| Identification | Back Directory | [Name]
ACETYLNEURAMINYL HYDROLASE | [CAS]
9001-67-6 | [Synonyms]
α(2→
SIALIDASE
SIALIDASE L
EC 3.2.1.18
IUB: 3.2.1.18
ALP Separator
NEURAMINIDASE
exo-α-sialidase
Neuraminidase B
Neuraminidase A
3) Neuraminidase
SIALIDASE TYPE X
SIALIDASE TYPE V
SIALIDASE TYPE VI
SIALIDASE TYPE II
Arylneuraminidase
SIALIDASE AGAROSE
SIALIDASE TYPE III
Neuraminidase， NRH
EC 3.2.1.18 TYPE V
EC 3.2.1.18 TYPE X
EC 3.2.1.18 TYPE VI
EC 3.2.1.18 TYPE II
alpha-neuraminidase
SIALIDASE TYPE VI-A
SIALIDASE TYPE VIII
Exo-alpha-sialidase
Acetylneuraminidase
α(2→3) NeuraMinidase
NEURAMINIDASE TYPE V
NEURAMINIDASE TYPE X
EC 3.2.1.18 TYPE III
EC 3.2.1.18 TYPE VI-A
EC 3.2.1.18 TYPE VIII
NEURAMINIDASE TYPE VI
NEURAMINIDASE TYPE II
N-Acetylneuraminidase
α(2→3,6) neuraminidase
NEURAMINIDASE TYPE III
ACYLNEURAMYL HYDROLASE
ALPHA2,3-NEURAMINIDASE
Neuraminidase,Purified
3,6,8,9) Neuraminidase
NEURAMINIDASE TYPE VI-A
NEURAMINIDASE TYPE VIII
ALPHA2-3,6-NEURAMINIDASE
ACYLNEURAMINYL HYDROLASE
ACETYLNEURAMINYL HYDROLASE
ALPHA2-3,6,8-NEURAMINIDASE
α(2→3,6,8,9) NeuraMinidase
N-Acylneuraminyl hydrolase
RECEPTOR-DESTROYING ENZYME
N-ACETYLNEURAMINYL HYDROLASE
ALPHA2-3,6,8,9-NEURAMINIDASE
ACYLNEURAMINYL HYDROLASE TYPE X
ACYLNEURAMINYL HYDROLASE TYPE V
ACYLNEURAMINYL HYDROLASE TYPE VI
ACYLNEURAMINYL HYDROLASE TYPE II
Neuraminidase from Microorganism
RECEPTOR DESTROYING ENZYME TYPE X
RECEPTOR DESTROYING ENZYME TYPE V
ACYLNEURAMINYL HYDROLASE TYPE III
ACYLNEURAMINYL HYDROLASE TYPE VI-A
ACYLNEURAMINYL HYDROLASE TYPE VIII
ACETYLNEURAMINYL HYDROLASE AGAROSE
neuraminidase from vibrio cholerae
RECEPTOR DESTROYING ENZYME TYPE VI
RECEPTOR DESTROYING ENZYME TYPE II
RECEPTOR DESTROYING ENZYME TYPE III
A(2-->3 6 8 9) NEURAMINIDASE FROM &
NeuraminidaseExVibrioComa(Cholerae)
NEURAMINIDASE FROM STREPTOCOCCUS SP.
RECEPTOR DESTROYING ENZYME TYPE VI-A
RECEPTOR DESTROYING ENZYME TYPE VIII
Native Vibrio cholerae Neuraminidase
ACETYLNEURAMINYL HYDROLASE USP/EP/BP
a2-3,6,8-Neuraminidase, Vibriocholerae
NEURAMINIDASE FROM CLOSTRIDIUM PERFRIN-&
NEURAMINIDASE, WIDE SPECTRUM, PROTEOMICS
NEURAMINIDASE FROM SALMONELLA &
neuraminidase from newcastle*disease virus
a2-3,6,8,9-Neuraminidase, Recomb., E. coli
ALPHA2,3-NEURAMINIDASE, MACROBDELLA DECORA
neuraminidase from arthrobacter*ureafaciens
neuraminidase from clostridium perfrin-gens
NEURAMINIDASE TYPE II FROM VIBRIO*CHOLER AE
Neuraminidase solution from Vibrio cholerae
ALPHA2-3,6,8-NEURAMINIDASE, VIBRIO CHOLERAE
Neuraminidase from vibrio cholerae, lyophil.
NEURAMINIDASE FROM VIBRIO CHOLERAE, ~2 U /ML
NEURAMINIDASE TYPE III FROM VIBRIO*CHOLE RAE
a2,3-Neuraminidase, Streptococcus pneumoniae
ALPHA2-3,6,8-NEURAMINIDASE, AGAROSE CONJUGATE
Parasite-derived mimic of neurotrophic factors
a2-3,6,8-Neuraminidase, Clostridium perfringens
a2,3-Neuraminidase, Macrobdella decora, Recomb.
Neuraminidase Clostridium perfringens (C.elchii)
A-2(3,6,8,9)-NEURAMINIDASE, EXPRESSED*IN E. COLI
neuraminidase type vi from clostridium*perfringen
neuraminidase type X from*clostridium perfringens
α(2→3) neuraminidase from streptococcus pneumoniae
NEURAMINIDASE TYPE V FROM CLOSTRIDIUM*PE RFRINGENS
NEURAMINIDASE TYPE VI FROM CLOSTRIDIUM*P ERFRINGENS
A-2(3,6)-NEURAMINIDASE, RECOMBINANT*EXPR ESSED IN E.
NEURAMINIDASE TYPE VIII FROM*CLOSTRIDIUM PERFRINGEN
A-2,3-NEURAMINIDASE, RECOMBINANT,*EXPRES SED IN E. C
NeuraMinidase froM ClostridiuM perfringens(Purified)
Sialidase 33A from Bacteroides fragilis, Recombinant
Native Streptococcus pneumoniae α (2→3) Neuraminidase
NEURAMINIDASE FROM CLOSTRIDIUM PERFRIN-G ENS, ~1 U/MG
neuraminidase from clostridium perfringens (c. welchii)
alpha(2->3) Neuraminidase from Streptococcus pneumoniae
Sialidase 33A from Clostridium perfringens, Recombinant
Sialidase 33A from Streptococcus pneumoniae, Recombinant
α(2→3,6,8,9) neuraminidase from arthrobacter ureafaciens
Native Arthrobacter ureafaciens α (2→3,6,8,9) Neuraminidase
a2-3,6,8,9-Neuraminidase, Arthrobacter ureafaciens, Recomb.
Neuraminidase from Arthrobacter ureafaciens, highly purified
NEURAMINIDASE F. CLOSTRIDIUM PERFRINGENS , >4 U/VIAL, 25 UG*
alpha(2->3,6,8,9) Neuraminidase from Arthrobacter ureafaciens
ALPHA2-3,6,8-NEURAMINIDASE, VIBRIO CHOLERAE, AGAROSE CONJUGATE
Neuraminidase from Salmonella enterica serotype typhimurium
Native Clostridium perfringens (C. welchii) Neuraminidase Agarose
Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase
Neuraminidase Agarose from Clostridium perfringens (C.welchii)
α2-3,6-Neuraminidase, Clostridium perfringens, Recombinant, E. coli
α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens, Recombinant
α2-3,6,8,9-Neuraminidase, Arthrobacter ureafaciens, Recombinant, E. coli
Acyl-neuraminyl Hydrolase, Neuraminidase from Arthrobacter ureafaciens, Sialidase
Acyl-neuraminyl Hydrolase, Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase
Neuraminidase from Vibrio cholerae,Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase
Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase, Neuraminidase from Clostridium perfringens (C.welchii) | [EINECS(EC#)]
232-624-6 | [Molecular Formula]
NULL | [MDL Number]
MFCD01092201 |
| Chemical Properties | Back Directory | [density ]
1.00 g/mL at 20 °C
| [storage temp. ]
2-8°C
| [form ]
lyophilized powder
| [color ]
white
| [biological source]
Vibrio cholerae | [Water Solubility ]
Soluble in water or 10mM phosphate buffer, pH 6.0 | [Specific Activity]
8-24units/mg protein (Lowry, using NAN-lactose) | [EPA Substance Registry System]
Neuraminidase (9001-67-6) |
| Safety Data | Back Directory | [Safety Statements ]
22-24/25 | [RIDADR ]
UN3373 - class 6.2 Biological substance, Category B | [WGK Germany ]
3
| [RTECS ]
QQ3450000
| [F ]
3-10 | [TSCA ]
Yes | [Storage Class]
11 - Combustible Solids | [Hazard Classifications]
Resp. Sens. 1 |
| Hazard Information | Back Directory | [Description]
Neuraminidase, also known as sialidase, is a family of glycosidases (EC 3.2.1.18) capable of hydrolysing terminal sialic acid residues on glycolipids, oligosaccharides and glycoproteins; this constitutes the first step in their degradation. Neuraminidases have been identified in a range of organisms, including viruses, protozoa, bacteria, fungi and vertebrates. The best-known neuraminidase is viral neuraminidase (viNEU), which is a drug target for preventing the spread of influenza infection. In mammals, four types of neuraminidase have been characterised: NEU1, NEU2, NEU3 and NEU4. | [Uses]
Neuraminidase from Vibrio cholera has been used in a study to describe a five-step purification method. It has also been used in a study to investigate modification of leukemia L1210 tumor cells. | [Uses]
Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α(2→6), α(2→3), α(2→8), and α(2→9) linkages (affinity in the order given). Branched sialic acids may also be cleaved with the use of high concentrations of enzyme and prolonged incubations. Desialylated glycoproteins may then be further characterized by treatment with various exoglycosidases resulting in partial or complete O-deglycosylation. SDS-PAGE and MALDI-TOF MS are typically utilized in purification, structural analysis, and sequencing process. These techniques also remove heterogeneity and charge from the glycoprotein. | [Uses]
Neuraminidase is used as a hydrolytic enzyme that removes sialic acid from mucoproteins, used in a study to assess binding with human T lymphocytes in sheep pretreated with neuraminidase. It has also been used in a study to investigate the effect of bile salts on the action of hydrolysis by neuraminidase. | [General Description]
Neuraminidase enzymes are glycoside hydrolase enzymes that catalyze hydrolysis of terminal sialic acid residues. The most well-known are the viral nearamidases, which promote influenza virus release. | [Biochem/physiol Actions]
Vibrio cholerae neuraminidase has been shown to promote cholera toxin infection by binding the toxin and aiding in its uptake by cells. | [References]
[1] Gatt, S, et al. “Effect of Bile Salts on the Hydrolysis of Gangliosides, Glycoproteins and Neuraminyl-Lactose by the Neuraminidase of Clostridium Perfringens.” Biochemical Journal, 193 1, 1981, pp. 267–73, https://doi.org/10.1042/bj1930267.
[2] Deman, J J, et al. “A Study on the Mechanism of Intercellular Adhesion. Effects of Neuraminidase, Calcium, and Trypsin on the Aggregation of Suspended HeLa Cells.” Journal of Cell Biology, 60 3, 1974, pp. 641–52, https://doi.org/10.1083/jcb.60.3.641.
[3] Weiner, Michael S., et al. “Enhanced Binding of Neuraminidase-Treated Sheep Erythrocytes to Human T Lymphocytes.” Blood, 42 6 1, 1973, pp. 939–46, https://doi.org/10.1182/BLOOD.V42.6.939.939. |
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Adamas Reagent, Ltd.
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| Telephone: |
4006009262 13023226327 |
| Website: |
http://www.tansoole.com |
| Company Name: |
Sigma-Aldrich
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021-61415566 800-8193336 |
| Website: |
https://www.sigmaaldrich.cn |
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