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| Product | Description | |
|---|---|---|
| 3-cyanoalanine hydratase | This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. This enzyme participates in cyanoamino acid metabolism. Group: Enzymes. Synonyms: β-cyanoalanine hydrolase; β-cyanoalanine hydratase; β-CNAla hydrolase; β-CNA nitrilase; L-asparagine hydro-lyase. Enzyme Commission Number: EC 4.2.1.65. CAS No. 37259-64-6. 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-5050; 3-cyanoalanine hydratase; EC 4.2.1.65; 37259-64-6; β-cyanoalanine hydrolase; β-cyanoalanine hydratase; β-CNAla hydrolase; β-CNA nitrilase; L-asparagine hydro-lyase. Cat No: EXWM-5050. |  |
| Ac-ESEN-MAC | Ac-ESEN-MAC is a synthetic peptide substrate for Vacuolar Processing Enzyme (VPE). Synonyms: Ac-ESEN-MCA; Ac-Glu-Ser-Glu-Asn-MCA; Ac-Glu-Ser-Glu-Asn-MAC; Acetyl-L-glutamyl-L-seryl-L-glutamyl-L-asparagine α-(4-methylcoumaryl-7-amide). CAS No. 896420-43-2. Molecular formula: C29H36N6O13. Mole weight: 676.63. |  |
| Asparaginase from E. coli, Recombinant | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Mole weight: ~ 37,900. Activity: ~ 15 U/mg. Stability: > 4 years at 4°C. Storage: 4°C. Form: In 2.5 M lithium sulphate. Source: E. coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: NATE-1932. | |
| asparagine-oxo-acid transaminase | A pyridoxal-phosphate protein. Group: Enzymes. Synonyms: asparagine-keto acid aminotransferase. Enzyme Commission Number: EC 2.6.1.14. CAS No. 9030-43-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2854; asparagine-oxo-acid transaminase; EC 2.6.1.14; 9030-43-7; asparagine-keto acid aminotransferase. Cat No: EXWM-2854. | |
| 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. | |
| asparagine-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 alanine and aspartate metabolism and aminoacyl-trna biosynthesis. Group: Enzymes. Synonyms: asparaginyl-tRNA synthetase; asparaginyl-transfer ribonucleate synthetase; asparaginyl transfer RNA synthetase; asparaginyl transfer ribonucleic acid synthetase; asparagyl-transfer RNA synthetase; asparagine translase. Enzyme Commission Number: EC 6.1.1.22. CAS No. 37211-76-0. 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-5654; asparagine-tRNA ligase; EC 6.1.1.22; 37211-76-0; asparaginyl-tRNA synthetase; asparaginyl-transfer ribonucleate synthetase; asparaginyl transfer RNA synthetase; asparaginyl transfer ribonucleic acid synthetase; asparagyl-transfer RNA synthetase; asparagine translase. Cat No: EXWM-5654. | |
| asparaginyl-tRNA synthase (glutamine-hydrolysing) | This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis. In the first step, a non-discriminating ligase (EC 6.1.1.23, aspartate-tRNAAsn ligase) mischarges tRNAAsn with aspartate, leading to the formation of Asp-tRNAAsn. The aspartyl-tRNAAsn is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNAAsn (aspartyl-tRNAAsp is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. Group: Enzymes. Synonyms: Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.6. CAS No. 37211-76-0. 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-5809; asparaginyl-tRNA synthase (glutamine-hydrolysing); EC 6.3.5.6; 37211-76-0; Asp-AdT; Asp-tRNAAsn amidotransferase; aspartyl-tRNAAsn amidotransferase; Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming); aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5809. | |
| aspartate-ammonia ligase | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases).This enzyme participates in 3 metabolic pathways: alanine and aspartate metabolism, cyanoamino acid metabolism, and nitrogen metabolism. Group: Enzymes. Synonyms: asparagine synthetase; L-asparagine synthetase. Enzyme Commission Number: EC 6.3.1.1. CAS No. 9023-69-2. 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-5712; aspartate-ammonia ligase; EC 6.3.1.1; 9023-69-2; asparagine synthetase; L-asparagine synthetase. Cat No: EXWM-5712. | |
| aspartate-ammonia ligase (ADP-forming) | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). This enzyme participates in nitrogen metabolism. Group: Enzymes. Synonyms: asparagine synthetase (ADP-forming); asparagine synthetase (adenosine diphosphate-forming). Enzyme Commission Number: EC 6.3.1.4. CAS No. 37318-61-9. 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-5724; aspartate-ammonia ligase (ADP-forming); EC 6.3.1.4; 37318-61-9; asparagine synthetase (ADP-forming); asparagine synthetase (adenosine diphosphate-forming). Cat No: EXWM-5724. | |
| cyanoalanine nitrilase | L-Asparagine is formed as an intermediate. cf. EC 4.2.1.65, 3-cyanoalanine hydratase and EC 3.5.1.1, asparaginase. Group: Enzymes. Synonyms: β-cyanoalanine nitrilase. Enzyme Commission Number: EC 3.5.5.4. CAS No. 85638-44-4. 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-4580; cyanoalanine nitrilase; EC 3.5.5.4; 85638-44-4; β-cyanoalanine nitrilase. Cat No: EXWM-4580. | |
| D-Asparagine | D-Asparagine (H-D-Asn-OH) is a competitive inhibitor of L-Asparagine hydrolysis with a K i value of 0.24 mM. D-Asparagine is a source of nitrogen for yeast strains. D-Asparagine is a good substrate for the external yeast asparaginase but is a poor substrate for the internal enzyme [1]. Uses: Scientific research. Group: Natural products. Alternative Names: H-D-Asn-OH. CAS No. 2058-58-4. Pack Sizes: 10 mM * 1 mL; 1 g. Product ID: HY-W010378. |  |
| D-aspartate ligase | This enzyme forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed. The enzyme belongs in the ATP-grasp protein superfamily. The enzyme is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates. In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13, aspartate racemase. Group: Enzymes. Synonyms: Aslfm; UDP-MurNAc-pentapeptide:D-aspartate ligase; D-aspartic acid-activating enzyme. Enzyme Commission Number: EC 6.3.1.12. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5715; D-aspartate ligase; EC 6.3.1.12; Aslfm; UDP-MurNAc-pentapeptide:D-aspartate ligase; D-aspartic acid-activating enzyme. Cat No: EXWM-5715. | |
| dolichyl-diphosphooligosaccharide-protein glycotransferase | Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram click here). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-aspa... oligopolysaccharidotransferase; STT3. Enzyme Commission Number: EC 2.4.99.18. CAS No. 75302-32-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2702; dolichyl-diphosphooligosaccharide-protein glycotransferase; EC 2.4.99.18; 75302-32-8; dolichyldiphosphooligosaccharide-protein glycosyltransferase; asparagine N-glycosyltransferase; dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase; dolichyl pyrophosphodiacetyl chitobiose-protein glycosyltransferase; oligomannosyltransferase; oligosaccharide transferase; dolichyldiphosphoryloligosaccharide-protein oligosaccharyl | |
| dolichyl-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. | |
| Endoglycosidase H from Streptomyces plicatus, Recombinant | The enzyme Endoglycosidase H is an enzyme with system name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase. It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins. It is used for research purposes to deglycosylate glycoproteins. Group: Enzymes. Synonyms: EC 3.2.1.96;. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Endo-β-N-acetylglucosaminidase. Storage: 2-8°C. Form: Type I, buffered aqueous solution, Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative; Type II, buffered aqueous solution, Solution in 20 mM Tris HCl, pH 7.5, containing 50 mM NaCl, 1 mM EDTA. Source: E. coli. Species: Streptomyces plicatus. EC 3.2.1.96; Endo H; β-N-Acetylglucosaminidase H; N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(14)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-&b | |
| Escherichia coli Asparaginase-polyethylene glycol | Asparaginase is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Asparaginase coupled to methoxy-polyethylene glycol, m.w. 5 kda, through secondary amine linkage. Group: Enzymes. Synonyms: PEG-Asparaginase; Asparaginase-polyethylene glycol. Asparaginase. Activity: ~70 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains PEG plus 5% Citrate buffer salts. Source: Escherichia coli. PEG-Asparaginase; Asparaginase-polyethylene glycol. Cat No: NATE-0538. | |
| Exoenzyme C3 from Clostridium botulinum, Recombinant | Exoenzyme C3 transferase is an ADP ribosyl transferase that selectively ribosylates RhoA, RhoB and RhoC proteins on asparagine residue 41, rendering them inactive. It has extremely low affinity for other members of the Rho family such as Cdc42 and Rac1 and does therefore not affect these GTPases. Hence, C3 transferase is a very potent and useful reagent to specifically block RhoA/B/C signaling. Applications: Inhibition of rho activity in vivo by microinjection or pinocyctic uptake into cells. inhibition of rho activity in vitro. Group: Enzymes. Synonyms: Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Purity: >80% by SDS-P...2, 200 mM NaCl, 5% sucrose and 1% dextran. In order to maintain high biological activity of the protein, it is recommended that the protein solution be supplemented with DTT to 1 mM, aliquoted into "experiment sized" amounts, snap frozen in liquid nitrogen and stored at -70°C. The protein is stable for 6 months if stored at -70° C. Storage: The protein should not be exposed to repeated freeze-thaw cycles. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year. Form: Lyophilized powder. Source: E. coli. Species: Clostridium botulinum. Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Cat No: NATE-0874. | |
| GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-&alph. Enzyme Commission Number: EC 2.4.1.132. CAS No. 81181-76-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2357; GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase; EC 2.4.1.132; 81181-76-2; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase. Cat No: EXWM-2357. | |
| GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1?4)-β-D-GlcNAc-(1?4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransfera. Enzyme Commission Number: EC 2.4.1.257. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2487; GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase; EC 2.4.1.257; GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1?3)-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase. Cat No: EXWM-2487. | |
| GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1?2) linkages to the nascent oligosaccharide. Group: Enzymes. Synonyms: ALG11; AL. Enzyme Commission Number: EC 2.4.1.131. CAS No. 74506-43-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2356; GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase; EC 2.4.1.131; 74506-43-7; ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man3GlcNAc2-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1?3)-[D-Man-α-(1?6)]-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase. Cat No: EXWM-2356. | |
| glutamin-(asparagin-)ase | The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase. Group: Enzymes. Synonyms: glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Enzyme Commission Number: EC 3.5.1.38. CAS No. 39335-03-0. 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-4426; glutamin-(asparagin-)ase; EC 3.5.1.38; 39335-03-0; glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Cat No: EXWM-4426. | |
| glutaminyl-tRNA synthase (glutamine-hydrolysing) | In systems lacking discernible glutamine-tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate-tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. Group: Enzymes. Synonyms: Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.7. CAS No. 52232-48-1. 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-5810; glutaminyl-tRNA synthase (glutamine-hydrolysing); EC 6.3.5.7; 52232-48-1; Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5810. | |
| glycine N-phenylacetyltransferase | Not identical with EC 2.3.1.13 (glycine N-acyltransferase).This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values. Group: Enzymes. Synonyms: arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Enzyme Commission Number: EC 2.3.1.192. 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-2135; glycine N-phenylacetyltransferase; EC 2.3.1.192; arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Cat No: EXWM-2135. | |
| glycoprotein 2-β-D-xylosyltransferase | Specific for N-linked oligosaccharides (N-glycans). Group: Enzymes. Synonyms: β1,2-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of 4-N-{N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?3)-[N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?6)]-β-D-mannosyl-(1?4)-N-acetyl-β-D-glucosaminyl-(1?4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase. Enzyme Commission Number: EC 2.4.2.38. CAS No. 141256-56-6. 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-2666; glycoprotein 2-β-D-xylosyltransferase; EC 2.4.2.38; 141256-56-6; β1,2-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of 4-N-{N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?3)-[N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?6)]-β-D-mannosyl-(1?4)-N-acetyl-β-D-glucosaminyl-(1?4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase. Cat No: EXWM-2666. | |
| glycoprotein 3-α-L-fucosyltransferase | Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-α-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-β-L-fucose to form an α1,3-linkage rather than an α1,6-linkage. The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea). Group: Enzymes. Synonyms: GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1?6GlcNAc)-Asn-peptide) α1?3-fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-. Enzyme Commission Number: EC 2.4.1.214. CAS No. 68247-53-0. α-fucosyltransferase. 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-2442; glycoprotein 3-α-L-fucosyltransferase; EC 2.4.1.214; 68247-53-0; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamin | |
| glycoprotein 6-α-L-fucosyltransferase | This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-α-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-β-L-fucose to form an α1,6-linkage rather than an α1,3-linkage. Group: Enzymes. Synonyms: GDP-fucose-glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1?6fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-link. Enzyme Commission Number: EC 2.4.1.68. CAS No. 9033-8-3. 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-2611; glycoprotein 6-α-L-fucosyltransferase; EC 2.4.1.68; 9033-08-3; GDP-fucose-glycoprotein fucosyltransferase; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1?6fucosyltransferase; GDP-L-fucose-glycoprotein fucosyltransferase; glycoprotein fucosyltransferase; guanosine diphosphofucose-glycoprotein fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of 4-N-{N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?3)-[N-acetyl-β-D-glucosaminyl-(1?2)-α-D-mannosyl-(1?6)]-β-D-mannosyl-(1?4)-N-acetyl-β-D-glucosaminyl- | |
| hypoxia-inducible factor-asparagine dioxygenase | Contains iron, and requires ascorbate. Catalyses hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-α, the α subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300. The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia. Group: Enzymes. Synonyms: HIF hydroxylase. Enzyme Commission Number: EC 1.14.11.30. 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-0648; hypoxia-inducible factor-asparagine dioxygenase; EC 1.14.11.30; HIF hydroxylase. Cat No: EXWM-0648. | |
| L-a-Asparagine,N-acetyl-L-tyrosyl-L-valyl-L-alanyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-(9ci) | L-a-Asparagine,N-acetyl-L-tyrosyl-L-valyl-L-alanyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-(9ci). Uses: Designed for use in research and industrial production. Additional or Alternative Names: Acetyl-YVAD-AMC, Ac-YVAD-AMC, Ac-Tyr-Val-Ala-Asp-AMC, A2452_SIGMA, AMC120, CID4337, CID 4337, ICE (CASPASE I) SUBSTRATE III, Ac-Tyr-Val-Ala-Asp-7-Amino-4-Methylcoumarin, IL-1 beta Converting Enzyme Fluorogenic Substrate, N-Acetyl-Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin, 149231-65-2. Product Category: Heterocyclic Organic Compound. Appearance: white powder. CAS No. 149231-65-2. Molecular formula: C33H39N5O10. Mole weight: 665.6903. Purity: 0.96. IUPACName: 3-[2-[[2-[[2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylbutanoyl]amino]propanoylamino]-4-[(4-methyl-2-oxochromen-7-yl)amino]-4-oxobutanoic acid. Canonical SMILES: CC1=CC(=O)OC2=C1C=CC(=C2)NC(=O)C(CC(=O)O)NC(=O)C(C)NC(=O)C(C(C)C)NC(=O)C(CC3=CC=C(C=C3)O)NC(=O)C. Density: 1.344 g/cm³. Product ID: ACM149231652. Alfa Chemistry ISO 9001:2015 Certified. |  |
| L-Asparaginase | Asparaginase is a hydrolytic enzyme that catalyzes the hydrolysis of asparagine to aspartic acid and is used for the treatment of acute lymphoblastic leukemia. Synonyms: L-ASNase; Asparaginase; L-Asparagine Amidohydrolase. Grade: ≥96% by RP-HPLC. CAS No. 9015-68-3. Molecular formula: C7H5NOS. Mole weight: 151.186. | |
| L-Asparaginase | L-Asparaginase (L-ASNase) is a deamidating enzyme that catalyses the hydrolysis of L-asparagine and L-glutamine, and can be used for the research of acute lymphoblastic leukemia. L-Asparaginase depletes L-asparagine from plasma resulting in inhibition of RNA and DNA synthesis with the subsequent blastic cell apoptosis [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: L-ASNase. CAS No. 9015-68-3. Pack Sizes: 1 mg; 5 mg; 10 mg; 25 mg. Product ID: HY-P1923. | |
| L-Asparaginase from Guinea pig, Recombinant | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Purity: >99% (SDS-PAGE). Asparaginase. Mole weight: ~63 kDa. Activity: > 1,400 IU/mg. Storage: at -80°C. Form: 25 mM Tris pH7.5, 500 mM NaCl, 2 mM DTT, 1 mM EDTA. Source: E. coli. Species: Guinea pig. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: NATE-1577. | |
| L-asparagine hydroxylase | Requires Fe2+. The enzyme is only able to hydroxylate free L-asparagine. It is not active toward D-asparagine. The β-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone. Group: Enzymes. Synonyms: L-asparagine 3-hydroxylase; AsnO. Enzyme Commission Number: EC 1.14.11.39. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0657; L-asparagine hydroxylase; EC 1.14.11.39; L-asparagine 3-hydroxylase; AsnO. Cat No: EXWM-0657. | |
| mannosylglycoprotein endo-β-mannosidase | The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further α-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the β-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum. Group: Enzymes. Synonyms: endo-β-mannosidase. Enzyme Commission Number: EC 3.2.1.152. CAS No. 141176-95-6. 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-3835; mannosylglycoprotein endo-β-mannosidase; EC 3.2.1.152; 141176-95-6; endo-β-mannosidase. Cat No: EXWM-3835. | |
| mannosyl-glycoprotein endo-β-N-acetylglucosaminidase | A group of related enzymes. Group: Enzymes. Synonyms: N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Endo-β-N-acetylglucosaminidase. 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-3959; mannosyl-glycoprotein endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 37278-88-9; N,N'-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1?4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H. Cat No: EXWM-3959. | |
| N4-(β-N-acetylglucosaminyl)-L-asparaginase | Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase]. Group: Enzymes. Synonyms: aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.26. CAS No. 9075-24-5. 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-4416; N4-(β-N-acetylglucosaminyl)-L-asparaginase; EC 3.5.1.26; 9075-24-5; aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase. Cat No: EXWM-4416. | |
| Native Almonds Glycopeptidase A | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Group: Enzymes. Synonyms: EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Activity: > 0.05 unit/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM Citrate-phosphate buffer, pH 5.0, and BSA. Source: Almonds. EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Cat No: NATE-0600. | |
| Native Elizabethkingia miricola PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. Group: Enzymes. Synonyms: glycopeptide N-glycosida. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: > 20,000 units/mg protein and > 5,000 units/ml. Stability: The product remains active for at least 12 months when stored properly. Exposure for several days to ambient temperatures will not reduce activity. Do Not Freeze. Storage: 2-8°C. Form: Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0602. | |
| Native Escherichia coli Asparaginase | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Applications: Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. asparaginase is used to reduce the formation of acrylamide in starchy food products. it is also used as a chemotherapy agent for acute lymphoblastic leukemia. product is from escherichia coli and is provided as a lyophilized powder containing sodium chloride. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Storage: 2-8°C. Form: lyophilized powder. Source: Escherichia coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: PHAM-226. | |
| Native Flavobacterium meningosepticum PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f is purified from flavobacterium meningosepticum (3) and it is free of proteases and endo f activities. the following reagents are supplied with this produ...osaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: 500,000 units/ml. Stability: Storage Conditions: 20 mM Tris-HCl, 50 mM NaCl, 5 mM Na2EDTA, 50% Glycerol, pH 7.5 25°C Heat Inactivation: 75°C for 10 min. Storage: Store at -20°C. Source: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0603. | |
| peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase | Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18. Group: Enzymes. Synonyms: glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. 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-4441; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; 83534-39-8; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F. Cat No: EXWM-4441. | |
| PNGase A from Oryza sativa (rice), Recombinant | PNGase A cleaves N-linked glycans from high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.PNGase A is a recombinant amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues. Group: Enzymes. Synonyms: N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Enzyme Commission Number: EC 3.5.1.52. Purity: > 95% pure as determined by SDS-PAGE. PNGase F. Mole weight: 63.8 kDa. Activity: 5,000 units/ml. Storage: 4°C. Form: Storage Conditions: 50 mM NaCl, 20 mM Tris-HCl, 5 mM EDTA, (pH 7.5 @ 25°C). Source: Pichia pastoris. Species: Oryza sativa (rice). N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Cat No: NATE-1941. | |
| PNGase F from Elizabethkingia meningoseptica, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. ...n 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5. Type III, buffered aqueous solution, Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: E. coli. Species: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Pack: PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on dox | |
| PNGase F from Elizabethkingia miricola, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Pngase f can be use to cleave n-glycans attached to proteins and antibodies. Group: Enzymes. Synonyms: glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycop. CAS No. 83534-39-8. Purity: >95% by SDS-PAGE gel. PNGase F. Stability: PNGase F retains >60% activity after left at room temperature for over 72 hours. Long term storage at - 20°C or below. Storage: Long term storage at -20°C or below. Form: 20 mM Tris pH8, 50% glycerol. Source: E. coli. Species: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-1286. | |
| PNGase F from Flavobacterium meningosepticum, Recombinant | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f, peptide n-glycosidase f, is a recombinantly expressed endoglycosidase from flavobacterium meningosepticum that cleaves the β-aspartylglucosami...cetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. CAS No. 83534-39-8. Purity: >95% by SDS-PAGE. PNGase F. Mole weight: 34,800 daltons (Apparent). Activity: >10 U/mg. Stability: 1 year. Storage: 2-8°C. Avoid multiple freeze/thaw cycles. Form: 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA. Source: E. coli. Species: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-1287. | |
| protein N-acetylglucosaminyltransferase | The acceptor is the asparagine residue in a sequence of the form Asn-Xaa-Thr or Asn-Xaa-Ser. Group: Enzymes. Synonyms: uridine diphosphoacetylglucosamine-protein acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase I. Enzyme Commission Number: EC 2.4.1.94. CAS No. 72319-34-7. 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-2633; protein N-acetylglucosaminyltransferase; EC 2.4.1.94; 72319-34-7; uridine diphosphoacetylglucosamine-protein acetylglucosaminyltransferase; uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase I. Cat No: EXWM-2633. | |
| UDP-N-acetylbacillosamine N-acetyltransferase | The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species and O-linked glycosylation of certain L-serine residues in Neisseria species. Group: Enzymes. Synonyms: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase; pglD (gene name). Enzyme Commission Number: EC 2.3.1.203. 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-2148; UDP-N-acetylbacillosamine N-acetyltransferase; EC 2.3.1.203; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase; pglD (gene name). Cat No: EXWM-2148. | |
| UDP-N-acetylbacillosamine transaminase | A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N'-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species and O-linked glycosylation of certain L-serine residues in Neisseria species. Group: Enzymes. Synonyms: uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase. Enzyme Commission Number: EC 2.6.1.34. CAS No. 37277-89-7. 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-2874; UDP-N-acetylbacillosamine transaminase; EC 2.6.1.34; 37277-89-7; uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase. Cat No: EXWM-2874. | |
| undecaprenyl-diphosphooligosaccharide-protein glycotransferase | A bacterial enzyme that has been isolated from Campylobacter jejuni and Campylobacter lari. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species. Group: Enzymes. Synonyms: PglB. Enzyme Commission Number: EC 2.4.99.19. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2703; undecaprenyl-diphosphooligosaccharide-protein glycotransferase; EC 2.4.99.19; PglB. Cat No: EXWM-2703. | |
| Abz-(Asn670,Leu671)-Amyloid β/A4 Protein Precursor770 (669-674)-EDDnp | Abz-(Asn670,Leu671)-Amyloid β/A4 Protein Precursor770 (669-674)-EDDnp is an intramolecularly quenched fluorescent substrate with the ortho-aminobenzoyl (Abz)/N-(2,4-dinitrophenyl)ethylenediamine (EDDnp) groups as the donor/acceptor pair. It corresponds to the Swedish-mutated (JMV2236) β-amyloid precursor protein (βAPP) sequence, which is targeted by β-secretase BACE (β-site APP-cleaving activity). It is more selectively cleaved by BACE1 and BACE2 than by cathepsin D, a disintegrin and metalloprotease 10 (ADAM10), tumor necrosis α-converting enzyme (TACE), presenilin-1 (PS1), or presenilin-2 (PS2). Synonyms: JMV2236; L-α-Glutamine, N-(2-aminobenzoyl)-L-valyl-L-asparaginyl-L-leucyl-L-α-aspartyl-L-alanyl-N-[2-[(2,4-dinitrophenyl)amino]ethyl]-; N-(2-Aminobenzoyl)-L-valyl-L-asparaginyl-L-leucyl-L-α-aspartyl-L-alanyl-N-{2-[(2,4-dinitrophenyl)amino]ethyl}-L-α-glutamine. Grade: ≥95%. CAS No. 1007306-20-8. Molecular formula: C42H58N12O16. Mole weight: 986.99. | |
| Ac-Glu-Asp(EDANS)-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Gly-Lys(DABCYL)-Glu-NH2 | Ac-Glu-Asp(EDANS)-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Gly-Lys(DABCYL)-Glu-NH2 is a sensitive fluorescent (FRET) peptide substrate for cathepsin D. This enzyme degrades extracellular matrix components and may promote the spread of tumor cells. High levels of active cathepsin D were found in senile plaques in the brains of Alzheimer's patients. Synonyms: L-α-Glutamine, N-acetyl-L-α-glutamyl-N-[2-[(5-sulfo-1-naphthalenyl)amino]ethyl]-L-asparaginyl-L-lysyl-L-prolyl-L-isoleucyl-L-leucyl-L-phenylalanyl-L-phenylalanyl-L-arginyl-L-leucylglycyl-N6-[4-[[4-(dimethylamino)phenyl]azo]benzoyl]-L-lysyl-; N-Acetyl-L-α-glutamyl-N-{2-[(5-sulfo-1-naphthyl)amino]ethyl}-L-asparaginyl-L-lysyl-L-prolyl-L-isoleucyl-L-leucyl-L-phenylalanyl-L-phenylalanyl-L-arginyl-L-leucylglycyl-N6-(4-{[4-(dimethylamino)phenyl]diazenyl}benzoyl)-L-lysyl-L-α-glutamine. Grade: ≥95%. CAS No. 400716-78-1. Molecular formula: C104H146N24O23S. Mole weight: 2132.52. | |
| asparaginase | Asparaginase, also known as crisantaspase, is an enzyme that is used as a medication and in food manufacturing. As a medication it is used to treat acute lymphoblastic leukemia (ALL), acute myeloid leukemia (AML), and non-Hodgkin's lymphoma. It is given by injection into a vein, muscle, or under the skin. A pegylated version is also available. In food manufacturing it is used to decrease the acrylamide. Group: Enzymes. Synonyms: asparaginase II; L-asparaginase; colaspase; elspar; leunase; crasnitin; α-asparaginase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. 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-4377; asparaginase; EC 3.5.1.1; 9015-68-3; asparaginase II; L-asparaginase; colaspase; elspar; leunase; crasnitin; α-asparaginase. Cat No: EXWM-4377. | |
| 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. | |
| Dynorphin (1-17) | Dynorphin A is a heptadecapeptide derived from the cleavage of prodynorphin and found widely distributed in the central nervous system. It acts as an endogenous kappa receptor agonist with nanomolar binding affinity. It also activates the human novel opioid receptor-like receptor of ORL1. It is resistant to enzymatic degradation and may have antinociceptive functions. Uses: Neurotransmitter agents. Synonyms: Dynorphin A (swine); Dynorphin A (pig); 1-17-Dynorphin; L-Glutamine, L-tyrosylglycylglycyl-L-phenylalanyl-L-leucyl-L-arginyl-L-arginyl-L-isoleucyl-L-arginyl-L-prolyl-L-lysyl-L-leucyl-L-lysyl-L-tryptophyl-L-α-aspartyl-L-asparaginyl-; Dyn-A17; Dynorphin 17; Dynorphin A; Dynorphin A (1-17); Dynorphin A (human); Dynorphin A (porcine); Dynorphin A (rat); Dynorphin A 1-17; Dynorphin-A (Bos taurus); Porcine dynorphin (1-17); Porcine dynorphin A (1-17); Proteins, Dyn-A17; Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln. Grade: ≥95%. CAS No. 80448-90-4. Molecular formula: C99H155N31O23. Mole weight: 2147.51. | |
| Dynorphin A acetate | Dynorphin A acetate is a heptadecapeptide derived from the cleavage of prodynorphin and found widely distributed in the central nervous system. It acts as an endogenous kappa receptor agonist with nanomolar binding affinity. It also activates the human novel opioid receptor-like receptor of ORL1. It is resistant to enzymatic degradation and may have antinociceptive functions. Synonyms: Dynorphin (1-17) acetate; Dynorphin A (human, pig, rat, Bos taurus) acetate; Porcine dynorphin (1-17) acetate; L-Glutamine, L-tyrosylglycylglycyl-L-phenylalanyl-L-leucyl-L-arginyl-L-arginyl-L-isoleucyl-L-arginyl-L-prolyl-L-lysyl-L-leucyl-L-lysyl-L-tryptophyl-L-α-aspartyl-L-asparaginyl-, acetate; H-Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-OH.CH3CO2H. Grade: ≥95%. Molecular formula: C101H159N31O25. Mole weight: 2207.58. | |
| Immobilized TLCK-Chymotrypsin on F7m | α-chymotrypsin hydrolyzes peptides, amides, and esters preferentially at the carboxyl groups of hydrophobic amino acids (L-tyrosine, L-phenylalanine, and L-tryptophan but also bonds of leucyl, methionyl, asparaginyl, and glutamyl residues). F7m: 1. 0 mg α-chymotrypsin per CR-column immobilized on polyvinyl. 55 units immobilized per CR-columnNr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 5 Reaction buffer: 50 mM Tris/HCl, pH 7. 5; also active in 0.1% SDSNr. 6 Washing buffer: 50 mM Tris/HCl, 1 M NaCl, pH 7. 5. Group: Enzymes. Synonyms: EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3. 4. 21. 1. Storage: 4 °C. Source: Bovine pancreas. EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; Immobilized TLCK-Chymotrypsin; Immobilized Chymotrypsin; TLCK-Chymotrypsin. Cat No: NATE-1769. | |
| Immobilized TLCK-Chymotrypsin on G3m | α-chymotrypsin hydrolyzes peptides, amides, and esters preferentially at the carboxyl groups of hydrophobic amino acids (L-tyrosine, L-phenylalanine, and L-tryptophan but also bonds of leucyl, methionyl, asparaginyl, and glutamyl residues). G3m: 25 ug α-chymotrypsin per CR-column immobilized on dextran. 1. 4 units immobilized per CR-column. This CR-column cuts at least 100 ug tubulin per application; it cuts 5 ug/minuteBSA without SDS, but at least 45 ug/minute BSA in the presence of 0.1% SDS. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 5 Reaction buffer: 50 mM Tris/HCl, pH 7. 5; also active in 0.1% SDSNr. 6 Washing buffer: 50 mM Tris/HCl, 1 M NaCl, pH 7. 5. Group: Enzymes. Synonyms: EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3. 4. 21. 1. Storage: 4 °C. Source: Bovine pancreas. EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; Immobilized TLCK-Chymotrypsin; Immobilized Chymotrypsin; TLCK-Chymotrypsin. Cat No: NATE-1770. | |
| legumain | Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13. Group: Enzymes. Synonyms: asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Enzyme Commission Number: EC 3.4.22.34. CAS No. 149371-18-6. 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-4209; legumain; EC 3.4.22.34; 149371-18-6; asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Cat No: EXWM-4209. | |
| Native Elizabethkingia meningoseptica PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. proteomics grade pngase f has been extensively purified and lyophilized from dilute potassium phosphate buffer to prod...eptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. Purity: > 95% (SDS-PAGE). PNGase F. Mole weight: ~36 kDa. Storage: 2-8°C. Source: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0601. | |
| Z-Ala-Ala-Asn-AMC | Z-Ala-Ala-Asn-AMC is a standard substrate for legumain (EC 3.4.22.34) originally used for plant enzymes, and later found in mammalian form. Legumain may be a physiologic local regulator of human osteoclast (OCL) activity and may negatively regulate OCL. Synonyms: Z-AAN-AMC; L-Aspartamide, N-[(phenylmethoxy)carbonyl]-L-alanyl-L-alanyl-N1-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-; Benzyloxycarbonyl-Ala-Ala-Asn-4-methyl-7-coumarylamide; Benzyloxycarbonylalanyl-alanyl-asparaginyl-4-methyl-7-coumarylamide. Grade: 95%. CAS No. 149697-16-5. Molecular formula: C28H31N5O8. Mole weight: 565.57. | |
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