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| Product | Description | |
|---|---|---|
| 4-hydroxy-3-polyprenylbenzoate decarboxylase | The enzyme catalyses a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase. Group: Enzymes. Synonyms: ubiD (gene name); 4-hydroxy-3-solanesylbenzoate decarboxylase; 3-octaprenyl-4-hydroxybenzoate decarboxylase. Enzyme Commission Number: EC 4.1.1.98. 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-4848; 4-hydroxy-3-polyprenylbenzoate decarboxylase; EC 4.1.1.98; ubiD (gene name); 4-hydroxy-3-solanesylbenzoate decarboxylase; 3-octaprenyl-4-hydroxybenzoate decarboxylase. Cat No: EXWM-4848. |  |
| anaerobic carbon-monoxide dehydrogenase | This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. 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-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227. | |
| assimilatory sulfite reductase (ferredoxin) | An iron protein. The enzyme participates in sulfate assimilation. While it is usually found in cyanobacteria, plants and algae, it has also been reported in bacteria. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.1.2, assimilatory sulfite reductase (NADPH). Group: Enzymes. Synonyms: ferredoxin-sulfite reductase; SIR (gene name); sulfite reductase (ferredoxin). Enzyme Commission Number: EC 1.8.7.1. CAS No. 37256-50-1. 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-1680; assimilatory sulfite reductase (ferredoxin); EC 1.8.7.1; 37256-50-1; ferredoxin-sulfite reductase; SIR (gene name); sulfite reductase (ferredoxin). Cat No: EXWM-1680. | |
| assimilatory sulfite reductase (NADPH) | Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). Group: Enzymes. Synonyms: sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Enzyme Commission Number: EC 1.8.1.2. CAS No. 9029-35-0. 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-1646; assimilatory sulfite reductase (NADPH); EC 1.8.1.2; 9029-35-0; sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Cat No: EXWM-1646. | |
| β-carotene 15,15'-dioxygenase | Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products. The enzyme can also process β-cryptoxanthin, 8'-apo-β-carotenal, 4'-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore. Group: Enzymes. Synonyms: blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15'-dioxygenase; BCMO1 (misleading); β-carotene 15,15'-monooxygenase (incorrect). Enzyme Commission Number: EC 1.13.11.63. 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-0583; β-carotene 15,15'-dioxygenase; EC 1.13.11.63; blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15'-dioxygenase; BCMO1 (misleading); β-carotene 15,15'-monooxygenase (incorrect). Cat No: EXWM-0583. | |
| (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. | |
| (d)CMP Kinase (Crude Enzyme) | This enzyme specifically phosphorylates CMP (or dCMP). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology. Group: Enzymes. Synonyms: prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase. Enzyme Commission Number: EC 2.7.4.25. dCMP kinase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. prokaryotic cytidylate kinase; deoxycytidylate kinase; dCMP kinase; deoxycytidine monophosphokinase. Pack: 100ml. Cat No: NATE-1828. | |
| dissimilatory sulfite reductase | Contain siroheme. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction). The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. This disulfide can be reduced by a number of proteins including DsrK and TcmB. This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation. Group: Enzymes. Synonyms: siroheme sulfite reductase; hydrogen-sulfide:(acceptor) oxidoredu. Enzyme Commission Number: EC 1.8.99.5. CAS No. 37256-51-2. 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-1686; dissimilatory sulfite reductase; EC 1.8.99.5; 37256-51-2; siroheme sulfite reductase; hydrogen-sulfide:(acceptor) oxidoreductase (ambiguous); DsrAB. Cat No: EXWM-1686. | |
| Glutathione S-Transferase from E.coli, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to iden...ferase. Mole weight: 26kDa. Activity: >20 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile Filtered clear solution in Phosphate Buffered Saline pH 7.4. Source: E.coli. Species: E.coli. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1945. | |
| Glutathione S-Transferase, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomalalso known as MAPEGproteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new...erase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. Purity: >90% (SDS-PAGE test). Mole weight: About 26kDa (SDS-PAGE detection). Activity: 30 u/mg. Appearance: White powder, lyophilized or colorless liquid. Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1141. | |
| glycine C-acetyltransferase | This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. Group: Enzymes. Synonyms: 2-amino-3-ketobutyrate CoA ligase; 2-amino-3-ketobutyrate coenzyme A ligase; 2-amino-3-ketobutyrate-CoA ligase; glycine acetyltransferase; aminoacetone synthase; aminoacetone synthetase; KBL; AKB ligase. Enzyme Commission Number: EC 2.3.1.29. CAS No. 37257-11-7. 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-2206; glycine C-acetyltransferase; EC 2.3.1.29; 37257-11-7; 2-amino-3-ketobutyrate CoA ligase; 2-amino-3-ketobutyrate coenzyme A ligase; 2-amino-3-ketobutyrate-CoA ligase; glycine acetyltransferase; aminoacetone synthase; aminoacetone synthetase; KBL; AKB ligase. Cat No: EXWM-2206. | |
| L-threonine 3-dehydrogenase | This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone. Group: Enzymes. Synonyms: L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH. Enzyme Commission Number: EC 1.1.1.103. CAS No. 9067-99-6. 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-0006; L-threonine 3-dehydrogenase; EC 1.1.1.103; 9067-99-6; L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH. Cat No: EXWM-0006. | |
| 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. | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Rat Glutathione-S-Transferase | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions. Group: Enzymes. Synonyms: Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase;. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Purity: Purified. Glutathione S-Transferase. Activity: > 10 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-0327. | |
| Native Rat Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| nitrite reductase (NADH) | An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H]. Group: Enzymes. Synonyms: nitrite reductase (reduced nicotinamide adenine dinucleotide); NADH-nitrite oxidoreductase; assimilatory nitrite reductase (ambiguous); nirB (gene name); nirD (gene name). Enzyme Commission Number: EC 1.7.1.15. CAS No. 9029-29-2. 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-1608; nitrite reductase (NADH); EC 1.7.1.15; 9029-29-2; nitrite reductase (reduced nicotinamide adenine dinucleotide); NADH-nitrite oxidoreductase; assimilatory nitrite reductase (ambiguous); nirB (gene name); nirD (gene name). Cat No: EXWM-1608. | |
| prokaryotic ubiquitin-like protein ligase | The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. It catalyses the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation. Group: Enzymes. Synonyms: PafA (ambiguous); Pup ligase; proteasome accessory factor A. Enzyme Commission Number: EC 6.3.1.19. 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-5721; prokaryotic ubiquitin-like protein ligase; EC 6.3.1.19; PafA (ambiguous); Pup ligase; proteasome accessory factor A. Cat No: EXWM-5721. | |
| 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. | |
| Pup amidohydrolase | The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis. The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein. Group: Enzymes. Synonyms: dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Enzyme Commission Number: EC 3.5.1.119. 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-4399; Pup amidohydrolase; EC 3.5.1.119; dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Cat No: EXWM-4399. | |
| Reverse Transcriptase from HIV, Recombinant | Chromatographically purified heterodimer composed of 66kDa and 51kDa subunits. Supplied as a solution in 10mM potassium phosphate, pH 7.4, 1mM DTT and 20% glycerol. Primarily for AIDS research purposes; this enzyme has less fidelity than the AMV enzyme in other applications such as the preparation of cDNA from mRNA for cloning purposes. Applications: Hiv reverse transcriptase is used for research on the aids primer. however it can be substituted for amv reverse transcriptase, which is mainly used to transcribe mrna into double stranded cdna, that can be inserted into prokaryotic vectors. the enzyme can also be used with either single stranded dna or rna templates to mak...or labeling the termini of dna fragments with protruding 5' termini. the enzyme can also be used to sequence dnas by the dideoxy chain termination method of sanger when the klenow fragment of e. coli dna polymerase i, or the t7 dna polymerase yield unsatisfactory results. Group: Enzymes. Synonyms: Reverse transcriptase; RT. Enzyme Commission Number: EC 2.7.7.49. CAS No. 9068-38-6. Purity: Chromatographically purified. RT. Mole weight: 66 kDa and 51 kDa. Activity: > 5,000 units per mg protein. Storage: Store at -20°C. Form: A solution in 10mM potassium phosphate, pH 7.4, 1mM DTT and 20% glycerol. Source: E. coli. Species: HIV. Reverse transcriptase; RT. Cat No: NATE-0987. | |
| signal peptidase I | The enzyme is found in bacterial membranes and in chloroplast thylakoid membranes. Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity. Hydrolyses a single bond -Ala?Ala- in M13 phage procoat protein, producing free signal peptide and coat protein. Formerly included in EC 3.4.99.36. Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane. Type example of peptidase family S26. Group: Enzymes. Synonyms: leader peptidase I; signal proteinase. Enzyme Commission Number: EC 3.4.21.89. CAS No. 65979-36-4. 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-4180; signal peptidase I; EC 3.4.21.89; 65979-36-4; leader peptidase I; signal proteinase; Escherichia coli leader peptidase; eukaryotic signal peptidase; eukaryotic signal proteinase; leader peptidase; leader peptide hydrolase; leader proteinase; signal peptidase; pilin leader peptidase; SPC; prokaryotic signal peptidase; prokaryotic leader peptidase; HOSP; prokaryotic signal proteinase; propeptidase; PuIO prepilin peptidase; signal peptide hydrolase; signal peptide peptidase; signalase; bacterial leader peptidase 1; pilin leader peptidase. Cat No: EXWM-4180. | |
| SUMO Protease 1 (GST-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...eaction by affinity chromatography using the Glutathione resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 52.6 kDa (403-621 aa + N-terminal GST). Activity: >10,000 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.1-0.5 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1708. | |
| SUMO Protease 1 (His-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO Protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...finity chromatography using the Ni chelating resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 28.7 kDa (403-621 aa + N-terminal Poly-His tag). Activity: 1 X 10^6 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.01-0.05 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1709. | |
| 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. | |
| tubulin GTPase | An intrinsic activity of α-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others. Group: Enzymes. Enzyme Commission Number: EC 3.6.5.6. 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-4717; tubulin GTPase; EC 3.6.5.6. Cat No: EXWM-4717. | |
| UMP/CMP kinase | This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase. Group: Enzymes. Synonyms: cytidylate kinase; deoxycytidylate kinase; CTP:CMP phosphotransferase; dCMP kinase; deoxycytidine monophosphokinase; UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase. Enzyme Commission Number: EC 2.7.4.14. CAS No. 37278-21-0. 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-3195; UMP/CMP kinase; EC 2.7.4.14; 37278-21-0; cytidylate kinase; deoxycytidylate kinase; CTP:CMP phosphotransferase; dCMP kinase; deoxycytidine monophosphokinase; UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase. Cat No: EXWM-3195. | |
| urea carboxylase | A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates. Group: Enzymes. Synonyms: urease (ATP-hydrolysing); urea carboxylase (hydrolysing); ATP-urea amidolyase; urea amidolyase; UALase; UCA. Enzyme Commission Number: EC 6.3.4.6. CAS No. 9058-98-4. 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-5798; urea carboxylase; EC 6.3.4.6; 9058-98-4; urease (ATP-hydrolysing); urea carboxylase (hydrolysing); ATP-urea amidolyase; urea amidolyase; UALase; UCA. Cat No: EXWM-5798. | |
| 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. | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| FAD synthetase | Requires Mg2+ and is highly specific for ATP as phosphate donor. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase. Group: Enzymes. Synonyms: FAD pyrophosphorylase; riboflavin mononucleotide adenylyltransferase; adenosine triphosphate-riboflavin mononucleotide transadenylase; adenosine triphosphate-riboflavine mononucleotide transadenylase; riboflavin adenine dinucleotide pyrophosp. Enzyme Commission Number: EC 2.7.7.2. CAS No. 9026-37-3. 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-3234; FAD synthetase; EC 2.7.7.2; 9026-37-3; FAD pyrophosphorylase; riboflavin mononucleotide adenylyltransferase; adenosine triphosphate-riboflavin mononucleotide transadenylase; adenosine triphosphate-riboflavine mononucleotide transadenylase; riboflavin adenine dinucleotide pyrophosphorylase; riboflavine adenine dinucleotide adenylyltransferase; flavin adenine dinucleotide synthetase; FADS; FMN adenylyltransferase. Cat No: EXWM-3234. | |
| Formate dehydrogenase | Formate dehydrogenase is an enzyme ubiquitous in prokaryotes and eukaryotes that catalyzes the reversible oxidation of formate to carbon dioxide. According to its metal content, structure and catalytic strategy, Formate dehydrogenase can be divided into two categories, non-metallic and metal-containing, which are often used in biochemical research [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9028-85-7. Pack Sizes: 50 U; 100 U. Product ID: HY-P2907. |  |
| futalosine hydrolase | This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes. Group: Enzymes. Synonyms: futalosine nucleosidase; MqnB. Enzyme Commission Number: EC 3.2.2.26. 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-3980; futalosine hydrolase; EC 3.2.2.26; futalosine nucleosidase; MqnB. Cat No: EXWM-3980. | |
| GlcNAc-1-phosphate uridyltransferase from Campylobacter jejuni, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Source: E. coli. Species: Campylobacter jejuni. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1492. | |
| GlcNAc1-phosphate uridyltransferase from E. coli K-12, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Mole weight: 25 kDa. Source: E. coli. Species: E. coli K-12. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1482. | |
| GlcNAc-1-phosphate uridyltransferase from Human, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. CAS No. 9023-06-7;9031-91-8. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Source: E. coli. Species: Human. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1500. | |
| Glutamate dehydrogenase | Glutamate dehydrogenase is an enzyme in both prokaryotes and eukaryotic mitochondria. Glutamate dehydrogenase can be used for the enzymatic determination of ammonia, alpha-ketoglutaric acid, L-glutamate and urease [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-46-1. Pack Sizes: 1 KU. Product ID: HY-E70003. | |
| halimadienyl-diphosphate synthase | Requires Mg2+ for activity. This enzyme is found in pathogenic prokaryotes such as Mycobacterium tuberculosis but not in non-pathogens such as Mycobacterium smegmatis so may play a role in pathogenicity. The product of the reaction is subsequently dephosphorylated yielding tuberculosinol (halima-5,13-dien-15-ol). Group: Enzymes. Synonyms: Rv3377c; halimadienyl diphosphate synthase; tuberculosinol diphosphate synthase; halima-5(6),13-dien-15-yl-diphosphate lyase (cyclizing); halima-5,13-dien-15-yl-diphosphate lyase (decyclizing). Enzyme Commission Number: EC 5.5.1.16. 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-5617; halimadienyl-diphosphate synthase; EC 5.5.1.16; Rv3377c; halimadienyl diphosphate synthase; tuberculosinol diphosphate synthase; halima-5(6),13-dien-15-yl-diphosphate lyase (cyclizing); halima-5,13-dien-15-yl-diphosphate lyase (decyclizing). Cat No: EXWM-5617. | |
| holo-[acyl-carrier-protein] synthase | Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes. Removal of the 4-pho...AS No. 37278-30-1. 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-3345; holo-[acyl-carrier-protein] synthase; EC 2.7.8.7; 37278-30-1; acyl carrier protein holoprotein (holo-ACP) synthetase; holo-ACP synthetase; coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase; holosynthase; acyl carrier protein synthetase; holo-ACP synthase; PPTase; AcpS; ACPS; acyl carrier protein synthase; P-pant transferase; CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase; CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein] 4'-pantetheinephosphotransferase. Cat No: EXWM-3345. | |
| Lactate Dehydrogenase from Chicken Heart, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Purity: > 96% (SDS-PAGE). LDH. Activity: >90%. (>200U/mL). Storage: -20°C. Form: Lyophilized. Source: E. coli. Species: Chicken Heart. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0383. | |
| Lactic Dehydrogenase, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Source: E. coli. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Cat No: NATE-0381. | |
| L-Lactate Dehydrogenase (Crude Enzyme) | Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion oflactate to pyruvic acid and back, as it converts NAD + to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; biotechnology; drug development. Group: Enzymes. Synonyms: lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Pack: 100ml. Cat No: NATE-1793. | |
| L-Lactate Dehydrogenase from Porcine, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: High purity l-lactate dehydrogenase (porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: ~ 330 U/mg. Storage: > 2 years at 4°C. Form: In 3.2 M ammonium sulphate. Source: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-1105. | |
| L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Recombinant, expressed in e. coli, lyophilized powder, > 200 units/mg protein (lowry). Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 200 units/mg protein (Lowry). Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Bacillus stearothermophilus. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0382. | |
| methenyltetrahydrofolate cyclohydrolase | In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate-tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity. Group: Enzymes. Synonyms: Citrovorum factor cyclodehydrase; cyclohydrolase; formyl-methenyl-methylenetetrahydrofolate synthetase (combined); 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing). Enzyme Commission Number: EC 3.5.4.9. CAS No. 9027-97-8. 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-4577; methenyltetrahydrofolate cyclohydrolase; EC 3.5.4.9; 9027-97-8; Citrovorum factor cyclodehydrase; cyclohydrolase; formyl-methenyl-methylenetetrahydrofolate synthetase (combined); 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing). Cat No: EXWM-4577. | |
| 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. | |
| methylenetetrahydrofolate dehydrogenase (NADP+) | In eukaryotes, occurs as a trifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and formate-tetrahydrofolate ligase(EC 6.3.4.3) activity. In some prokaryotes occurs as a bifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9). Group: Enzymes. Synonyms: N5,N10-methylenetetrahydrofolate dehydrogenase; 5,10-methylenetetrahydrofolate:NADP oxidoreductase; 5,10-methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase (NADP). Enzyme Commission Number: EC 1.5.1.5. CAS No. 9029-14-5. 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-1531; methylenetetrahydrofolate dehydrogenase (NADP+); EC 1.5.1.5; 9029-14-5; N5,N10-methylenetetrahydrofolate dehydrogenase; 5,10-methylenetetrahydrofolate:NADP oxidoreductase; 5,10-methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase (NADP). Cat No: EXWM-1531. | |
| molybdenum cofactor cytidylyltransferase | Catalyses the cytidylation of the molybdenum cofactor. This modification occurs only in prokaryotes. Divalent cations such as Mg2+ or Mn2+ are required for activity. ATP or GTP cannot replace CTP. Group: Enzymes. Synonyms: MocA; CTP:molybdopterin cytidylyltransferase; MoCo cytidylyltransferase; Mo-MPT cytidyltransferase. Enzyme Commission Number: EC 2.7.7.76. 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-3288; molybdenum cofactor cytidylyltransferase; EC 2.7.7.76; MocA; CTP:molybdopterin cytidylyltransferase; MoCo cytidylyltransferase; Mo-MPT cytidyltransferase. Cat No: EXWM-3288. | |
| molybdenum cofactor guanylyltransferase | Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes. Group: Enzymes. Synonyms: MobA; MoCo guanylyltransferase. Enzyme Commission Number: EC 2.7.7.77. 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-3289; molybdenum cofactor guanylyltransferase; EC 2.7.7.77; MobA; MoCo guanylyltransferase. Cat No: EXWM-3289. | |
| molybdenum cofactor sulfurtransferase | Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein. Group: Enzymes. Synonyms: molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase. Enzyme Commission Number: EC 2.8.1.9. 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-3367; molybdenum cofactor sulfurtransferase; EC 2.8.1.9; molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase. Cat No: EXWM-3367. | |
| 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. | |
| molybdopterin-synthase adenylyltransferase | Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain. Group: Enzymes. Synonyms: MoeB; adenylyltransferase and sulfurtransferase MOCS3. Enzyme Commission Number: EC 2.7.7.80. 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-3293; molybdopterin-synthase adenylyltransferase; EC 2.7.7.80; MoeB; adenylyltransferase and sulfurtransferase MOCS3. Cat No: EXWM-3293. | |
| Native Bovine L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: For use in enzymatic determination of lactate or pyruvate. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nL. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5. Source: Bovine heart. Species: Bovine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0409. | |
| Native Chicken L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 1.3 M (NH4)2SO4, pH 6.0. Source: Chicken heart. Species: Chicken. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0411. | |
| Native Human Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0380. | |
| Native Human Lactate Dehydrogenase 1 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0384. | |
| Native Human Lactate Dehydrogenase 2 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0386. | |
| Native Human Lactate Dehydrogenase 3 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0388. | |
| Native Human Lactate Dehydrogenase 4 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; validation studies; manufacturing. Group: Enzymes. Synonyms: LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 35 U/mg protein (> 110 U/mL). Stability: 2 years. Storage: 2-8°C. Form: Liquid; Suspension in 3.1 M ammonium sulfate, 20 mM tris chloride, 1 mM DTT, 1 mM EDTA, pH 7.5. Source: Human Liver. Species: Human. LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme; Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0965. | |
| Native Human Lactate Dehydrogenase 5 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Liver. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0390. | |
| Native Lactate Dehydrogenase from Thermophillic bacteria | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic test and biosensors; nadh recycling. this enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-400. | |
| Native Microorganism D-lactate dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: 400U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Storage: Store at -20°C. Form: Freeze dried powder. Source: Microorganism. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-207. | |
| Native Porcine heart Lactate dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 115 kDa±6,500. Activity: Grade? 2,000U/ml or more. Stability: Stable at 5°C for at least one year. Appearance: Crystalline suspension in 1.6M ammonium sulfate solution. Source: Porcine heart. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-206. | |
| Native Porcine Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: ~136,700. Activity: > 100 U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Lyophilized. Source: Porcine Muscle. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0964. | |
| Native Porcine L-Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Dehydrogenase that catalyzes the interconversion of specific for l(+)-lactate to pyruvate. apply this ready-to-use enzyme directly in your diagnostic test. rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase,...ehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. CAS No. 9001-60-9. LDH. Activity: >550 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5. Source: Porcine muscle. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0982. | |
| Native Porcine L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0412. | |
| 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 Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 140 kDa. Activity: > 250 units per mg protein. Source: Rabbit Muscle. Species: Rabbit. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-268. | |
| Native Rabbit L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Lactic dehydrogenase (ldh) has a total molecular weight of 140 kda and is composed of 4 subunits which are designated m subunit (muscle) and h subunit (heart). these subunits may be mixed in any of 5 combinations (m4, m3h1, m2h2, mh3, and h4). skeletal muscle contains ldh that is predominately m4 with some small amounts of m3h and traces of h2h2. the h and m subunits are quite ...reductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, lyophilized powder; Type II, ; Type III, ammonium sulfate suspension, Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0. Source: Rabbit muscle. Species: Rabbit. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0413. | |
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