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| Product | Description | |
|---|---|---|
| 18S rRNA (guanine1575-N7)-methyltransferase | The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: 18S rRNA methylase Bud23; BUD23 (gene name). Enzyme Commission Number: EC 2.1.1.309. 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-1917; 18S rRNA (guanine1575-N7)-methyltransferase; EC 2.1.1.309; 18S rRNA methylase Bud23; BUD23 (gene name). Cat No: EXWM-1917. |  |
| 25S rRNA (cytosine2278-C5)-methyltransferase | The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: RCM1 (gene name). Enzyme Commission Number: EC 2.1.1.311. 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-1919; 25S rRNA (cytosine2278-C5)-methyltransferase; EC 2.1.1.311; RCM1 (gene name). Cat No: EXWM-1919. | |
| 25S rRNA (cytosine2870-C5)-methyltransferase | The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: NOP2 (gene name). Enzyme Commission Number: EC 2.1.1.310. 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-1918; 25S rRNA (cytosine2870-C5)-methyltransferase; EC 2.1.1.310; NOP2 (gene name). Cat No: EXWM-1918. | |
| adenylyl-sulfate reductase (glutathione) | This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis. Group: Enzymes. Synonyms: 5'-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming); plant-type 5'-adenylylsulfate reductase. Enzyme Commission Number: EC 1.8.4.9. CAS No. 355840-27-6. 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-1675; adenylyl-sulfate reductase (glutathione); EC 1.8.4.9; 355840-27-6; 5'-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming); plant-type 5'-adenylylsulfate reductase. Cat No: EXWM-1675. | |
| ADP-dependent NAD(P)H-hydrate dehydratase | Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers. The enzyme from bacteria consists of two domains, one of which acts as an NAD(P)H-hydrate epimerase that interconverts the two isomers to a 60:40 ratio (cf. EC 5.1.99.6), while the other catalyses the dehydration. Hence the enzyme can restore the complete mixture of isomers into NAD(P)H. The enzyme has no activity with ATP, contrary to the enzyme from eukaryotes (cf. EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase). Group: Enzymes. Synonyms: (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ADP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ADP-hydrolysing; NADH-forming). Enzyme Commission Number: EC 4.2.1.136. 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-4977; ADP-dependent NAD(P)H-hydrate dehydratase; EC 4.2.1.136; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ADP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ADP-hydrolysing; NADH-forming). Cat No: EXWM-4977. | |
| Alanine Racemase (Crude Enzyme) | This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. This enzyme participates in alanine and aspartatemetabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme. The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of all bacteria, including many which are harmful to humans. The enzyme is absent in higher eukaryotes but found everywhere in prokaryotes, making alanine racemase a great target for antimicrobial drug...udies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. Therefore, the alr gene is a feasible target for antimicrobial drugs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; pharmacology; medicine; pharmacology. Group: Enzymes. Synonyms: L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-alanine racemase. Pack: 100ml. Cat No: NATE-1854. | |
| Apyrase from Potato, Recombinant | Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis. Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM. Apyrase (recombinant, e. coli) is a highly active atp-diphosphohydrolase that catalyses the sequential hydrolysis of atp to adp and adp to amp releasing inorganic phosphate. it is a recombinant version of one of several isoforms of apyrase. it can also hydrol...version of 5? triphosphorylated rna to ligatable monophosphorylated form that can be used for 5? rna adaptor ligation. conversion of 5? triphosphorylated rna to 5? exonuclease xrn-1 sensitive monophosphorylated rna. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Apyrase. Mole weight: 47 kDa. Activity: 3,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM MES (pH 6.5 25°C), 0.1 mM CaCl2, 1 mM DTT, 0.1% Tween-20 and 50% glycerol. Source: E. coli. Species: Potato. ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Cat No: NATE-1268. | |
| ATP-dependent NAD(P)H-hydrate dehydratase | Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase). Group: Enzymes. Synonyms: reduced nicotinamide adenine dinucleotide hydrate dehydratase; ATP-dependent H4NAD(P)+OH dehydratase; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-. Enzyme Commission Number: EC 4.2.1.93. CAS No. 116669-08-0. 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-5077; ATP-dependent NAD(P)H-hydrate dehydratase; EC 4.2.1.93; 116669-08-0; reduced nicotinamide adenine dinucleotide hydrate dehydratase; ATP-dependent H4NAD(P)+OH dehydratase; (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing); (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming). Cat No: EXWM-5077. | |
| β-N-Acetylhexosaminidase from Xanthomonas manihotis, Recombinant | This enzyme releases non-reducing terminal β1-2, β1-3, β1-4 and β1-6 linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (<50 mU/ml) the enzyme can differentiate between GlcNAcβ1-2Man, GlcNAcβ1-4Man and GlcNAcβ1-6Man linkages. Under such conditions, the enzyme cleaves essentially only β1-2 linked GlcNAc, with two provisos. Firstly, β1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of tri-antennary oligosaccharides. Secondly, if the β-linked mannose of the ...cing β-n-acetylglucosamine residues from oligosaccharides. Applications: Biosynthesis of glycans in eukaryotes, glycoprotein production in various expression systems, protein digestion, removal of n-linked & o-linked glycans from glycoproteins, sequencing glycans. Group: Enzymes. Synonyms: β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β-N-Acetylhexosaminidase. Mole weight: 71000 daltons. Storage: 4°C, Avoid repeated freeze/thaw cycles. Source: E.coli. Species: Xanthomonas manihotis. β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-0934. | |
| coproporphyrinogen dehydrogenase | This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. It occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. This conversion, -?CH-CH2-COO- ? -CH=CH2 + CO2 + e- replaces the electron initially used. Group: Enzymes. Synonyms: oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase. Enzyme Commission Number: EC 1.3.98.3. 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-1418; coproporphyrinogen dehydrogenase; EC 1.3.98.3; oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase. Cat No: EXWM-1418. | |
| dihydroorotate dehydrogenase (quinone) | This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. Methyl-, ethyl-, tert-butyl and benzyl (S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. Group: Enzymes. Synonyms: dihydroorot. Enzyme Commission Number: EC 1.3.5.2. CAS No. 59088-23-2. 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-1386; dihydroorotate dehydrogenase (quinone); EC 1.3.5.2; 59088-23-2; dihydroorotate:ubiquinone oxidoreductase; (S)-dihydroorotate:(acceptor) oxidoreductase; (S)-dihydroorotate:acceptor oxidoreductase; DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); DHODH. Cat No: EXWM-1386. | |
| dolichyl-diphosphooligosaccharide-protein glycotransferase | Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram click here). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-aspa... oligopolysaccharidotransferase; STT3. Enzyme Commission Number: EC 2.4.99.18. CAS No. 75302-32-8. 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-2702; dolichyl-diphosphooligosaccharide-protein glycotransferase; EC 2.4.99.18; 75302-32-8; dolichyldiphosphooligosaccharide-protein glycosyltransferase; asparagine N-glycosyltransferase; dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase; dolichyl pyrophosphodiacetyl chitobiose-protein glycosyltransferase; oligomannosyltransferase; oligosaccharide transferase; dolichyldiphosphoryloligosaccharide-protein oligosaccharyl | |
| dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase | The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain. Group: Enzymes. Synonyms: AglC; UDP-Glc-2,3-diNAcA glycosyltransferase. Enzyme Commission Number: EC 2.4.1.335. 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-2573; dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase; EC 2.4.1.335; AglC; UDP-Glc-2,3-diNAcA glycosyltransferase. Cat No: EXWM-2573. | |
| dolichyl-phosphooligosaccharide-protein glycotransferase | The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC 2.4.99.18, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain. Group: Enzymes. Synonyms: AglB; archaeal oligosaccharyl transferase; dolichyl-monophosphooligosaccharide-protein glycotransferase. Enzyme Commission Number: EC 2.4.99.21. 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-2706; dolichyl-phosphooligosaccharide-protein glycotransferase; EC 2.4.99.21; AglB; archaeal oligosaccharyl transferase; dolichyl-monophosphooligosaccharide-protein glycotransferase. Cat No: EXWM-2706. | |
| glutamate formimidoyltransferase | A pyridoxal-phosphate protein. Also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity. Group: Enzymes. Synonyms: glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase. Enzyme Commission Number: EC 2.1.2.5. CAS No. 9032-83-1. 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-2007; glutamate formimidoyltransferase; EC 2.1.2.5; 9032-83-1; glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase. Cat No: EXWM-2007. | |
| 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 | |
| histone deacetylase | A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation. May be identical to EC 3.5.1.17, acyl-lysine deacylase. Group: Enzymes. Synonyms: HDAC. Enzyme Commission Number: EC 3.5.1.98. 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-4490; histone deacetylase; EC 3.5.1.98; HDAC. Cat No: EXWM-4490. | |
| hydroxysqualene dehydroxylase | This enzyme, isolated from the bacteria Rhodopseudomonas palustris and Zymomonas mobilis, participates, along with EC 2.5.1.103, presqualene diphosphate synthase, and EC 4.2.3.156, hydroxysqualene synthase, in the conversion of all-trans-farnesyl diphosphate to squalene. Eukaryotes achieve the same goal in a single step, catalysed by EC 2.5.1.21, squalene synthase. Group: Enzymes. Synonyms: hpnE (gene name). Enzyme Commission Number: EC 1.17.8.1. 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-1100; hydroxysqualene dehydroxylase; EC 1.17.8.1; hpnE (gene name). Cat No: EXWM-1100. | |
| hydroxysqualene synthase | This enzyme, isolated from the bacteria Rhodopseudomonas palustris and Zymomonas mobilis, participates, along with EC 2.5.1.103, presqualene diphosphate synthase, and EC 1.17.8.1, hydroxysqualene dehydroxylase, in the conversion of all-trans-farnesyl diphosphate to squalene. Eukaryotes achieve the same goal in a single step, catalysed by EC 2.5.1.21, squalene synthase. Group: Enzymes. Synonyms: hpnC (gene name). Enzyme Commission Number: EC 4.2.3.156. 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-5171; hydroxysqualene synthase; EC 4.2.3.156; hpnC (gene name). Cat No: EXWM-5171. | |
| isocitrate dehydrogenase (NAD+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NADP+ but much more slowly. Group: Enzymes. Synonyms: isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydr. Enzyme Commission Number: EC 1.1.1.41. CAS No. 9001-58-5. IDH. 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-0326; isocitrate dehydrogenase (NAD+); EC 1.1.1.41; 9001-58-5; isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydrogenase; NAD isocitric dehydrogenase; isocitrate dehydrogenase (NAD); IDH (ambiguous); nicotinamide adenine dinucleotide isocitrate dehydrogenase. Cat No: EXWM-0326. | |
| isocitrate dehydrogenase (NADP+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NAD+ but much more slowly. Group: Enzymes. Synonyms: ox. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. 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-0327; isocitrate dehydrogenase (NADP+); EC 1.1.1.42; 9028-48-2; oxalosuccinate decarboxylase; oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3. | |
| 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. | |
| mevalonate 3-kinase | Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea. Group: Enzymes. Synonyms: ATP:(R)-MVA 3-phosphotransferase. Enzyme Commission Number: EC 2.7.1.185. 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-3017; mevalonate 3-kinase; EC 2.7.1.185; ATP:(R)-MVA 3-phosphotransferase. Cat No: EXWM-3017. | |
| molybdopterin synthase | Catalyses the synthesis of molybdopterin from cyclic pyranopterin monophosphate. Two sulfur atoms are transferred to cyclic pyranopterin monophosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor. Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur-carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase. The reaction occurs in prokaryotes and eukaryotes. Group: Enzymes. Synonyms: MPT synthase. Enzyme Commission Number: EC 2.8.1.12. 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-3357; molybdopterin synthase; EC 2.8.1.12; MPT synthase. Cat No: EXWM-3357. | |
| Native Bovine Glutamate Dehydrogenase | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9001-46-1. GLDH. Mole weight: 260 kDa (gel). Activity: > 500U /mg protein. Appearance: White/off white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bovine liver. Species: Bovine. glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Cat No: DIA-146. | |
| Native Clostridium botulinum ADP-ribosyltransferase C3 | ADP-ribosyltransferase C3 from Clostridium botulinum ribosylates rho in eukaryotes in the presence of NAD. The ADP-ribosylating exoenzyme forms a single major 25 kDA (approx.) band with SDS electrophoresis. The enzyme labels 21-24 kDa proteins in tissues such as the human platelet membranes. Applications: Adp-ribosyltransferase c3 from clostridium botulinum may be used to study cellular signaling and g protein expression. Group: Enzymes. Synonyms: ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. CAS No. 58319-92-9. C3 Transferase. Storage: 2-8°C. Source: Clostridium botulinum. ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. Cat No: NATE-0095. | |
| Native Porcine Fumarase | Fumarase catalyzes the reversible hydration of fumarate to malate. In its mitochondrial form, fumarate is involved in the Krebs Cycle, while the cytosolic form is involved in amino acid metabolism. Fumarase (fh in human) is a well-known tricarboxylic-acid-cycle enzyme found in both the cytoplasm and mit ochondria of all eukaryotes. Applications: Fumarase is used as a protein calibration standard in the purification of intact dna polymerase a/primase from mouse cells. Group: Enzymes. Synonyms: EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Enzyme Commission Number: EC 4.2.1.2. CAS No. 9032-88-6. Fumarase. Activity: 300-500 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4, 0.05 M KH2PO4, pH 7.5, 0.014 M 2-mercaptoethanol. Source: Porcine heart. Species: Porcine. EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Cat No: NATE-0267. | |
| Native Potatoes Apyrase | Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis. Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM. Applications: At least two isoenzymes are found in different varieties of s. tuberosum:4,5 one with a high atpase/adpase ratio (~10) and another with a low ratio (~1). reaction: atp ? adp+pi ? amp+2pi.apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. for hydrolysis of organic di and triphosphates, the optimal ph is 6, and for inorganic substrates, the optimal ph is 5.1. apyrase, from creative enzymes, has been used in inhibition studies of platelet-aggregation. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase. Enzyme Commission Number: EC 3.6.1.5. CAS No. 9000-95-7. Apyrase. Activity: > 200 units/mg protein; > 600 units/mg protein. Storage: -20°C. Form: lyophilized powder. Partially purified, lyophilized powder containing potassium succinate buffer salts. Source: Potatoes. ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Cat No: NATE-0085. | |
| Native Rabbit Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Phosphoglucose isomerase (pgi) is an enzyme crucial for the interconversion of d-glucose 6-phosphate and d-fructose 6-phosphate. pgi is responsible for the second step of glycolysis and is involved in glucogenesis. it is highly conserved in bacteria and eukaryotes. it is used in sugar assays to convert fructose to glucose. this product is type xi and is from rabbit muscle. it is useful in enzyme systems requiring low sulfate. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder; Essentially sulfate-free powder containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0555. | |
| nicotinate-nucleotide diphosphorylase (carboxylating) | The reaction is catalysed in the opposite direction. Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD+ biosynthesis enzyme shared by both eukaryotes and prokaryotes. Group: Enzymes. Synonyms: quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase. Enzyme Commission Number: EC 2.4.2.19. CAS No. 37277-74-0. 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-2646; nicotinate-nucleotide diphosphorylase (carboxylating); EC 2.4.2.19; 37277-74-0; quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase. Cat No: EXWM-2646. | |
| nucleoside-triphosphate phosphatase | The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin. Group: Enzymes. Synonyms: nucleoside-triphosphatase; nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; unspecific diphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.15. CAS No. 9075-51-8. 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-4599; nucleoside-triphosphate phosphatase; EC 3.6.1.15; 9075-51-8; nucleoside-triphosphatase; nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; unspecific diphosphate phosphohydrolase. Cat No: EXWM-4599. | |
| orotate phosphoribosyltransferase | The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase. Group: Enzymes. Synonyms: orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase. Enzyme Commission Number: EC 2.4.2.10. CAS No. 9030-25-5. OPRTase. 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-2639; orotate phosphoribosyltransferase; EC 2.4.2.10; 9030-25-5; orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase. Cat No: EXWM-2639. | |
| orotidine-5'-phosphate decarboxylase | The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase. Group: Enzymes. Synonyms: orotidine-5'-monophosphate decarboxylase; orotodylate decarboxylase; orotidine phosphate decarboxylase; OMP decarboxylase; orotate monophosphate decarboxylase; orotidine monophosphate decarboxylase; orotidine phosphate decarboxylase; OMP-DC; orotate decarboxylase; orotidine 5'-phosphate decarboxylase; orotidylic decarboxylase; orotidylic acid decarboxylase; orotodylate decarboxylase; ODCase; orotic decarboxylase; orotidine-5'-phosphate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.23. CAS No. 9024-62-8. 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-4768; orotidine-5'-phosphate decarboxylase; EC 4.1.1.23; 9024-62-8; orotidine-5'-monophosphate decarboxylase; orotodylate decarboxylase; orotidine phosphate decarboxylase; OMP decarboxylase; orotate monophosphate decarboxylase; orotidine monophosphate decarboxylase; orotidine phosphate decarboxylase; OMP-DC; orotate decarboxylase; orotidine 5'-phosphate decarboxylase; orotidylic decarboxylase; orotidylic acid decarboxylase; orotodylate decarboxylase; ODCase; orotic decarboxylase; orotidine-5'-phosphate carboxy-lyase. Cat No: EXWM-4768. | |
| polyprenol reductase | The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length. Group: Enzymes. Synonyms: SRD5A3 (gene name); DFG10 (gene name). Enzyme Commission Number: EC 1.3.1.94. 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-1364; polyprenol reductase; EC 1.3.1.94; SRD5A3 (gene name); DFG10 (gene name). Cat No: EXWM-1364. | |
| protein O-GlcNAcase | Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins. Group: Enzymes. Synonyms: OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase. Enzyme Commission Number: EC 3.2.1.169. 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-3851; protein O-GlcNAcase; EC 3.2.1.169; OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase. Cat No: EXWM-3851. | |
| protein O-GlcNAc transferase | Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins. Group: Enzymes. Synonyms: O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase. Enzyme Commission Number: EC 2.4.1.255. 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-2485; protein O-GlcNAc transferase; EC 2.4.1.255; O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; protein O-linked β-N-acetylglucosamine transferase. Cat No: EXWM-2485. | |
| protein-synthesizing GTPase | This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs. Group: Enzymes. Synonyms: elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Enzyme Commission Number: EC 3.6.5.3. 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-4714; protein-synthesizing GTPase; EC 3.6.5.3; elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Cat No: EXWM-4714. | |
| quinol-cytochrome-c reductase | The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase). Group: Enzymes. Synonyms: ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitocho. Enzyme Commission Number: EC 1.10.2.2. CAS No. 9027-3-6. 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-0474; quinol-cytochrome-c reductase; EC 1.10.2.2; 9027-03-6; ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxido | |
| Ribonuclease H from Escherichia coli, Recombinant | Ribonuclease H (RNase H) is a family of non-sequence-specific endonucleases that catalyze the cleavage of RNA via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes. RNase Hs ribonuclease activity cleaves the 3-O-P bond of RNA in a DNA/RNA duplex substrate to produce 3-hydroxyl and 5-phosphate terminated products. In DNA replication, RNase H is responsible for removing the RNA primer, allowing completion of the newly synthesized DNA. Applications: Ribonuclease h from escherichia coli has been used in a study to assess metallobi ochemistry of the magnesium ion. ribonuclease h has also been used in a study to investigate selective inhibitors of hiv-1 reverse transcriptase ass ociated rnase h activity. Group: Enzymes. Synonyms: Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Enzyme Commission Number: EC 3.1.4.34. CAS No. 9050-76-4. Rnase. Activity: 1,000-4,000 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 20 mM Tris-HCl, pH 7.5, 100 mM KCl, 10 mM MgCl2, 0.1 mM EDTA, 0.1 mM DTT and 0.05 mg BSA per ml. Source: E. coli. Species: Escherichia coli. Ribonuclease H; RNase H; EC 3.1.4.34; 9050-76-4. Pack: vial of ~30 units. Cat No: NATE-0657. | |
| rRNA small subunit pseudouridine methyltransferase Nep1 | This enzyme, which occurs in both prokaryotes and eukaryotes, recognizes specific pseudouridine residues (ψ) in small subunits of ribosomal RNA based on the local RNA structure. It recognizes ψ914 in 16S rRNA from the archaeon Methanocaldococcus jannaschii, ψ1191 in yeast 18S rRNA, and ψ1248 in human 18S rRNA. Group: Enzymes. Synonyms: Nep1; nucleolar essential protein 1. Enzyme Commission Number: EC 2.1.1.260. 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-1865; rRNA small subunit pseudouridine methyltransferase Nep1; EC 2.1.1.260; Nep1; nucleolar essential protein 1. Cat No: EXWM-1865. | |
| succinate dehydrogenase | A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone). Group: Enzymes. Synonyms: succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Enzyme Commission Number: EC 1.3.5.1. CAS No. 9028-11-9. 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-1385; succinate dehydrogenase; EC 1.3.5.1; 9028-11-9; succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Cat No: EXWM-1385. | |
| superoxide dismutase | A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron. Group: Enzymes. Synonyms: superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein; hepatocuprein. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. 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-1063; superoxide dismutase; EC 1.15.1.1; 9054-89-1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein; hepatocuprein. Cat No: EXWM-1063. | |
| tRNA 4-demethylwyosine synthase (AdoMet-dependent) | This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine. Group: Enzymes. Synonyms: TYW1. Enzyme Commission Number: EC 4.1.3.44. 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-4921; tRNA 4-demethylwyosine synthase (AdoMet-dependent); EC 4.1.3.44; TYW1. Cat No: EXWM-4921. | |
| tRNA-guanosine34 transglycosylase | Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine. The eubacterial enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. Group: Enzymes. Synonyms: guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguou. Enzyme Commission Number: EC 2.4.2.29. CAS No. 72162-89-1. 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-2656; tRNA-guanosine34 transglycosylase; EC 2.4.2.29; 72162-89-1; guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguous); Q-insertase (ambiguous); queuine34 transfer ribonucleate ribosyltransferase; transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine34 transglycosidase; queuine tRNA-ribosyltransferase (ambiguous); TGT; [tRNA]-guanine34:queuine tRNA-D-ribosyltransferase; transfer ribonucleic acid guanine34 transglycosylase. Cat No: EXWM-2656. | |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. 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-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| 2-(3-amino-3-carboxypropyl)histidine synthase | A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis. Group: Enzymes. Synonyms: Dph2. Enzyme Commission Number: EC 2.5.1.108. 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-2724; 2-(3-amino-3-carboxypropyl)histidine synthase; EC 2.5.1.108; Dph2. Cat No: EXWM-2724. | |
| 25S rRNA (adenine645-N1)-methyltransferase | The enzyme is found in eukaryotes. The adenine position refers to rRNA in the yeast Saccharomyces cerevisiae, in which the enzyme is important for ribosome biogenesis. Group: Enzymes. Synonyms: 25S rRNA m1A645 methyltransferase; Rrp8. Enzyme Commission Number: EC 2.1.1.287. 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-1894; 25S rRNA (adenine645-N1)-methyltransferase; EC 2.1.1.287; 25S rRNA m1A645 methyltransferase; Rrp8. Cat No: EXWM-1894. | |
| 2-Phenyl-1,3-propanediol-d4 | Labeled Felbamate derived compounds. A labeled substrate for eukaryotic lipase enzymes. Group: Biochemicals. Alternative Names: 2-Phenyl-1,3-propane-1,1,3,3-d4-diol; NSC 78023-d4. Grades: Highly Purified. CAS No. 98704-00-8. Pack Sizes: 10mg. US Biological Life Sciences. |  Worldwide |
| 2-Phenyl-1,3-propanediol-[d4] | 2-Phenyl-1,3-propanediol-[d4]. Uses: Labelled felbamate derived compounds. a labelled substrate for eukaryotic lipase enzymes. Synonyms: 2-Phenyl-1,3-propanediol D4; 2-Phenyl-1,3-propane-1,1,3,3-d4-diol; NSC 78023-d4. Grade: 98%. CAS No. 98704-00-8. Molecular formula: C9H8D4O2. Mole weight: 156.22. |  |
| 2-polyprenyl-6-hydroxyphenol methylase | UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase). In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety. Group: Enzymes. Synonyms: ubiG (gene name, ambiguous); ubiG methyltransferase (ambiguous); 2-octaprenyl-6-hydroxyphenol methylase. Enzyme Commission Number: EC 2.1.1.222. 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-1825; 2-polyprenyl-6-hydroxyphenol methylase; EC 2.1.1.222; ubiG (gene name, ambiguous); ubiG methyltransferase (ambiguous); 2-octaprenyl-6-hydroxyphenol methylase. Cat No: EXWM-1825. | |
| 4-phosphopantoate-β-alanine ligase | The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphorylation (EC 6.3.2.1 [pantoate-β-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme. Group: Enzymes. Synonyms: phosphopantothenate synthetase; TK1686 protein. Enzyme Commission Number: EC 6.3.2.36. 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-5753; 4-phosphopantoate-β-alanine ligase; EC 6.3.2.36; phosphopantothenate synthetase; TK1686 protein. Cat No: EXWM-5753. | |
| 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase | The enzyme removes (decaps) the N7-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides. Decapping is an important process in the control of eukaryotic mRNA degradation. The enzyme functions to clear the cell of cap structure following decay of the RNA body. The nematode enzyme can also decap triply methylated substrates, 5'-(N2,N2,N7-trimethyl 5'-triphosphoguanosine)-[mRNA]. Group: Enzymes. Synonyms: DcpS; m7GpppX pyrophosphatase; m7GpppN m7GMP phosphohydrolase; m7GpppX diphosphatase; m7G5'ppp5'N m7GMP phosphohydrolase. Enzyme Commission Number: EC 3.6.1.59. 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-4631; 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase; EC 3.6.1.59; DcpS; m7GpppX pyrophosphatase; m7GpppN m7GMP phosphohydrolase; m7GpppX diphosphatase; m7G5'ppp5'N m7GMP phosphohydrolase. Cat No: EXWM-4631. | |
| 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase | Decapping of mRNA is a critical step in eukaryotic mRNA turnover. The enzyme is unable to cleave a free cap structure (m7GpppG). The enzyme from Vaccinia virus is synergistically activated in the presence of Mg2+ and Mn2+. Group: Enzymes. Synonyms: Dcp2; NUDT16; D10 protein; D9 protein; D10 decapping enzyme; decapping enzyme; m7GpppN-mRNA hydrolase; m7GpppN-mRNA m7GDP phosphohydrolase. Enzyme Commission Number: EC 3.6.1.62. 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-4635; 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase; EC 3.6.1.62; Dcp2; NUDT16; D10 protein; D9 protein; D10 decapping enzyme; decapping enzyme; m7GpppN-mRNA hydrolase; m7GpppN-mRNA m7GDP phosphohydrolase. Cat No: EXWM-4635. | |
| A 484954 | A 484954 is a eukaryotic elongation factor-2 (eEF-2) kinase inhibitor (IC50 = 0.28 μM in enzymatic assay). A 484954 reduces eEF-2 phosphorylation with little effect on cancer cell growth. Synonyms: A-484954; A 484954; A484954; 7-Amino-1-cyclopropyl-3-ethyl-1,2,3,4-tetrahydro-2,4-dioxopyrido[2,3-d]pyrimidine-6-carboxamide. Grade: ≥98% by HPLC. CAS No. 142557-61-7. Molecular formula: C13H15N5O3. Mole weight: 289.29. | |
| Anhydrotetracycline hydrochloride | Anhydrotetracycline hydrochloride, a tetracycline biosynthetic precursor, is a potent competitive broad-spectrum tetracycline destructase enzymes inhibitor. Anhydrotetracycline hydrochloride is an effector for tetracycline controlled gene expression systems in eukaryotic cells [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 13803-65-1. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-118660. |  |
| apyrase | Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Enzyme Commission Number: EC 3.6.1.5. CAS No. 9000-95-7. Apyrase. 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-4623; apyrase; EC 3.6.1.5; 9000-95-7; ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]. Cat No: EXWM-4623. | |
| Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme) | GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859. | |
| bleomycin hydrolase | The molecule is a homohexamer in which the monomers have a papain-like tertiary structure (in peptidase family C1). The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Known from bacteria as well as eukaryotic organisms. Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyses Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates. Group: Enzymes. Synonyms: aminopeptidase C (Lactococcus lactis). Enzyme Commission Number: EC 3.4.22.40. CAS No. 53096-17-6. 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-4215; bleomycin hydrolase; EC 3.4.22.40; 53096-17-6; aminopeptidase C (Lactococcus lactis). Cat No: EXWM-4215. | |
| carboxypeptidase C | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in). Widely distributed in eukaryotes. Type example of peptidase family S10. Group: Enzymes. Synonyms: carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin. Enzyme Commission Number: EC 3.4.16.5. CAS No. 9046-67-7. Carboxypeptidase Y. 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-4059; carboxypeptidase C; EC 3.4.16.5; 9046-67-7; carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin. Cat No: EXWM-4059. | |
| cardiolipin synthase (CMP-forming) | The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin. It requires divalent cations for activity. Group: Enzymes. Enzyme Commission Number: EC 2.7.8.41. 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-3341; cardiolipin synthase (CMP-forming); EC 2.7.8.41. Cat No: EXWM-3341. | |
| Casein Kinase Iδ rat, Recombinant | The Casein kinase 1 family of protein kinases are serine/threonine-selective enzymes that function as regulators of signal transduction pathways in most eukaryotic cell types. CK1 isoforms are involved in Wnt signaling, circadian rhythms, nucleo-cytoplasmic shuttling of transcription factors, DNA repair, and DNA transcription. C-terminal truncated, n-terminal his-tag/s-tag, > 90% (sds-page), recombinant, expressed in e. coli, solution. Group: Enzymes. Synonyms: Casein Kinase Iδ; Casein Kinase I; CK-Iδ; CK-I; Non-specific serine/threonine protein kinase; Protein phosphokinase; Protein serine kinase; Protein serine-threonine kinase; Protein-serine kinase; Serine kinase; Serine protein kinase; Serine (threonine) protein kinase; Serine-specific protein kinase; Serine/t. Purity: > 90% (SDS-PAGE). CK-I&delta. Mole weight: mol wt 41.8 kDa. Activity: 1,000-3,000 units/mg protein. Stability: -20°C. Form: solution. Source: E. coli. Species: Rat. Casein Kinase Iδ; Casein Kinase I; CK-Iδ; CK-I; Non-specific serine/threonine protein kinase; Protein phosphokinase; Protein serine kinase; Protein serine-threonine kinase; Protein-serine kinase; Serine kinase; Serine protein kinase; Serine (threonine) protein kinase; Serine-specific protein kinase; Serine/threonine protein kinase; Threonine-specific protein kinase. Cat No: NATE-0140. | |
| CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase | This enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes. The enzyme requires Mg2+ and K+ for maximal activity. Group: Enzymes. Synonyms: carS (gene name); CDP-2,3-di-O-geranylgeranyl-sn-glycerol synthase; CTP:2,3-GG-GP ether cytidylyltransferase; CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase; CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol synthase; CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase; CDP-unsaturated archaeol synthase; . Enzyme Commission Number: EC 2.7.7.67. CAS No. 329791-09-5. 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-3278; CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase; EC 2.7.7.67; 329791-09-5; carS (gene name); CDP-2,3-di-O-geranylgeranyl-sn-glycerol synthase; CTP:2,3-GG-GP ether cytidylyltransferase; CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase; CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol synthase; CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase; CDP-unsaturated archaeol synthase; CDP-archaeol synthase (incorrect). Cat No: EXWM-3278. | |
| cGMP-dependent protein kinase | CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase. Group: Enzymes. Synonyms: 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Enzyme Commission Number: EC 2.7.11.12. CAS No. 141588-27-4. 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-3131; cGMP-dependent protein kinase; EC 2.7.11.12; 141588-27-4; 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Cat No: EXWM-3131. | |
| (d)CMP kinase | The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP. Group: Enzymes. Synonyms: prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase. Enzyme Commission Number: EC 2.7.4.25. dCMP kinase. 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-3207; (d)CMP kinase; EC 2.7.4.25; prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase. Cat No: EXWM-3207. | |
| Dehydroaltenusin | Dehydroaltenusin is a selective eukaryotic DNA polymerase α inhibitor and a type of antibiotic produced by a fungus (IC50 = 0.68 μM). Dehydroaltenusin inhibits mammalian pol α activity. Dehydroaltenusin arrests the cancer cell cycle at the S-phase and triggers apoptosis. Dehydroaltenusin possesses anti-tumor activity against human adenocarcinoma tumor in vivo. Uses: Enzyme inhibitors. Synonyms: 6H-Dibenzo(b,d)pyran-2,6(4ah)-dione, 3,7-dihydroxy-9-methoxy-4a-methyl-, (4aS)-; (S)-Dehydroaltenusin. CAS No. 31186-13-7. Molecular formula: C15H12O6. Mole weight: 288.25. | |
| 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. | |
| deoxyhypusine monooxygenase | The enzyme catalyses the final step in the formation of the amino acid hypusine in the eukaryotic initiation factor 5A. Group: Enzymes. Synonyms: deoxyhypusine hydroxylase; deoxyhypusine dioxygenase. Enzyme Commission Number: EC 1.14.99.29. CAS No. 101920-83-6. 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-1045; deoxyhypusine monooxygenase; EC 1.14.99.29; 101920-83-6; deoxyhypusine hydroxylase; deoxyhypusine dioxygenase. Cat No: EXWM-1045. | |
| deoxyhypusine synthase | The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase. Group: Enzymes. Synonyms: spermidine:eIF5A-lysine 4-amino. Enzyme Commission Number: EC 2.5.1.46. CAS No. 127069-31-2. 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-2782; deoxyhypusine synthase; EC 2.5.1.46; 127069-31-2; spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming). Cat No: EXWM-2782. | |
| D-galacturonate reductase | The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis. The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate. It is also active with D-glucuronate and glyceraldehyde. Neither enzyme shows any activity with NADH. Group: Enzymes. Synonyms: GalUR; gar1 (gene name). Enzyme Commission Number: EC 1.1.1.365. 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-0282; D-galacturonate reductase; EC 1.1.1.365; GalUR; gar1 (gene name). Cat No: EXWM-0282. | |
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