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| Product | Description | |
|---|---|---|
| glutamine synthetase | Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements. Group: Enzymes. Synonyms: glutamate-ammonia ligase; glutamylhydroxamic synthetase; L-glutamine synthetase; GS. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. 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-5722; glutamine synthetase; EC 6.3.1.2; 9023-70-5; glutamate-ammonia ligase; glutamylhydroxamic synthetase; L-glutamine synthetase; GS. Cat No: EXWM-5722. |  |
| Glutamine Synthetase from Human, recombinant | GLUL also known as Glutamine synthetase. It is a trimetallic enzyme containing two divalent cation sites and one monovalent cation site per subunit. GLUL is able to regulate intracellular concentrations of glutamate and catalyzes the synthesis of glutamine form glutamate and ammonia. It is ubiquitously expressed in the human and plays a major role for many metabolic pathways such as cell proliferation, inhibition of apoptosis, and cell signaling. Recombinant Human GLUL was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: > 85% by SDS-PAGE. GS. Mole weight: 42 kDa. Activity: > 2.000 pmol/min/ug. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Cat No: NATE-1675. | |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase). The two activities are present on separate domains. Group: Enzymes. Synonyms: adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Enzyme Commission Number: EC 2.7.7.89. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3302; [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; EC 2.7.7.89; adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Cat No: EXWM-3302. | |
| [glutamine synthetase] adenylyltransferase | This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase). The two activities are present on separate domains. Group: Enzymes. Synonyms: glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Enzyme Commission Number: EC 2.7.7.42. CAS No. 9077-66-1. 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-3254; [glutamine synthetase] adenylyltransferase; EC 2.7.7.42; 9077-66-1; glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Cat No: EXWM-3254. | |
| Native Bacillus sp. Glutamine synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Native glutamine synthetase (ec 6.3.1.2) was purified from bacillus sp. Applications: Useful for the determination of ammonia and atp in clinical analysis. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Activity: > 15 U/mg. Appearance: White to pale brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-155. | |
| Native Escherichia coli L-Glutamine Synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by Nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Applications: L-glutamine synthetase may be used for the purification of proteases from escherichia coli. Group: Enzymes. Synonyms: glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: affinity chromatography. GS. Activity: 400-2,000 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains potassium phosphate, sodium Citrate and magnesium acetate buffer salts. Source: Escherichia coli. glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Cat No: NATE-0321. | |
| Native Glutamine Synthetase from Microorganism | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Mole weight: ca. 900 kDa. Activity: > 7 U/mg lyophilizate. Appearance: Light yellow lyophilizate. Storage: at -20°C. Source: Microorganism. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-411. | |
| 4-methyleneglutamate-ammonia ligase | Glutamine can act instead of NH3, but more slowly. Group: Enzymes. Synonyms: 4-methyleneglutamine synthetase. Enzyme Commission Number: EC 6.3.1.7. CAS No. 85537-85-5. 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-5727; 4-methyleneglutamate-ammonia ligase; EC 6.3.1.7; 85537-85-5; 4-methyleneglutamine synthetase. Cat No: EXWM-5727. | |
| anthranilate synthase | In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only. Group: Enzymes. Synonyms: anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE. Enzyme Commission Number: EC 4.1.3.27. CAS No. 9031-59-8. 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-4907; anthranilate synthase; EC 4.1.3.27; 9031-59-8; anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE. Cat No: EXWM-4907. | |
| asparagine synthase (glutamine-hydrolysing) | The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a β-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine. Group: Enzymes. Synonyms: asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Enzyme Commission Number: EC 6.3.5.4. CAS No. 37318-72-2. 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-5807; asparagine synthase (glutamine-hydrolysing); EC 6.3.5.4; 37318-72-2; asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Cat No: EXWM-5807. | |
| aspartate-tRNAAsn ligase | When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate-tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNAAsp (GUC anticodon) and tRNAAsn (GUU anticodon). The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn. Group: Enzymes. Synonyms: nondiscriminating aspartyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.23. CAS No. 9027-32-1. 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-5655; aspartate-tRNAAsn ligase; EC 6.1.1.23; 9027-32-1; nondiscriminating aspartyl-tRNA synthetase. Cat No: EXWM-5655. | |
| carbamoyl-phosphate synthase (ammonia) | The enzyme catalyses the first committed step in the urea cycle. The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate. Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible. The enzyme requires the allosteric activator N-acetyl-L-glutamate. cf. EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing). Group: Enzymes. Synonyms: carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate s. Enzyme Commission Number: EC 6.3.4.16. CAS No. 9026-23-7. 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-5785; carbamoyl-phosphate synthase (ammonia); EC 6.3.4.16; 9026-23-7; carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate synthetase I; CPSI (gene name); carbon-dioxide:ammonia ligase (ADP-forming, carbamate-phosphorylating). Cat No: EXWM-5785. | |
| carbamoyl-phosphate synthase (glutamine-hydrolysing) | The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 ? in length. The amidotransferase domain within the small subunit of the enzyme hydrolyses glutamine to ammonia via a thioester intermediate. The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large ... (gene name); CAD (gene name); hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating). Enzyme Commission Number: EC 6.3.5.5. CAS No. 37233-48-0. 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-5808; carbamoyl-phosphate synthase (glutamine-hydrolysing); EC 6.3.5.5; 37233-48-0; carbamoyl-phosphate synthetase (glutamine-hydrolysing); carbamyl phosphate synthetase (glutamine); carbamoylphosphate synthetase II; glutamine-dependent carbamyl phosphate synthetase; carbamoyl phosphate synthetase; CPS; carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbam | |
| cobyrinate a,c-diamide synthase | This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyses the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source. It is proposed that the enzyme first catalyses the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate. The Km for ammonia is substantially higher than that for L-glutamine. Group: Enzymes. Synonyms: cobyrinic acid a,c-diamide synthetase; CbiA. Enzyme Commission Number: EC 6.3.5.11. 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-5804; cobyrinate a,c-diamide synthase; EC 6.3.5.11; cobyrinic acid a,c-diamide synthetase; CbiA. Cat No: EXWM-5804. | |
| CTP synthase (glutamine hydrolysing) | The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2, glutaminase), and the active site where CTP synthesis takes place. The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. Ammonia then reacts with this intermediate generating CTP and a phosphate. The enzyme can also use ammonia from the surrounding solution. Group: Enzymes. Synonyms: UTP-ammonia ligase; cytidine triphosphate synthetase; uridine triphosphate aminase; cytidine 5'-triphosphate synthetase; CTPS (gene name); pyrG (gene name); CTP synthase; UTP:ammonia ligase (ADP-forming). Enzyme Commission Number: EC 6.3.4.2. CAS No. 9023-56-7. 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-5789; CTP synthase (glutamine hydrolysing); EC 6.3.4.2; 9023-56-7; UTP-ammonia ligase; cytidine triphosphate synthetase; uridine triphosphate aminase; cytidine 5'-triphosphate synthetase; CTPS (gene name); pyrG (gene name); CTP synthase; UTP:ammonia ligase (ADP-forming). Cat No: EXWM-5789. | |
| D-Glutamine tert-Butyl Ester Hydrochloride | D-Glutamine tert-Butyl Ester Hydrochloride is a protected form of D-Glutamine. D-Glutamine is an unnatural isomer of L-Glutamine that is present in human plasma an is a source of liberated ammonia. D-Glutamine can be synthesized by enzymatic means or can be found in cheeses, wine and vinegars as well. It is often used to determine the activity of Glutamine synthetase, an enzyme that is commonly found in the mammalian liver and brain that controls the use of nitrogen in cells. Group: Biochemicals. Alternative Names: D-Glutamine 1,1-Dimethylethyl Ester Hydrochloride; (R)-2-Amino-4-carbamoylbutyric Acid tert-Butyl Ester Hydrochloride. Grades: Highly Purified. CAS No. 422324-35-4. Pack Sizes: 250mg, 500mg, 1g. Molecular Formula: C?H??ClN?O?, Molecular Weight: 238.71. US Biological Life Sciences. |  Worldwide |
| DL-a-Aminoadipic Acid | An alpha-amino acid that is adipic acid bearing a single amino substituent at position 2. An intermediate in the formation of lysine. A glutamine synthetase inhibitor. Group: Biochemicals. Alternative Names: DL-Aad-OH; DL-2-Aminohexanedioic acid; DL-Homoglutamic acid. Grades: Highly Purified. CAS No. 542-32-5. Pack Sizes: 5g, 25g. US Biological Life Sciences. | Worldwide |
| Duvakitug | Duvakitug is a humanized IgG1-λ2 monoclonal antibody targeting to TNFSF15 /TL1A. Duvakitug' main expression system is CHOK1SV cells endogenously expressing glutamine synthetase (GS). Duvakitug can be used in the study of Crohn's Disease (CD) [1] [2]. Uses: Scientific research. Group: Inhibitory antibodies. CAS No. 2750005-84-4. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P990006. |  |
| Glucokinase from Human, recombinant | Glucose is phosphorylated to glucose-6-phosphate by glucokinases. This gene is alternatively spliced to generate three different forms of the enzyme; one found in the pancreas and two found in the liver. The main function of this gene is to regulate carbohydrate metabolism. Recombinant human pancreatic Glucokinase has a C-terminal FLAG tag and has 470 amino acid residues. It can be useful for studies including enzyme kinetics, activator screening and kinase selectivity. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2; Hexokinase type IV; HK IV; Hexokinase-4; Hexokinase-D. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: > 80% by SDS-PAGE. GCK. Mole weight: 53.1 kDa. Activity: 303 pmol/min/ug. Storage: Store at -80°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human pancreatic. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Cat No: NATE-1686. | |
| glutamate-ethylamine ligase | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). Group: Enzymes. Synonyms: N5-ethyl-L-glutamine synthetase; theanine synthetase; N5-ethylglutamine synthetase. Enzyme Commission Number: EC 6.3.1.6. CAS No. 62213-31-4. 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-5726; glutamate-ethylamine ligase; EC 6.3.1.6; 62213-31-4; N5-ethyl-L-glutamine synthetase; theanine synthetase; N5-ethylglutamine synthetase. Cat No: EXWM-5726. | |
| glutamate synthase (NADPH) | Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction to that shown. The protein is composed of two subunits, α and &beta. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 ? channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit...mmission Number: EC 1.4.1.13. CAS No. 37213-53-9. 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-1446; glutamate synthase (NADPH); EC 1.4.1.13; 37213-53-9; glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT. Cat No: EXWM-1446. | |
| glutamate-tRNAGln ligase | When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate-tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln. Group: Enzymes. Synonyms: nondiscriminating glutamyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.24. CAS No. 9068-76-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5656; glutamate-tRNAGln ligase; EC 6.1.1.24; 9068-76-2; nondiscriminating glutamyl-tRNA synthetase. Cat No: EXWM-5656. | |
| glutamine-tRNA ligase | This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in glutamate metabolism and aminoacyl-trna biosynthesis. Group: Enzymes. Synonyms: glutaminyl-tRNA synthetase; glutaminyl-transfer RNA synthetase; glutaminyl-transfer ribonucleate synthetase; glutamine-tRNA synthetase; glutamine translase; glutamate-tRNA ligase; glutaminyl ribonucleic acid; GlnRS. Enzyme Commission Number: EC 6.1.1.18. CAS No. 9075-59-6. 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-5649; glutamine-tRNA ligase; EC 6.1.1.18; 9075-59-6; glutaminyl-tRNA synthetase; glutaminyl-transfer RNA synthetase; glutaminyl-transfer ribonucleate synthetase; glutamine-tRNA synthetase; glutamine translase; glutamate-tRNA ligase; glutaminyl ribonucleic acid; GlnRS. Cat No: EXWM-5649. | |
| Glutathione EP Impurity D | Glutathione EP Impurity D is a substrate used for the biosynthesis of L-glutathione by glutathione synthetase. It is used to study the active sites and kinetics of glutathione synthestase(s). It is also used in biological studies for the detection of thiols. Synonyms: γ-L-Glutamyl-L-cysteine; des-Gly-glutathione reduced form; γ-Glu-Cys; N-L-γ-glutamyl-; γ-Glutamylcysteine; N-(1-Carboxy-2-mercaptoethyl)-glutamine; L-gamma-Glutamyl-L-cysteine. Grades: > 95%. CAS No. 636-58-8. Molecular formula: C8H14N2O5S. Mole weight: 250.28. |  |
| GMP synthase (glutamine-hydrolysing) | Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia. Group: Enzymes. Synonyms: GMP synthetase (glutamine-hydrolysing); guanylate synthetase (glutamine-hydrolyzing); guanosine monophosphate synthetase (glutamine-hydrolyzing); xanthosine 5'-phosphate amidotransferase; guanosine 5'-monophosphate synthetase. Enzyme Commission Number: EC 6.3.5.2. CAS No. 37318-71-1. 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-5805; GMP synthase (glutamine-hydrolysing); EC 6.3.5.2; 37318-71-1; GMP synthetase (glutamine-hydrolysing); guanylate synthetase (glutamine-hydrolyzing); guanosine monophosphate synthetase (glutamine-hydrolyzing); xanthosine 5'-phosphate amidotransferase; guanosine 5'-monophosphate synthetase. Cat No: EXWM-5805. | |
| L-Asparagine monohydrate | Asparagine biosynthesis is catalyzed by glutamine-dependent asparagine synthetase in mammalian tissues. Elevated levels of free asparagine is observed in plants facing stress in the form of drought or high salt. It is also present in senescing leaves and germinating seeds. Uses: L-asparagine monohydrate has been used: as a component of sauton's and chelated sauton's media for mycobacterial growth to test its effect in the induction of ca2+ flux in rice roots using aequorin luminescence imaging as a component of fermentation medium for the blakeslea trispora spores. Additional or Alternative Names: (S)-(+)-2-Aminosuccinamic acid, (S)-2-Aminosuccinic acid 4-amide, L-Aspartic acid 4-amide. Product Category: Amino Acids. CAS No. 5794-13-8. Molecular formula: NH2COCH2CH(NH2)COOH · H2O. Mole weight: 150.13. Canonical SMILES: [H]O[H].N[C@@H](CC(N)=O)C(O)=O. ECNumber: 200-735-9. Product ID: ACM5794138. Alfa Chemistry ISO 9001:2015 Certified. |  |
| L- Buthionine Sulfoximine | A cell-permeable, sulfoximine based compound that acts a potent, fast acting, irreversible inhibitor of g-glutamylcysteine synthetase and depletes cellular glutathione levels. Closely resembles the structure of g-glutamylphosphate cysteine adduct. The inhibition follows the first order kinetics with t1/2 = ~11 sec at saturating inhibitor concentration. Does not affect the activity of glutamine synthetase. Shown to improve the outcome of chemotherapy by lowering the levels of glutathione in cancer cells (IC50 = 1.9, 8.6, and 29uM in melanoma, breast, and ovarian tumor cells, respectively). Group: Biochemicals. Grades: Highly Purified. CAS No. 83730-53-4. Pack Sizes: 100mg. Molecular Formula: C?H??N?O?S. US Biological Life Sciences. | Worldwide |
| L-Glufosinate | L-Glufosinate is a glutamine synthetase inhibitor and is used as a herbicide (usually as the corresponding ammonium or sodium salt, known as glufosinate-P-ammonium and glufosinate-P-sodium, respectively) to control annual weeds and grasses. Synonyms: Butanoic acid, 2-amino-4-(hydroxymethylphosphinyl)-, (2S)-; Glufosinate-P; (S)-Phosphinothricin; L-Phosphinothricin; (S)-Glufosinate; (+)-glufosinate; L-homoalanin-4-yl(methyl)phosphinic acid; 4-[hydroxy(methyl)phosphinoyl]-L-homoalanine; L-2-Amino-4-(hydroxymethylphosphinyl)butanoate-; (S)-2-Amino-4-(hydroxymethylphosphinyl)butyric acid. Grades: ≥95%. CAS No. 35597-44-5. Molecular formula: C5H12NO4P. Mole weight: 181.13. | |
| L-Methionine [R,S]-Sulfoximine | L-Methionine-(S,R)-sulfoximine is an inhibitor of glutamine synthetase and a sulfoximine derivative of L-methionine. Synonyms: L-Methionine Sulfoximine. CAS No. 15985-39-4. Molecular formula: C5H12N2O3S. Mole weight: 180.23. | |
| L-Methionine [R,S]-Sulfoximine | Methionine sulfoximine inhibits both glutamine synthetase and g-glutamylcysteine synthetase. Working concentrations for inhibition of g-glutamylcysteine synthetase are 0.2-2.0mM (52% inhibition occured at 100mM).Methionine sulfoximine is also a toxic byproduct of nitrogen trichloride, a compound that was used to bleach unprocessed wheat flour prior to 1968. The compound has been investigated as a potential neurotoxin linked to diseases such as amyotrophic lateral sclerosis (ALS) and Parkinsons disease. Group: Biochemicals. Alternative Names: L-S-[3-Amino-3-carboxypropyl]-S-methyl-[R,S]-sulfoximine; (2S) -2-Amino-4- (S-methylsulfonimidoyl) butanoic Acid. Grades: Highly Purified. CAS No. 15985-39-4. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C?H??N?O?S, Molecular Weight: 180.23. US Biological Life Sciences. | Worldwide |
| L-Methionine [S]-Sulfoximine | It is the diastereoisomer of L-Methionine [R,S]-Sulfoximine that inhibits glutamine synthetase. Group: Biochemicals. Alternative Names: (2S) -2-Amino-4- [ [S (S) ] -S-methylsulfonimidoyl] butanoic Acid; [S- (R*, R*) ]-2-Amino-4- (S-methylsulfonimidoyl) butanoic Acid; (S)-L-S-(3-amino-3-carboxypropyl)-S-methylsulfoximine. Grades: Highly Purified. CAS No. 21752-32-9. Pack Sizes: 50mg. US Biological Life Sciences. | Worldwide |
| Methionine sulfoximine | Methionine sulfoximine (2-Amino-4-(S-methylsulfonimidoyl)butanoic acid) is an irreversible inhibitor of glutamine synthetase with convulsive effects. Methionine sulfoximine is able to affect the metabolism of glutamate and glutamine, which may provide important insights in neurobiological research. Methionine sulfoximine has also been used to study mechanisms related to epilepsy and its inhibitory potential [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 2-Amino-4-(S-methylsulfonimidoyl)butanoic acid. CAS No. 1982-67-8. Pack Sizes: 5 mg; 10 mg. Product ID: HY-W338140. | |
| NAAD sodium | NAAD sodium (Deamido nad sodium), a functional NAD + precursor, is the substrate of glutamine-dependent NAD + synthetase. NAAD sodium is used to study the structure of nicotinate mononucleotide adenylyltransferases [1] [2]. Uses: Scientific research. Group: Natural products. Alternative Names: Deamido nad sodium. CAS No. 104809-30-5. Pack Sizes: 5 mg; 10 mg. Product ID: HY-117029. | |
| N-acetyldemethylphosphinothricin P-methyltransferase | The enzyme was originally characterized from bacteria that produce the tripeptides bialaphos and phosalacine, which inhibit plant and bacterial glutamine synthetases. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. According to the proposed mechanism, the reduced iron-sulfur center donates an electron to SAM, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical. This radical reacts with methylcob(III)alamin to produce the methylated product and cob...hosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively. This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature. Group: Enzymes. Synonyms: phpK (gene name); bcpD (gene name); P-methylase. Enzyme Commission Number: EC 2.1.1.326. 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-1934; N-acetyldemethylphosphinothricin P-methyltransferase; EC 2.1.1.326; phpK (gene name); bcpD (gene name); P-methylase. Cat No: EXWM-1934. | |
| N-Acetyl-L-Glutamic acid | N-Acety-L-Glutamic acid is a biologically active compound that is found in the cells. It is a product of the urea cycle and has been shown to inhibit the activity of enzymes such as ester hydrochloride synthetase, which catalyzes the conversion of arginine and citrulline to ornithine and carbamoyl phosphate. N-Acetylglutamic acid also plays an important role in cellular physiology, such as transcriptional regulation and protein synthesis. Deficiency can lead to glutamate accumulation and neurological disorders such as epilepsy. The biochemical properties of N-acetylglutamic acid are still not well known, but it has been shown to react with ammonia to form glutamine. CAS No. 1188-37-0. Product ID: PAP-0020. Molecular formula: C7H11NO5. Category: Amino acid. Product Keywords: Amino Acid Series; N-Acetyl-L-Glutamic acid; PAP-0020; Amino acid; C7H11NO5; 1188-37-0. Color: White. EC Number: 214-708-4. Physical State: Solid. Solubility: 36g/l (Lit.). Storage: 2-8°C. Applications: N-Acetyl-L-Glutamic acid is a product of the urea cycle and has been shown to inhibit the activity of enzymes such as ester hydrochloride synthetase, which catalyzes the conversion of arginine and citrulline to ornithine and carbamoyl phosphate. N-Acetylglutamic acid also plays an important role in cellular physiology, such as transcriptional regulation and protein synthesis. Deficiency can lead to glutamate accumulation and neurological |  |
| NAD+ synthase | L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1]. Group: Enzymes. Synonyms: NAD synthetase; NAD synthase; nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase. Enzyme Commission Number: EC 6.3.1.5. CAS No. 9032-69-3. NAD Synthetase. 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-5725; NAD+ synthase; EC 6.3.1.5; 9032-69-3; NAD synthetase; NAD synthase; nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase. Cat No: EXWM-5725. | |
| NAD+ synthase (glutamine-hydrolysing) | NH3 can act instead of glutamine (cf. EC 6.3.1.5 NAD+ synthase). Group: Enzymes. Synonyms: NAD synthetase (glutamine-hydrolysing); nicotinamide adenine dinucleotide synthetase (glutamine); desamidonicotinamide adenine dinucleotide amidotransferase; DPN synthetase. Enzyme Commission Number: EC 6.3.5.1. CAS No. 37318-70-0. 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-5802; NAD+ synthase (glutamine-hydrolysing); EC 6.3.5.1; 37318-70-0; NAD synthetase (glutamine-hydrolysing); nicotinamide adenine dinucleotide synthetase (glutamine); desamidonicotinamide adenine dinucleotide amidotransferase; DPN synthetase. Cat No: EXWM-5802. | |
| phosphinomethylmalate isomerase | The enzyme, characterized from the bacterium Streptomyces viridochromogenes, is involved in bialaphos biosynthesis. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase. The similar enzyme EC 4.2.1.3, aconitate hydratase, cannot catalyse this reaction. Group: Enzymes. Synonyms: pmi (gene name). Enzyme Commission Number: EC 4.2.1.166. 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-5007; phosphinomethylmalate isomerase; EC 4.2.1.166; pmi (gene name). Cat No: EXWM-5007. | |
| phosphonoformate cytidylyltransferase | The enzyme, characterized from the bacterium Streptomyces viridochromogenes, participates in the biosynthesis of the herbicide antibiotic bialaphos. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase. Group: Enzymes. Synonyms: phpF (gene name). Enzyme Commission Number: EC 2.7.7.93. 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-3307; phosphonoformate cytidylyltransferase; EC 2.7.7.93; phpF (gene name). Cat No: EXWM-3307. | |
| phosphoribosylformylglycinamidine synthase | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: phosphoribosylformylglycinamidine synthetase; formylglycinamide ribonucloetide amidotransferase; phosphoribosylformylglycineamidine synthetase; FGAM synthetase; FGAR amidotransferase; 5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase (ADP-forming); 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.3. CAS No. 9032-84-2. 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-5806; phosphoribosylformylglycinamidine synthase; EC 6.3.5.3; 9032-84-2; phosphoribosylformylglycinamidine synthetase; formylglycinamide ribonucloetide amidotransferase; phosphoribosylformylglycineamidine synthetase; FGAM synthetase; FGAR amidotransferase; 5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase (ADP-forming); 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5806. | |
| Temtokibart | Temtokibart is a humanized IgG1 λ2 antibody targeting IL22RA1. Expressed by cells lacking the glutamine synthetase gene. Uses: Scientific research. Group: Inhibitory antibodies. Alternative Names: ARGX-112. CAS No. 2639874-57-8. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P990016. | |
| 3-[(Aminocarbony)amino]-L-alanine | 3-[(Aminocarbony)amino]-L-alanine is a glutamase inhibitor, a glutaminyl-tRNA synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. It is also a potential effector group in affinity chromatography. Uses: Albizziin is a glutamase inhibitor, a glutaminyl-trna synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. it is also a potential effector group in affinity chromatography. Synonyms: L-Ala(ureido)-OH; L-Albizzine; L-(-)-2-Amino-3-uraeidopropionic acid; Albizziin; L-2-Amino-3-ureidopropionic acid; L-Alanine, 3-[(aminocarbonyl)amino]-; (2S)-2-amino-3-(carbamoylamino)propanoic acid. Grades: ≥ 99% (Titration). CAS No. 1483-07-4. Molecular formula: C4H9N3O3. Mole weight: 147.13. | |
| D-Albizziin (D-(-)-2-Amino-3-ureidopropionic Acid) | Albizziin is a glutamase inhibitor, a glutaminyl-tRNA synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. It is also a potential effector group in affinity chromatography. Group: Biochemicals. Alternative Names: D-(-)-2-Amino-3-ureidopropionic Acid. Grades: Highly Purified. Pack Sizes: 250mg. US Biological Life Sciences. | Worldwide |
| D-Albizziine | D-Albizziine is a glutamase inhibitor, a glutaminyl-tRNA synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. It is also a potential effector group in affinity chromatography. Uses: Albizziin is a glutamase inhibitor, a glutaminyl-trna synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. it is also a potential effector group in affinity chromatography. Synonyms: H-D-Alb-OH; H-D-Dap(2-Carbamoyl)-OH; N-β-carbamoyl-D-α,β-diaminopropionic acid. Grades: 98%. CAS No. 134053-09-1. Molecular formula: C4H9N3O3. Mole weight: 147.13. | |
| γ-glutamylhistamine synthase | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). Group: Enzymes. Synonyms: γ-glutaminylhistamine synthetase; γ-GHA synthetase. Enzyme Commission Number: EC 6.3.2.18. CAS No. 82904-08-3. 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-5738; γ-glutamylhistamine synthase; EC 6.3.2.18; 82904-08-3; γ-glutaminylhistamine synthetase; γ-GHA synthetase. Cat No: EXWM-5738. | |
| L-Albizziin (L-(-)-2-Amino-3-ureidopropionic Acid) | Albizziin is a glutamase inhibitor, a glutaminyl-tRNA synthetase inhibitor as well as an intermediate in the synthesis of heterocycles. It is also a potential effector group in affinity chromatography. Group: Biochemicals. Alternative Names: L-(-)-2-Amino-3-ureidopropionic Acid. Grades: Highly Purified. Pack Sizes: 100mg. US Biological Life Sciences. | Worldwide |
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