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| Product | Description | |
|---|---|---|
| β-Agarase I from E. coli, Recombinant | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Β-agarase cleaves the agarose subunit, unsubstituted...garase i can be used to purify both large (> 50 kb) and small (< 50 kb) fragments of dna from gels. the remaining carbohydrate molecules and β-agarase i will not, in general, interfere with subsequent dna manipulations such as restriction endonuclease digestion, ligation, and transformation. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Agarase. Storage: at -20°C. Form: 50 mM Bis Tris-HCl (pH 6.5), 1 mM Na2EDTA and 50% glycerol. Source: E. coli. Species: E. coli. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6; β-Agarase I. Cat No: NATE-1282. |  |
| FA2G1 N-Glycan | FA2G1 N-Glycan is a compound assuming a paramount role in the comprehensive exploration and comprehension of glycoproteins alongside their intricate functionalities. With its widespread employment as a research tool, this N-glycan holds the potential for the profound investigation of diverse maladies encompassing cancer, inflammation and hereditary disorders. Synonyms: Asialo, core fucosylated, bi-antennary N-linked glycan; NA2G1F N-Glycan. CAS No. 721918-59-8. Molecular formula: C62H104N4O45. Mole weight: 1625.49. |  |
| 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. | |
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