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| Product | Description | |
|---|---|---|
| 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. |  |
| 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. | |
| 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 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. | |
| 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 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. | |
| 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. | |
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