To order chemicals, medical devices, or other restricted products please provide ID that includes your business name & shipping address via email [email protected] or fax 484.881.5997 referencing your VWR account number. Acceptable forms of ID are:
- • State issued document with your organization's Federal Tax ID Number
- • State issued document with your organization's Resale Tax ID Number
- • City or County issued Business License
- • State Department of Health Services License
- • Any other ID issued by the State that includes the business name & address
* ATTN: California Customers may require additional documentation as part of the CA Health & Safety Code. Products that fall under this regulation will be placed on a mandatory 21-day hold after documentation is received. Avantor will not lift restrictions for residential shipping addresses.
Specifications
- Source:E. coli
- Species:Arthrobacter ureafaciens
- Size:200 µl (1 U)
- Enzyme Name:Sialidase
- Enzyme Activity:40 units/mg
- Molecular Weight:~88 kD
- Concentration:5 U/ml
- Formulation:20 mM Tris HCl pH 7.5, containing 25 mM NaCl
- Cat. No.:AGGK80040
Specifications
About this item
The enzyme releases Alpha (2,3)-, Alpha (2,6)-, Alpha (2,8)-, and Alpha (2,9)-linked N-acetylneuraminic acid from oligosaccharides and glycoproteins. It is also capable of releasing N-glycolylneuraminic acid.
- pH Optimum: 6
- Unit definition: One unit is defined as the amount of enzyme required to catalyze the release of 1 µmole of p-nitrophenol from p-nitrophenyl-α-D-N-acetylneuraminic acid per minute at 37° C, pH 5.5.
Break the glycosidic bonds at the terminal residue, and enable glycoanalysis studies
These enzymes are useful in the study of isolated glycans, glycolipids, glycoproteins, or sequencing studies, especially when used in combination.
Agilent Exoglycosidases (formerly ProZyme) are glycoside hydrolase enzymes that cleave the glycosidic bonds at the terminal residues. These enzymes are useful in the study of isolated glycans, glycolipids, glycoproteins. Linkage-specific exoglycosidases may also be used for sequencing of oligosaccharides. When used in combination, exoglycosidases enable flexible analytical tools for glycan analysis.
Source: Recombinant gene from Arthrobacter ureafaciens, expressed in E. coli. Sialidases are also known as neuraminidases.
Specificity: The enzyme releases a(2,3)-, a(2,6)-, a(2,8)-, and a(2,9)-linked N-acetylneuraminic acid from complex carbohydrates. The initial rate of hydrolysis of a(2,6) linkages is reported to be approximately twice that of a(2,3)-linked sialic acid however, in practice, this kinetic selectivity is of little consequence during extended incubations. Effective digestion of glycolipid substrates is facilitated by addition of a detergent, such as sodium taurodeoxycholate to the incubation. Sialidase A is capable of releasing N-glycolylneuraminic acid (Neu5Gc, NGNA) in addition to N-acetylneuraminic acid (Neu5Ac, NANA) [1], although similarly to other sialidases [2] the activity is lower toward Neu5Gc than Neu5Ac. The enzyme can also be used to remove sialic acid from gangliosides [3], glycosphingolipids (ceramide and oligosaccharide) with sialic acid. May be used for exoglycosidase sequencing with Sialidase S (GK80021), which is specific for a(2,3)-linked sialic acids. Sialidases are also known as neuraminidase.