Neuraminidase derived from arthrobacter ureafaciens

Manufactured by Nacalai Tesque

Sourced in Japan

Neuraminidase derived from Arthrobacter ureafaciens is an enzyme that catalyzes the removal of terminal sialic acid residues from glycoconjugates. It functions by hydrolyzing the glycosidic linkages between sialic acid and adjacent sugar residues.

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Lab products found in correlation

Tskgel deae 5pw, by Tosoh (1 mentions)

2 protocols using neuraminidase derived from arthrobacter ureafaciens

Glycan Analysis Using Enzymatic Digestion

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Anhydrous hydrazine was purchased from Tokyo Chemical Industry (Tokyo, Japan), 2-aminopyridine was from Kanto Chemical (Tokyo, Japan), and dimethylamine borane was from Wako (Osaka, Japan). Graphite carbon columns (GL-Pak carbograph, Cat. No. 5010–23005) were purchased from GL Science (Tokyo, Japan). Cellulose cartridge columns were from Takara Bio (Cat. No. 4404; Otsu, Japan) and GL Science (Cat. No. 5010–11130). Microgranular cellulose for packed cellulose columns was from Sigma (St. Louis, MO, USA). Neuraminidase derived from Arthrobacter ureafaciens was purchased from Nacalai Tesque (Kyoto, Japan). α2,3-sialidase, specific for α(2-3)-NeuAc, was from New England BioLabs (Ipswich, MA, USA). Pyridylaminated (PA)-sugar chains used as a standard were purchased from Takara Bio and Seikagaku Corporation (Tokyo, Japan).

Torii T., Yoshimura T., Narumi M., Hitoshi S., Takaki Y., Tsuji S, & Ikenaka K. (2014). Determination of major sialylated N-glycans and identification of branched sialylated N-glycans that dynamically change their content during development in the mouse cerebral cortex. Glycoconjugate Journal, 31(9), 671-683.

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Desialylation and Separation of N-glycans

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Desialylation of N-glycans was performed as described previously (Torii et al., 2014; Yoshimura et al., 2012 Yoshimura et al., , 2017)) . Purified pyridylaminated (PA)-N-glycans were treated with neuraminidase derived from Arthrobacter ureafaciens (Nacalai Tesque, Kyoto, Japan) at 37°C for 14 h to cleave sialic acids, followed by heating at 100°C for 5 min and filtering through a 0.20 μm spin filter (Ultrafree-MC LG, Merck Millipore). To separate neutral Nglycans from acidic ones, PA-N-glycans were passed through an anion exchange DEAE column (TSKgel DEAE-5PW, Tosoh, Tokyo, Japan) using HPLC or a Microgranular DE52-packed column (Whatman, GE Healthcare). Water adjusted to pH 9.0 with ammonia was used as a mobile solvent. Neutral N-glycans were collected in the non-adsorbed fraction.

Handa-Narumi M., Yoshimura T., Konishi H., Fukata Y., Manabe Y., Tanaka K., Bao G.M., Kiyama H., Fukase K, & Ikenaka K. (2018). Branched Sialylated N-glycans Are Accumulated in Brain Synaptosomes and Interact with Siglec-H. Cell structure and function, 43(2).

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