes. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. 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-0399; choline oxidase; EC 1.1.3.17; 9028-67-5. Cat No: EXWM-0399. | |
| Creatine Kinase BB Fraction Human, Recombinant | Brain-type creatine kinase also known as CK-BB is a creatine kinase that in humans is encoded by the CKB gene. The protein encoded by this gene, CK-BB, consists of a homodimer of two identical brain-type CK-B subunits. BB-CK is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. > 90% (sds-page), liquid, recombinant, expressed in pichia pastoris. Applications: Human creatine kinase bb fraction has been used to investigate the survival benefit of the late percutaneous coronary intervention in patients after acute myocardial infarction. human creatine kinase bb fraction has also been used in a study to analyze protein oxidations and resultant loss of function. Group: Enzymes. Synonyms: CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Purity: > 90% (SDS-PAGE). CK. Stability: -70°C. Form: liquid. Source: Pichia pastoris. Species: Human. CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Cat No: NATE-0139. | |
| Cytochrome P450 Reductase from Human, Recombinant | Cytochrome P450 reductase is a membrane bound enzyme required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. The cytochrome P450 enzyme system is mainly involved in the detoxification of xenobiotics in the liver. It also participates in the activation of procarcinogens and the metabolism of endogeneous substrates such as steroids. Applications: Human cytochrome p450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat. human cytochrome p450 reductase has also been u...AD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-3-4. Purity: >90% (SDS-PAGE). CPR. Mole weight: 76.5 kDa. Activity: >30 U/mg. Storage: Store at -70°C. Form: Supplied in a solution containing 10 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.5 mM DTT, 20% (v/v) glycerol. Source: Baculovirus infected insect cells. Species: Human. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-1586. | |
| D-3-HYDROXYBUTYRATE DEHYDROGENASE | D-3-HYDROXYBUTYRATE DEHYDROGENASE. Synonyms: D-3-HYDROXYBUTYRATE: NAD OXIDOREDUCTASE;BETA-HYDROXYBUTYRATE DEHYDROGENASE;BETA-HYDROXYBUTYRATE DEHYDROGENASE TYPE V;3-HBDH;3-HYDROXYBUTYRATE DEHYDROGENASE;(R)-3-HYDROXYBUTANOATE: NAD+ OXIDOREDUCTASE;[R]-3-HYDROXYBUTANOATE: NAD+ OXIDOREDUCTASE TYPE V;B-HYDROXYBUTYRATE DEHYDROGENASE TYPE IV FROM PSEUDO. CAS No. 9028-38-0. Pack Sizes: 1 kg. Product ID: CDF4-0049. Molecular formula: NULL. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; D-3-HYDROXYBUTYRATE DEHYDROGENASE; CDF4-0049; 9028-38-0; 232-830-6; 9028-38-0. Purity: 0.99. EC Number: 232-830-6. Physical State: Lyophilized Powder. Storage: -20°C. Product Description: D-β-hydroxybutyrate dehydrogenase (BDH) is a membrane bound lipid-requiring enzyme. |  |
| Δ7-sterol 5(6)-desaturase | This enzyme, found in eukaryotic organisms, catalyses the introduction of a double bond between the C5 and C6 carbons of the B ring of Δ7-sterols, to yield the corresponding Δ5,7-sterols. The enzymes from yeast, plants and vertebrates act on avenasterol, episterol, and lathosterol, respectively. The enzyme is located at the endoplasmic reticulum and is membrane bound. Group: Enzymes. Synonyms: lathosterol oxidase; Δ7-sterol Δ5-dehydrogenase; Δ7-sterol 5-desaturase; Δ7-sterol-C5(6)-desaturase; 5-DES; SC5DL (gene name); ERG3 (gene name). Enzyme Commission Number: EC 1.14.19.20. CAS No. 37255-37-1. 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-0983; Δ7-sterol 5(6)-desaturase; EC 1.14.19.20; 37255-37-1; lathosterol oxidase; Δ7-sterol Δ5-dehydrogenase; Δ7-sterol 5-desaturase; Δ7-sterol-C5(6)-desaturase; 5-DES; SC5DL (gene name); ERG3 (gene name). Cat No: EXWM-0983. | |
| dihydroorotate dehydrogenase (fumarate) | Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. Group: Enzymes. Synonyms: DHOdehase (ambiguous); dihydroorotate dehydrogenase (ambiguous); dihydoorotic acid dehydrogenase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyr4 (gene name). Enzyme Commission Number: EC 1.3.98.1. CAS No. 9029-3-2. 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-1417; dihydroorotate dehydrogenase (fumarate); EC 1.3.98.1; 9029-03-2; DHOdehase (ambiguous); dihydroorotate dehydrogenase (ambiguous); dihydoorotic acid dehydrogenase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyr4 (gene name). Cat No: EXWM-1417. | |
| dihydroorotate dehydrogenase (NAD+) | Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. Group: Enzymes. Synonyms: orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name). Enzyme Commission Number: EC 1.3.1.14. CAS No. 37255-26-8. 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-1288; dihydroorotate dehydrogenase (NAD+); EC 1.3.1.14; 37255-26-8; orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name). Cat No: EXWM-1288. | |
| dihydroorotate dehydrogenase (NADP+) | Binds FMN and FAD. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NAD+ (EC 1.3.1.14) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. Group: Enzymes. Synonyms: orotate reductase; dihydro-orotic dehydrogenase; L-5,6-dihydro-orotate:NAD+ oxidoreductase; orotate reductase (NADPH). Enzyme Commission Number: EC 1.3.1.15. CAS No. 37255-27-9. 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-1289; dihydroorotate dehydrogenase (NADP+); EC 1.3.1.15; 37255-27-9; orotate reductase; dihydro-orotic dehydrogenase; L-5,6-dihydro-orotate:NAD+ oxidoreductase; orotate reductase (NADPH). Cat No: EXWM-1289. | |
| ferric-chelate reductase (NADH) | Contains FAD. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The plant enzyme is involved in the transport of iron across plant plasma membranes. The enzyme from the bacterium Paracoccus denitrificans can also reduce chromate. cf. EC 1.16.1.9, ferric-chelate reductase (NADPH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H]. Group: Enzymes. Synonyms: ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADH:Fe3+-EDTA reductase; NADH2:Fe3+ oxidoreductase; ferB (gene name); Fe(II):NAD+ oxidoreductase. Enzyme Commission Number: EC 1.16.1.7. CAS No. 120720-17-4. 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-1072; ferric-chelate reductase (NADH); EC 1.16.1.7; 120720-17-4; ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADH:Fe3+-EDTA reductase; NADH2:Fe3+ oxidoreductase; ferB (gene name); Fe(II):NAD+ oxidoreductase. Cat No: EXWM-1072. | |
| GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-&alph. Enzyme Commission Number: EC 2.4.1.132. CAS No. 81181-76-2. 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-2357; GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase; EC 2.4.1.132; 81181-76-2; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase. Cat No: EXWM-2357. | |
| GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1?4)-β-D-GlcNAc-(1?4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransfera. Enzyme Commission Number: EC 2.4.1.257. 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-2487; GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase; EC 2.4.1.257; GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1?3)-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase. Cat No: EXWM-2487. | |
| GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1?2) linkages to the nascent oligosaccharide. Group: Enzymes. Synonyms: ALG11; AL. Enzyme Commission Number: EC 2.4.1.131. CAS No. 74506-43-7. 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-2356; GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase; EC 2.4.1.131; 74506-43-7; ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man3GlcNAc2-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1?3)-[D-Man-α-(1?6)]-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase. Cat No: EXWM-2356. | |
| glucose 1-dehydrogenase (PQQ, quinone) | Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed propeller structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses. Group: Enzymes. Synonyms: quinoprotein glucose dehydrogenase; membrane-bound glucose dehydrogenase; mGDH; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase. Enzyme Commission Number: EC 1.1.5.2. CAS No. 81669-60-5. Glucose Dehyrogenase. 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-0430; glucose 1-dehydrogenase (PQQ, quinone); EC 1.1.5.2; 81669-60-5; quinoprotein glucose dehydrogenase; membrane-bound glucose dehydrogenase; mGDH; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase. Cat No: EXWM-0430. | |
| glutamate carboxypeptidase II | A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa, but also exists in a soluble form. Hydrolyses α-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also γ-glutamyl bonds in γ-Glu-Glu, and folylpoly-γ-glutamates. With folylpoly-γ-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate. Does not hydrolyse Ac-β-Asp-Glu. Known inhibitors: quisqualic acid, Ac-β-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. The release of C-terminal glutamate from folylpoly-γ-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (γ-Glu-X carboxypeptidase). Group: Enzymes. Synonyms: N-acetylated-γ-linked-acidic dipeptidase (NAALADas. Enzyme Commission Number: EC 3.4.17.21. CAS No. 9074-87-7. 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-4074; glutamate carboxypeptidase II; EC 3.4.17.21; 9074-87-7; N-acetylated-γ-linked-acidic dipeptidase (NAALADase); folate hydrolase; prostate-specific membrane antigen; pteroylpoly-γ-glutamate carboxypeptidase; microsomal γ-glutamyl carboxypeptidase; pteroylpolyglutamate hydrolase; folylpolyglutamate h | |
| glutamyl aminopeptidase | Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Enzyme Commission Number: EC 3.4.11.7. CAS No. 9074-83-3. 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-4028; glutamyl aminopeptidase; EC 3.4.11.7; 9074-83-3; aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Cat No: EXWM-4028. | |
| glycerol-3-phosphate dehydrogenase | This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain.This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9. The enzyme is activated by calcium. Group: Enzymes. Synonyms: α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenas | |
| glycine dehydrogenase (cyanide-forming) | The enzyme from Pseudomonas sp. contains FAD. The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain. The enzyme can act with various artificial electron acceptors, including phenazine methosulfate. Group: Enzymes. Synonyms: hydrogen cyanide synthase; HCN synthase. Enzyme Commission Number: EC 1.4.99.5. 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-1491; glycine dehydrogenase (cyanide-forming); EC 1.4.99.5; hydrogen cyanide synthase; HCN synthase. Cat No: EXWM-1491. | |
| hepsin | This type-II membrane-associated serine peptidase has been implicated in cell growth and development. The enzyme has been shown to activate blood coagulation factor VII by cleavage of the Arg152?Ile153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation. There is no cleavage after aromatic or aliphatic residues. The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphaticresidue. The nature of the residue at S3 also affects hydrolysis, with Gln being much more favourable than Ala. Belongs in peptidase family S1A. Group: Enzymes. Enzyme Commission Number: EC 3.4.21.106. CAS No. 112398-23-9. 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-4101; hepsin; EC 3.4.21.106; 112398-23-9. Cat No: EXWM-4101. | |
| Hyaluronan synthase from Pasteurella multocida, Recombinant | Hyaluronan synthases (HAS) are membrane-bound enzymes which use UDP-α-N-acetyl-D-glucosamine and UDP-α-D-glucuronate as substrates to produce the glycosaminoglycan hyaluronan at the cell surface and extrude it through the membrane into the extracellular space. Group: Enzymes. Synonyms: EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Enzyme Commission Number: EC 2.4.1.212. CAS No. 39346-43-5. Purity: min 95% by SDS-PAGE. Hyaluronan synthase. Source: E. coli. Species: Pasteurella multocida. EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Cat No: NATE-1485. | |
| hydrogen:quinone oxidoreductase | Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen). Group: Enzymes. Synonyms: hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase. Enzyme Commission Number: EC 1.12.5.1. CAS No. 151616-65-8. 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-0522; hydrogen:quinone oxidoreductase; EC 1.12.5.1; 151616-65-8; hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase. Cat No: EXWM-0522. | |
| leachianone-G 2''-dimethylallyltransferase | This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a dimethylallyl group to the 2'' position of another dimethylallyl group attached at postiion 8 of leachianone G. The enzyme is specific for dimethylallyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. Group: Enzymes. Synonyms: LG 2''-dimethylallyltransferase; leachianone G 2''-dimethylallyltransferase; LGDT. Enzyme Commission Number: EC 2.5.1.71. 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-2809; leachianone-G 2''-dimethylallyltransferase; EC 2.5.1.71; LG 2''-dimethylallyltransferase; leachianone G 2''-dimethylallyltransferase; LGDT. Cat No: EXWM-2809. | |
| leishmanolysin | A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100?Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8. Group: Enzymes. Synonyms: promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Enzyme Commission Number: EC 3.4.24.36. CAS No. 161052-06-8. 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-4318; leishmanolysin; EC 3.4.24.36; 161052-06-8; promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Cat No: EXWM-4318. | |
| L-sorbose 1-dehydrogenase | The product, L-sorbosone, is an intermediate in bacterial 2-keto-L-gulonic-acid formation. The activity of this membrane-bound enzyme is stimulated by Fe(III) or Co2+ but is inhibited by Cu2+. The enzyme is highly specific for L-sorboseas other sugars, such as glucose, mannitol and sorbitol, are not substrates. Phenazine methosulfate and DCIP can act as artificial acceptors. Group: Enzymes. Synonyms: SDH. Enzyme Commission Number: EC 1.1.99.32. 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-0461; L-sorbose 1-dehydrogenase; EC 1.1.99.32; SDH. Cat No: EXWM-0461. | |
| membrane alanyl aminopeptidase | A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1. Group: Enzymes. Synonyms: microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. 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-4016; membrane alanyl aminopeptidase; EC 3.4.11.2; 9054-63-1; microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Cat No: EXWM-4016. | |
| membrane dipeptidase | A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19. Group: Enzymes. Synonyms: renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Enzyme Commission Number: EC 3.4.13.19. CAS No. 9031-99-6. 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-4033; membrane dipeptidase; EC 3.4.13.19; 9031-99-6; renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Cat No: EXWM-4033. | |
| meprin A | A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 3.4.24.11 (astacin family). Formerly included in EC 3.4.24.11. Group: Enzymes. Synonyms: endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH. Enzyme Commission Number: EC 3.4.24.18. CAS No. 148938-24-3. 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-4299; meprin A; EC 3.4.24.18; 148938-24-3; endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH. Cat No: EXWM-4299. | |
| meprin B | A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin β subunits (in contrast to meprin A, which contains both α and β subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: meprin-b. Enzyme Commission Number: EC 3.4.24.63. CAS No. 150679-52-0. 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-4346; meprin B; EC 3.4.24.63; 150679-52-0; meprin-b. Cat No: EXWM-4346. | |
| methane monooxygenase (particulate) | Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25). Group: Enzymes. Enzyme Commission Number: EC 1.14.18.3. 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-0965; methane monooxygenase (particulate); EC 1.14.18.3. Cat No: EXWM-0965. | |
| Methionine Aminopeptidase from Pyrococcus furiosus, Recombinant | Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the following chemical reaction:Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. This membrane-bound enzyme is present in both prokaryotes and eukaryotes. X-ray crystallography of the structure of methionine aminopeptidase from pyrococcus furiosus or pfmap was performed at a resolution of 1.75a and showed that the protein consists of a catalytic domain containing two cobalt ions in the active site and a unique insertion domain which is specific to the prokaryotic form of...o the methionyl aminopeptidases from escherichia coli and pyrococcus furiosus. it has also been used in a study to examine the binding of a new class of pseudopeptide analog inhibitors. Group: Enzymes. Synonyms: Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Enzyme Commission Number: EC 3.4.11.18. CAS No. 9025-42-7. MAP. Storage: -20°C. Form: Solution containing 0.01% Tween 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Pyrococcus furiosus. Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Cat No: NATE-0442. | |
| methionyl aminopeptidase | This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). Group: Enzymes. Synonyms: methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Enzyme Commission Number: EC 3.4.11.18. CAS No. 61229-81-0. MAP. 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-4014; methionyl aminopeptidase; EC 3.4.11.18; 61229-81-0; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Cat No: EXWM-4014. | |
| Monoamine Oxidase (Crude Enzyme) | L-Monoamine oxidases (MAO) are a family of enzymes that catalyze the oxidation of monoamines. They are found bound to the outer membrane of mitochondria in most cell types in the body. The enzyme was originally discovered by Mary Bernheim in the liver and was named tyramine oxidase. They belong to the protein family of flavin-containing amine oxidoreductases. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; drug development; analysis; medicine. Group: Enzymes. Synonyms: equilase; caperase; optidase; catalase-peroxidase; CAT. Enzyme Commission Number: EC 1.4.3.4. CAS No. 9001-66-5. Monoamine Oxidase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. equilase; caperase; optidase; catalase-peroxidase; CAT. Pack: 100ml. Cat No: NATE-1808. | |
| naringenin 8-dimethylallyltransferase | Requires Mg2+. This membrane-bound protein is located in the plastids. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.71 (leachianone G 2''-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. Group: Enzymes. Synonyms: N8DT. Enzyme Commission Number: EC 2.5.1.70. 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-2808; naringenin 8-dimethylallyltransferase; EC 2.5.1.70; N8DT. Cat No: EXWM-2808. | |
| Native Bovine α-Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748. | |
| 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 Bovine Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Group: Zymogens. Synonyms: chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. CAS No. 9035-75-0. Purity: Purified, Five times crystallized, electrophoretically homogeneous. Chymotrypsinogen A. Activity: Activates to at least 45 units per mg protein. Stability: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bovine Pancreas. Species: Bovine. chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. Cat No: NATE-0134. | |
| Native Bovine Phosphodiesterase II | Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. The enzyme acts on poly (A), poly (U), and poly (I). Native DNA and poly (C) are quite resistant to the action of this enzyme. Hydrolyzes RNA, RNA-Core, 3'-alkyl-and 3'-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3'-phosphate end groups to 3'-mononucleotides. Polynucleotides having 5'-phosphomonoester end groups are not attacked. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. phosphodiesterase ii has been used in t...yloxobutyl (pob) base adducts from dna. furthermore, it has been used along with micr oc occal endonuclease to hydrolyze purified dna to 3-nucleoside monophosphates. Group: Enzymes. Synonyms: 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Enzyme Commission Number: EC 3.1.16.1. CAS No. 9068-54-6. PDE. Activity: > 5.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine spleen. Species: Bovine. 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Cat No: NATE-0518. | |
| Native Crotalus atrox (Western Diamondback Rattlesnake) Phosphodiesterase I | Phosphodiesterase I breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. phosphodiesterase i from western diamondback rattlesnake, is used in phosphodiesterase activation assays for calmodulin. it is added to hydrolyze amp. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodi. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 0.01 unit/mg solid. Storage: -20°C. Form: crude dried venom. Source: Crotalus atrox (Western Diamondback Rattlesnake). Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0513. | |
| Native Gluconobacter industrius D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. fructose dehydrogenase (fdh) is used in a numb...he bio-industry. a direct electron transfer reaction of d-fructose dehydrogenase adsorbed on a porous carbon electrode surface has been used to describe a batch-type coulometric d-fructose biosensor. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Activity: 400-1,200 units/mg. Storage: -20°C. Form: Lyophilized powder. Source: Gluconobacter industrius. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0184. | |
| Native Gluconobacter sp. D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. this enzyme is also used in a number of basic res...tic determination of d-fructose in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Mole weight: mol wt ~140 kDa. Activity: > 20 units/mg solid; 400-1,200 units/mg protein. Storage: -20°C. Form: lyophilized powder. supplied as a lyophilized powder containing approx 80% stabilizers, sugars, amino acids and BSA. Source: Gluconobacter sp. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0185. | |
| Native Porcine Catechol-O-methyl Transferase | Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines such as dopamine, epinephrine, and norepinephrine. In Humans, catechol-O-methyltransferase protein is encoded by the COMT gene. As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines. COMT was first discovered by the biochemist Julius Axelrod in 1957. Group: Enzymes. Synonyms: catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Py. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. Activity: > 150 units/mg protein. Form: Lyophilized powder containing phosphate buffer and dithiothreitol. Source: Porcine liver. Species: Porcine. catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Pyrocatechol-O-methyl Transferase; S-Adenosyl-L-methionine:catechol O-methyltransferase. Cat No: NATE-0148. | |
| neprilysin | A membrane-bound glycoprotein widely distributed in animal tissues. Inhibited by phosphoramidon and thiorphan. Common acute lymphoblastic leukemia antigen (CALLA). Type example of peptidase family M13. Group: Enzymes. Synonyms: neutral endopeptidase; endopeptidase 24.11; kidney-brush-border neutral peptidase; enkephalinase (misleading); endopeptidase-2; CALLA (common acute lymphoblastic leukemia-associated) antigens; CALLA antigen; endopeptidase; membrane metallo. Enzyme Commission Number: EC 3.4.24.11. CAS No. 82707-54-8. 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-4292; neprilysin; EC 3.4.24.11; 82707-54-8; neutral endopeptidase; endopeptidase 24.11; kidney-brush-border neutral peptidase; enkephalinase (misleading); endopeptidase-2; CALLA (common acute lymphoblastic leukemia-associated) antigens; CALLA antigen; endopeptidase; membrane metalloendopeptidase; kidney-brush-border neutral endopeptidase; kidney-brush-border neutral proteinase; endopeptidase-2; CALLA glycoprotein; CALLA; common acute lymphoblastic leukemia antigen; CALLA glycoproteins; common acute lymphoblastic leukemia-associated antigens; neutral metallendopeptidase; membrane metalloendopeptidase; NEP; neutral endopeptidase 24.11; CD10; neutral endopeptidase; acute lymphoblastic leukemia antigen. Cat No: EXWM-4292. | |
| NiFe-type cytoplasmic hydrogenase from Pyrococcus furiosus, recombinant | The [NiFe] hydrogenases contain a minimum of two subunits known as the small (S) and large (L) subunits. The small subunit contains three iron-sulfur clusters while the large subunit contains the active site, a nickel-iron center which is connected to the solvent by a molecular tunnel. To date, periplasmic, cytoplasmic, and membrane-bound hydrogenases have been found. [NiFe] hydrogenases are known to be deactivated by molecular oxygen (O2). The [NiFe] hydrogenase of Pyrococcus furiosus is heterotetrameric wherein the additional two subunits allow the enzyme to use NAD(P)(H) as an electron carrier. Group: Enzymes. Synonyms: Cytoplasmic [NiFe]-Hydrogenase; OE-SHI; Cytoplasmic Hydrogenase; NiFe-type cytoplas. Purity: > 90% by SDS-PAGE. Cytoplasmic hydrogenase. Mole weight: Predicted: 155 kDa, Size Exclusion: 149 kDa +/- 5 kDa. Activity: >100 U/mL. Storage: This item is oxygen sensitive. Stable when stored sealed in strictly anaerobic environment (<10 ppm O2) at room temperature for up to 6 months. For long-term storage, protein can be flash frozen in nitrogen and stored at -80°C. Form: Liquid. Source: Pyrococcus furiosus. Cytoplasmic [NiFe]-Hydrogenase; OE-SHI; Cytoplasmic Hydrogenase; NiFe-type cytoplasmic hydrogenase; SHI; [NiFe] hydrogenase; NADP-specific NiFe-type cytoplasmic hydrogenase. Cat No: NATE-1691. | |
| nitrate reductase (quinone) | A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits. Group: Enzymes. Synonyms: nitrate reductase A; nitrate reductase Z; quinol/nitrate oxidoreductase; quinol-nitrate oxidoreductase; quinol:nitrate oxidoreductase; NarA; NarZ; NarGHI; dissimilatory nitrate reductase. Enzyme Commission Number: EC 1.7.5.1. 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-1629; nitrate reductase (quinone); EC 1.7.5.1; nitrate reductase A; nitrate reductase Z; quinol/nitrate oxidoreductase; quinol-nitrate oxidoreductase; quinol:nitrate oxidoreductase; NarA; NarZ; NarGHI; dissimilatory nitrate reductase. Cat No: EXWM-1629. | |
| Nonyl b-D-thiomaltopyranoside | Nonyl b-D-thiomaltopyranoside is a valuable compound widely used industry. It acts as a nonionic detergent and is utilized in various biochemical studies, including the isolation and purification of proteins and membrane-bound enzymes. Synonyms: n-Nonyl-b-D-thiomaltoside. CAS No. 148565-55-3. Molecular formula: C21H40O10S. Mole weight: 484.6. |  |
| Octyl a-L-rhamnopyranoside | Octyl a-L-rhamnopyranoside is a highly bioactive compound widely employed in the biomedical sector, serving as an indispensable nonionic detergent that possesses substantial value in the solubilization,olation and purification processes of diverse proteins and membrane-bound enzymes. | |
| P1,P5-Di(adenosine-5')pentaphosphate trilithium salt | A diadenosine polyphosphate stored in secretory granules of thrombocytes, chromaffin and neuronal cells. After release into the extracellular space, it affects a variety of biological activities in a wide range of target tissues. In the nervous system it acts through various purinergic receptors. It also activates 5?-nucleotidase and inhibits adenosine kinase activity in vitro. Ap5A is metabolized by soluble enzymes in the blood plasma and by membrane-bound ectoenzymes of a number of cell types including endothelial and smooth muscle cells. In cardiac muscle, pM to nM concentrations significantly increase the open-probability of ryanodine-receptor (RyR2) gates, with prolonged action due to slow dissociation from the receptor. Group: Biochemicals. Alternative Names: P1,P5-Di(adenosine-5) pentaphosphate pentalithium salt, 94108-02-8, A(5)P5(5)A, AC1O4WDE, D6392_SIGMA, CTK8G2238, EINECS 302-339-2, AP5A lithium salt P1,P5-Di(adenosine-5) pentaphosphate pentalithium salt, AG-H-86941, Diadenosine pentaphosphate trilithium salt, Diadenosine pentaphosphate pentalithium salt, K00187, A(5 inverted exclamation marka)P5(5 inverted exclamation marka)A trilithium sal. Grades: Highly Purified. CAS No. 75522-97-3. Pack Sizes: 25mg, 50mg, 100mg, 250mg. Molecular Formula: C20H26N10O22P5Li3, Molecular Weight: 934.17. US Biological Life Sciences. |  Worldwide |
| peptidyl-dipeptidase A | A Cl--dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Type example of peptidase family M2. Group: Enzymes. Synonyms: dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase (ambiguous); peptidyl dipeptidase; angiotensin converting enzym. Enzyme Commission Number: EC 3.4.15.1. CAS No. 9015-82-1. Angiotensin Converting Enzyme. 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-4053; peptidyl-dipeptidase A; EC 3.4.15.1; 9015-82-1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase (ambiguous); peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; ACE; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat No: EXWM-4053. | |
| peptidyl-dipeptidase B | A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence and shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II. Group: Enzymes. Synonyms: dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase. Enzyme Commission Number: EC 3.4.15.4. CAS No. 147014-93-5. 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-4054; peptidyl-dipeptidase B; EC 3.4.15.4; 147014-93-5; dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase. Cat No: EXWM-4054. | |
| phenylacetyl-CoA dehydrogenase | The enzyme from Thauera aromatica is a membrane-bound molybdenum-iron-sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone. A second enzyme, EC 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate. Group: Enzymes. Synonyms: phenylacetyl-CoA:acceptor oxidoreductase. Enzyme Commission Number: EC 1.17.5.1. CAS No. 210756-43-7. 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-1094; phenylacetyl-CoA dehydrogenase; EC 1.17.5.1; 210756-43-7; phenylacetyl-CoA:acceptor oxidoreductase. Cat No: EXWM-1094. | |
| plant seed peroxygenase | A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin. Group: Enzymes. Synonyms: plant peroxygenase, soybean peroxygenase. Enzyme Commission Number: EC 1.11.2.3. 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-0514; plant seed peroxygenase; EC 1.11.2.3; plant peroxygenase, soybean peroxygenase. Cat No: EXWM-0514. | |
| pro-opiomelanocortin converting enzyme | A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle. Group: Enzymes. Synonyms: prohormone converting enzyme; pro-opiomelanocortin-converting enzyme; proopiomelanocortin proteinase; PCE. Enzyme Commission Number: EC 3.4.23.17. CAS No. 80891-34-5. 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-4254; pro-opiomelanocortin converting enzyme; EC 3.4.23.17; 80891-34-5; prohormone converting enzyme; pro-opiomelanocortin-converting enzyme; proopiomelanocortin proteinase; PCE. Cat No: EXWM-4254. | |
| protein geranylgeranyltransferase type II | This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type I (EC 2.5.1.59), constitutes the protein prenyltransferase family of enzymes. Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion. Group: Enzymes. Synonyms: GGTaseII; Rab geranylgeranyltransferase; RabGGTase; geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-cysteine geranyltransferase. Enzyme Commission Number: EC 2.5.1.60. CAS No. 135371-29-8. 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-2798; protein geranylgeranyltransferase type II; EC 2.5.1.60; 135371-29-8; GGTaseII; Rab geranylgeranyltransferase; RabGGTase; geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-cysteine geranyltransferase. Cat No: EXWM-2798. | |
| proton-translocating NAD(P)+ transhydrogenase | The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme. Group: Enzymes. Synonyms: pntA (gene name); pntB (gene name); NNT (gene name). Enzyme Commission Number: EC 7.1.1.1 (Formerly EC 1.6.1.5). 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-1578; proton-translocating NAD(P)+ transhydrogenase; EC 1.6.1.5; pntA (gene name); pntB (gene name); NNT (gene name). Cat No: EXWM-1578. | |
| quinate dehydrogenase (quinone) | The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. Group: Enzymes. Synonyms: NAD(P)+-independent quinate dehydrogenase; quinate:pyrroloquinoline-quinone 5-oxidoreductase. Enzyme Commission Number: EC 1.1.5.8. CAS No. 115299-99-5. 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-0436; quinate dehydrogenase (quinone); EC 1.1.5.8; 115299-99-5; NAD(P)+-independent quinate dehydrogenase; quinate:pyrroloquinoline-quinone 5-oxidoreductase. Cat No: EXWM-0436. | |
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