Neuraminidase A (NanA)

Product summary

Neuraminidase A (NanA) from Streptococcus pneumoniae cleaves terminal α2-3 and α2-6 sialic acids from glycoconjugates, exposing underlying sugars. It is used for glycoprotein/glycan analysis, biopharmaceutical desialylation, and enzymatic synthesis or modification of glycoconjugates.

Product Description

Neuraminidase A (NanA) from Streptococcus pneumoniae is an enzyme that catalyzes the hydrolysis of terminal sialic acid residues from glycoproteins, glycolipids, and oligosaccharides. It acts specifically on α-ketosidic linkages of sialic acids, releasing free sialic acid and exposing underlying sugar residues. NanA efficiently cleaves both α2-3 and α2-6 linkages, making it useful for broad desialylation applications.(Ref).

Additonal Information

Product Name

Sialidase A

Synonyms

Neuraminidase A, NanA.

Source (Organism/Expression)

Streptococcus pneumoniae, expressed in E. coli

UniProt

P62575

Molecular Weight

86 kDa (appears 70–100 kDa on SDS-PAGE)

Isoform / Subunit Structure

Amino acids 122–883 with C-terminal 6×His tag

Storage Buffer

20 mM Tris-HCl, 100 mM NaCl, 10 % vol/vol glycerol, pH 7.5

Concentration

7.3 U/μL

Storage Conditions

−80 °C

Catalogue Number

Purity

>95% by SDS-PAGE (see Figure 1)

Enzyme Activity Definition

1 unit (U) of enzyme activity is the amount of enzyme that catalyzes the conversion of 1 µmol of 4-Methylumbelliferyl-N-acetyl-α-D-neuraminic acid (4-MUNANA) per minute under specified assay conditions specified as follows: -Buffer: 66mM MES, 8mM CaCl2, 25 mM Na2CO3, pH 6.5.
-Temperature 37° C.
-[4-MUNANA] = 75 µM

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