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| Product | Description | |
|---|---|---|
| 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-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. |  |
| 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. | |
| 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. | |
| 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. | |
| (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. | |
| 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. | |
| diphthine methyl ester synthase | This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.314. 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-1922; diphthine methyl ester synthase; EC 2.1.1.314; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Cat No: EXWM-1922. | |
| diphthine synthase | This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine-ammonia ligase. Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). In the archaeon Pyrococcus horikoshii the enzyme acts on His600 of elongation factor 2. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.98. CAS No. 114514-25-9. 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-1998; diphthine synthase; EC 2.1.1.98; 114514-25-9; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous). Cat No: EXWM-1998. | |
| dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase | This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells. Group: Enzymes. Synonyms: ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.256. 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-2486; dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase; EC 2.4.1.256; ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase. Cat No: EXWM-2486. | |
| double-stranded RNA adenine deaminase | This eukaryotic enzyme is involved in RNA editing. It destabilizes double-stranded RNA through conversion of adenosine to inosine. Inositol hexakisphosphate is required for activity. Group: Enzymes. Synonyms: ADAR; double-stranded RNA adenosine deaminase; dsRAD; dsRNA adenosine deaminase; DRADA1; double-stranded RNA-specific adenosine deaminase. Enzyme Commission Number: EC 3.5.4.37. 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-4565; double-stranded RNA adenine deaminase; EC 3.5.4.37; ADAR; double-stranded RNA adenosine deaminase; dsRAD; dsRNA adenosine deaminase; DRADA1; double-stranded RNA-specific adenosine deaminase. Cat No: EXWM-4565. | |
| dynein ATPase | A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa). Group: Enzymes. Synonyms: dynein adenosine 5'-triphosphatase. Enzyme Commission Number: EC 3.6.4.2. 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-4704; dynein ATPase; EC 3.6.4.2; dynein adenosine 5'-triphosphatase. Cat No: EXWM-4704. | |
| EDA-m7GTP - ATTO-MB2 | EDA-m7GTP - ATTO-MB2 is a fluorescent substrate used for studying RNA capping enzymes. It is structurally similar to m7GTP, a cap structure found at the 5' end of eukaryotic messenger RNA (mRNA). This product can be used for fluorescence polarization assays to measure the activity of RNA capping enzymes such as RNA guanine-7 methyltransferase (RNMT). Understanding the activity of these enzymes can provide insight into diseases that rely on mRNA modification, such as cancer and viral infections. Synonyms: 2'/3'-O-(2-Aminoethyl-carbamoyl)-7-methyl-guanosine-5'-triphosphate, labeled with ATTO-MB2, Triethylammonium salt. Grades: ≥ 95 % by HPLC. Molecular formula: C33H43N10O16P3S (free acid). Mole weight: 960.74 (free acid). |  |
| 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. | |
| 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. | |
| guanine-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A eukaryotic enzyme that imports guanine and tryptophan (it contains a single ATP-binding site). Group: Enzymes. Enzyme Commission Number: EC 7.6.2.6 (Formerly EC 3.6.3.37). 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-4675; guanine-transporting ATPase; EC 3.6.3.37. Cat No: EXWM-4675. | |
| infectious pancreatic necrosis birnavirus Vp4 peptidase | Infectious pancreatic necrosis virus (IPNV) is a birnavirus that causes an acute, contagious disease in young salmonid fish. As with most viruses that infect eukaryotic cells, the proteolytic processing of viral precursor proteins is a crucial step in the life cycle of this virus. pVP2 is converted into VP2 by cleavage near the carboxy end of pVP2. This cleavage is most likely due to host-cell proteases rather than VP4. Differs from most serine peptidases in not having the catalytic triad Ser-His-Asp. Belongs in peptidase family S50. Group: Enzymes. Synonyms: infectious pancreatic necrosis virus protease; IPNV Vp4 protease; IPNV Vp4 peptidase; NS protease; NS-associated protease; Vp4 protease. Enzyme Commission Number: EC 3.4.21.115. 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-4110; infectious pancreatic necrosis birnavirus Vp4 peptidase; EC 3.4.21.115; infectious pancreatic necrosis virus protease; IPNV Vp4 protease; IPNV Vp4 peptidase; NS protease; NS-associated protease; Vp4 protease. Cat No: EXWM-4110. | |
| limit dextrin α-1,6-maltotetraose-hydrolase | This bacterial enzyme catalyses a reaction similar to EC 3.2.1.33, amylo-α-1,6-glucosidase (one of the activities of the eukaryotic glycogen debranching enzyme). However, while EC 3.2.1.33 removes single glucose residues linked by 1,6-α-linkage, and thus requires the additional activity of 4-α-glucanotransferase (EC 2.4.1.25) to act on limit dextrins formed by glycogen phosphorylase (EC 2.4.1.1), this enzyme removes maltotriose and maltotetraose chains that are attached by 1,6-α-linkage to the limit dextrin main chain, generating a debranched limit dextrin without a need for another enzyme. Group: Enzymes. Synonyms: glgX (gene name); glycogen debranching enzyme (ambiguous). Enzyme Commission Number: EC 3.2.1.196. 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-3880; limit dextrin α-1,6-maltotetraose-hydrolase; EC 3.2.1.196; glgX (gene name); glycogen debranching enzyme (ambiguous). Cat No: EXWM-3880. | |
| 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. | |
| 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. | |
| Native Aspergillus restrictus Restrictocin | Restrictocin from Aspergillus restrictus is a ribosome-inactivating protein that acts by specifically cleaving rRNA. Approximately 70% of the protein is active restrictocin. Restrictocin shares a high degree of amino acid sequence homology with mitogillin, a ribotoxin that cleaves a single phosphodiester bond of the 29S rRNA of eukaryotic ribosomes. Restrictocin is thought to be activated during the process of secretion. Applications: Restrictocin from aspergillus restrictus is used to inhibit protein synthesis. it may be useful as a component of immunotoxins. this product is provided as a lyophilized powder. Group: Enzymes. Synonyms: Restrictocin; 1406-72-0. CAS No. 1406-72-0. Restrictocin. Storage: Store at -20°C. Form: Lyophilized powder. Source: Aspergillus restrictus. Restrictocin; 1406-72-0. Cat No: NATE-0865. | |
| Native Bovine Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from bovine heart contains a histidine residue at the nad-binding active site which is critical for activity. when this histidine is mutated a loss in activity is observed. Applications: Malic dehydrogenase has been used in a study to assess a flow injection system for on-line monitoring of fumaric acid in biological pr ocesses. 1 it has also been used in a study to investigate a root-knot nematode parasitizing peanut in...001-64-3. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: 2000-4000 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3 M (NH4)2SO4-0.01 M KH2PO4 solution, pH 7.3. Source: Bovine heart. Species: Bovine. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0445. | |
| Native Bovine Nucleoside 5'-Diphosphate Kinase | Nucleoside-diphosphate kinases are enzymes that catalyze the exchange of phosphate groups between different nucleoside diphosphates. NDK activities maintain an equilibrium between the concentrations of different nucleoside triphosphates such as, for example, when GTP produced in the citric acid (Krebs) cycle is converted to ATP. Nucleoside Diphosphate Kinase exists in two isoforms in eukaryotic cells, NDK-A and NDK-B. These enzymes are found expressed both in the mitochondria and the cytoplasm. Nucleoside diphosphate kinase exists in two isoforms in eukaryotic cells, ndk-a and ndk-b. these enzymes are found expressed both in the mit ochondria and the cytoplasm. Applica...cleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Activity: > 1,000 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous glycerol solution. Source: Bovine liver. Species: Bovine. nucleoside-diphosphate kinase; nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Cat No: NATE-0477. | |
| Native Bovine Protamine Kinase, Cytosolic | Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase. Applications: Cytosolic protamine kinase (cpk) is isolated from bovine kidney and has a molecular mass of approximately 45 kda. it phosphorylates the eukaryotic initiation factor 4e (eif4e), which initiates translation by mrna. it is used to study protein synthesis and various cellular processes. Group: Enzymes. Synonyms: Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Purity: >90% (SDS-PAGE). CPK. Activity: > 15,000 units/mg protein. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Cat No: NATE-0155. | |
| Native Chicken Malic Dehydrogenase (oxalacetate-decarboxylating) | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase (mdh) exists as two isoforms within eukaryotic cells, one that is expressed in the mit ochondria and functions in the tca cycle and one in the cytoplasm that converts malate from the mit ochondria back into oxaloacetate. Applications: Malic dehydrogenase has been used in a study to assess the dietary manganese requirement of juvenile yellow catfish (pelteobagrus fulvidraco) and effects on whole body minera...ctivity: 10-30 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.9 M (NH4)2SO4 solution containing 10 mM potassium phosphate, 0.5 mM 2-mercaptoethanol, 10 mM manganese chloride, and 3 mM Na4EDTA, pH 6.0. Source: Chicken liver. Species: Chicken. malic enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+oxidoreductase; EC 1.1.1.40; 9028-47-1. Cat No: NATE-0446. | |
| Native Porcine Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: Type I, ~1,000 units/mg protein (biuret); Type II, > 400 units/mg protein (biuret); Type III, > 600 units/mg protein (biuret); Type IV, 600-1000 units/mg protein (biuret). Storage: 2-8°C. Form: Type I, Type III, ammonium sulfate suspension; Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4, 0.1 M KH2PO4, pH 7.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.05 M potassium phosphate buffer, pH 7.5. Source: Porcine heart. Species: Porcine. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0447. | |
| 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 Thermus flavus Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from thermus flavus is stable and active at 90 oc. Applications: Malic dehydrogenase has been used in a study to assess electron transport chain activity in mit ochondria from human skeletal muscle. it has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 50 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains dextran. Source: Thermus flavus. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0448. | |
| nitric-oxide synthase (NADPH) | Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals, consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent]. Group: Enzymes. Synonyms: nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Enzyme Commission Number: EC 1.14.13.39. CAS No. 125978-95-2. NOSs. 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-0846; nitric-oxide synthase (NADPH); EC 1.14.13.39; 125978-95-2; nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Cat No: EXWM-0846. | |
| phosphohistidine phosphatase | This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most). The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate and peptide-bound phospholysine. Group: Enzymes. Synonyms: PHPT1 (gene name); protein histidine phosphatase; PHP. Enzyme Commission Number: EC 3.9.1.3. 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-4751; phosphohistidine phosphatase; EC 3.9.1.3; PHPT1 (gene name); protein histidine phosphatase; PHP. Cat No: EXWM-4751. | |
| proteasome endopeptidase complex | A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of α subunits, but the β subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of β subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the spec...atalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. 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-4374; proteasome endopeptidase complex; EC 3.4.25.1; 140879-24-9; ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Cat No: EXWM-4374. | |
| 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. | |
| Rbin-1 | Rbin-1 (ribozinoindole-1) is a potent and reversible inhibitor of Midasin (Mdn1), an enzyme belonging to the AAA+ (ATPases associated with diverse cellular activities) protein family (GI50 value 136 nM in wild-type cells). Rbin-2 can be used as a chemical probe for the eukaryotic ribosome assembly. Uses: Chemical probe for the eukaryotic ribosome assembly. Synonyms: Rbin-1; Rbin 1; Rbin1; Ribozinoindole-1; 3-[(2-methylprop-2-en-1-yl)sulfanyl]-5H-[1,2,4]triazino[5,6-b]indole; 3-[(2-methyl-2-propenyl)sulfanyl]-5H-[1,2,4]triazino[5,6-b]indole. Grades: 99%. CAS No. 328023-11-6. Molecular formula: C13H12N4S. Mole weight: 256.33. | |
| Rbin-2 | Rbin-2 is a potent, reversible and selective inhibitor of Midasin (Mdn1), an enzyme belonging to the AAA+ (ATPases associated with diverse cellular activities) protein family. Rbin-2 inhibits eukaryotic ribosome biogenesis and is a powerful probe for the eukaryotic ribosome assembly [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 2032282-97-4. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-100817. | |
| Rbin-2 | Rbin-2 (ribozinoindole-2) is a potent and reversible inhibitor of Midasin (Mdn1), an enzyme belonging to the AAA+ (ATPases associated with diverse cellular activities) protein family (GI50 value 14 nM in wild-type cells). Rbin-2 can be used as a chemical probe for the eukaryotic ribosome assembly. Uses: Chemical probe for the eukaryotic ribosome assembly. Synonyms: Rbin-2; Rbin 2; Rbin2; 7-Bromo-2-(2-methyl-allylsulfanyl)-9H-1,3,4,9-tetraaza-fluorene. Grades: 98%. CAS No. 2032282-97-4. Molecular formula: C13H11BrN4S. Mole weight: 335.22. | |
| [RNA-polymerase]-subunit kinase | The enzyme appears to be distinct from other protein kinases. It brings about multiple phosphorylations of the unique C-terminal repeat domain of the largest subunit of eukaryotic DNA-directed RNA polymerase (EC 2.7.7.6). The enzyme does not phosphorylate casein, phosvitin or histone. Group: Enzymes. Synonyms: CTD kinase; STK9. Enzyme Commission Number: EC 2.7.11.23. CAS No. 122097-00-1. 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-3143; [RNA-polymerase]-subunit kinase; EC 2.7.11.23; 122097-00-1; CTD kinase; STK9. Cat No: EXWM-3143. | |
| 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. | |
| 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. | |
| 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. | |
| tRNAAla(adenine37) deaminase | The enzyme deaminates adenosine37 to inosine in eukaryotic tRNAAla. tRNA editing is strictly dependent on Mg2+. Group: Enzymes. Synonyms: ADAT1; Tad1p. Enzyme Commission Number: EC 3.5.4.34. 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-4562; tRNAAla(adenine37) deaminase; EC 3.5.4.34; ADAT1; Tad1p. Cat No: EXWM-4562. | |
| tRNA (cytosine38-C5)-methyltransferase | The eukaryotic enzyme catalyses methylation of cytosine38 in the anti-codon loop of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC). Methylation by Dnmt2 protects tRNAs against stress-induced cleavage by ribonuclease. Group: Enzymes. Synonyms: hDNMT2 (gene name); DNMT2 (gene name); TRDMT1 (gene name). Enzyme Commission Number: EC 2.1.1.204. 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-1805; tRNA (cytosine38-C5)-methyltransferase; EC 2.1.1.204; hDNMT2 (gene name); DNMT2 (gene name); TRDMT1 (gene name). Cat No: EXWM-1805. | |
| 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. | |
| tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase | The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe. Group: Enzymes. Synonyms: TYW2; tRNA-yW synthesizing enzyme-2; TRM12 (gene name); taw2 (gene name). Enzyme Commission Number: EC 2.5.1.114. 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-2730; tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase; EC 2.5.1.114; TYW2; tRNA-yW synthesizing enzyme-2; TRM12 (gene name); taw2 (gene name). Cat No: EXWM-2730. | |
| tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase | The enzyme is involved in the biosynthesis of hypermodified tricyclic bases found at position 37 of certain tRNAs. These modifications are important for translational reading-frame maintenance. The enzyme is found in all eukaryotes and in some archaea, but not in bacteria. The eukaryotic enzyme is involved in the biosynthesis of wybutosine. Group: Enzymes. Synonyms: TYW3 (gene name); tRNA-yW synthesizing enzyme-3. Enzyme Commission Number: EC 2.1.1.282. 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-1889; tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase; EC 2.1.1.282; TYW3 (gene name); tRNA-yW synthesizing enzyme-3. Cat No: EXWM-1889. | |
| type I protein arginine methyltransferase | This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase. Group: Enzymes. Synonyms: PRMT1 (gene name); PRMT2 (gene name); PRMT3 (gene name); PRMT4 (gene name); PRMT6 (gene name); PRMT8 (gene name); RMT1 (gene name); CARM1 (gene name). Enzyme Commission Number: EC 2.1.1.319. 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-1927; type I protein arginine methyltransferase; EC 2.1.1.319; PRMT1 (gene name); PRMT2 (gene name); PRMT3 (gene name); PRMT4 (gene name); PRMT6 (gene name); PRMT8 (gene name); RMT1 (gene name); CARM1 (gene name). Cat No: EXWM-1927. | |
| UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminyltransferase | The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase). Group: Enzymes. Synonyms: aglK (gene name); dolichyl-phosphate α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase. Enzyme Commission Number: EC 2.4.1.153. CAS No. 63363-73-5. 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-2379; UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminyltransferase; EC 2.4.1.153; 63363-73-5; aglK (gene name); dolichyl-phosphate α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase. Cat No: EXWM-2379. | |
| 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. | |
| xenobiotic-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. The enzyme from Gram-positive bacteria and eukaryotic cells export a number of drugs, with unusual specificity, covering various groups of unrelated substances, while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them transport glutathione-drug conjugates. Some also show some 'flippase' (phospholipid-translocating ATPase; EC 3.6.3.1) activity. Group: Enzymes. Synonyms: multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting). Enzyme Commission Number: EC 7.6.2.2 (Formerly EC 3.6.3.44). 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-4683; xenobiotic-transporting ATPase; EC 3.6.3.44; multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting). Cat No: EXWM-4683. | |
| 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. | |
| 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. | |
| 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. | |
| 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. | |
| 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. Grades: ≥98% by HPLC. CAS No. 142557-61-7. Molecular formula: C13H15N5O3. Mole weight: 289.29. | |
| 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. | |
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