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Principaux documents

N2876

Sigma-Aldrich

Neuraminidase from Clostridium perfringens (C. welchii)

Suitable for manufacturing of diagnostic kits and reagents, Type V, lyophilized powder

Synonyme(s) :

Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
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Niveau de qualité

Type

Type V

Forme

lyophilized powder

Activité spécifique

≥0.1 units/mg solid (using mucin)
≥1.3 units/mg solid (using 4MU-NANA)

Application(s)

diagnostic assay manufacturing

Activité étrangère

Protease and NAN-aldolase, present

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

Clostridium perfringens str. 13 ... nanI(988807)

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Description générale

Neuraminidase enzymes are hydrolase enzymes that promote influenza virus release from infected cells and facilitate virus spread.

Application

Neuraminidase from Clostridium perfringens has been used in a study to assess binding with human T lymphocytes in sheep pretreated with neuraminidase. [1] It has also been used in a study to investigate the effect of bile salts on the action of hydrolysis by neuraminidase. [2]

Actions biochimiques/physiologiques

Neuraminidase can increase aggregation in certain cell lines by removing exposed negatively charged sialic acid residues on the cell surface. [3]
Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods.
Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-linked to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 linked sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 linked residues.
The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C.

Définition de l'unité

One unit will liberate 1.0 micromole of N-acetyl neuraminic acid per minute at pH 5.0 at 37 °C using bovine submaxillary mucin.

One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl)-a-D-N-actetylneuraminic acid per minute at pH 5.0 at 37 °C (using 4MU-NANA as a substrate)

Notes préparatoires

Prepared by salt fractionation.

Remarque sur l'analyse

Package sizes based on 4MU-NANA units
Package sizes based on the 4MU-NANA units

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Enhanced binding of neuraminidase-treated sheep erythrocytes to human T lymphocytes.
M S Weiner et al.
Blood, 42(6), 939-946 (1973-12-01)
Randa Bittar et al.
Practical laboratory medicine, 18, e00150-e00150 (2020-01-08)
A qualitative, semi-automatized method for apolipoprotein E (apoE) phenotyping by isoelectric focusing method has been evaluated on 40 serum samples from patients previously genotyped for apoE, especially as regards concordance with genotyping, but also repeatability and reproducibility of the method
J J Deman et al.
The Journal of cell biology, 60(3), 641-652 (1974-03-01)
Aggregation of suspended HeLa cells is increased on removal of cell surface sialic acid. Calcium ions promote aggregation whereas magnesium ions have no effect. The calcium effect is abolished by previous treatment of the cells with neuraminidase. Trypsinization of the
S Gatt et al.
The Biochemical journal, 193(1), 267-273 (1981-01-01)
Studies were done on the effect of bile salts on the rates of hydrolysis of the N-acetylneuraminyl linkages of several sialic acid-containing compounds by the neuraminidase of Clostridium perfringens. When GM3-ganglioside, two glycolipids (glycophorin and orosomucoid) and neuraminyl-lactose were used
Bessi Qorri et al.
Drug design, development and therapy, 14, 4149-4167 (2020-10-30)
Aspirin (acetylsalicylic acid) and celecoxib have been used as potential anti-cancer therapies. Aspirin exerts its therapeutic effect in both cyclooxygenase (COX)-dependent and -independent pathways to reduce tumor growth and disable tumorigenesis. Celecoxib, a selective cyclooxygenase-2 (COX-2) inhibitor, reduces factors that

Articles

Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.

Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.

Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.

Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.

Protocoles

Enzymatic Assay of Neuraminidase applies to products that have a specification for neuraminidase content by enzymatic determination.

Contenu apparenté

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

Questions

1–4 of 4 Questions  
  1. What should I use to dilute this product?

    1 answer
    1. For assay purposes, this product is reconstituted at 0.02 - 0.04 u/mL in water containing 0.2% bovine serum albumin (BSA). The enzyme may also be prepared as follows:
      Water containing 0.2% BSA at 2 mg/mL yielding a clear tan or brown solution
      10 mM phosphate buffer, pH 6, containing 25 to 150 mM KCl at 120ug/mL. This stock solution may be stored refrigerated for several months.

      Helpful?

  2. Does this enzyme cleave Neu5Gc?

    1 answer
    1. Product N2876, Neuraminidase, will cleave α2-3, α2-6, and α2-8 glycosidic linkages. Neu5Gc are mostly found terminally on glycan chains of glycoproteins and glycolipids. They are commonly linked via an α2-3 or α2-6 linkage to Gal, an α2-6 linkage to GalNAc, or via an α2-8 linkage to another sialic acid.

      Helpful?

  3. What is the gene sequence for this product?

    1 answer
    1. See the link below to review the gene information of Clostridium perfringens str. 13 nanI(988807) on NCBI:
      https://www.ncbi.nlm.nih.gov/gene/988807

      The specific sequence of the orgnism use in the production of this product is considered proprietary.

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  4. How should lyophilized neuraminidase be resuspended for storage in aqueous form? I plan to introduce it to cell culture.

    1 answer
    1. The recommendation is to dissolve in water containing 0.2% BSA (albumin) at 2 mg/mL. This will yield a clear tan or brown solution. Neuraminidase is a comparatively stable enzyme in solution. When dissolved at 120 µg/mL in 10 mM phosphate buffer, pH 6, containing 25 to 150 mM KCl, the enzyme retained activity at 0-4 C for over 30 months. At a concentration of 2 µg/mL under the same conditions, activity was lost unless albumin (BSA) was added.

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