Neuraminidase C (NanC)
Product summary
Neuraminidase C (NanC) from Streptococcus pneumoniae selectively cleaves terminal α2-3-linked sialic acids with limited activity toward α2-6 linkages, releasing free sialic acid. Its mild, controlled desialylation makes it useful for glycoprotein/glycan structural analysis, biopharmaceutical desialylation, production of analytical sialic-acid standards, and enzymatic synthesis or modification of glycoconjugates
Product Description
Neuraminidase C (NanC) from Streptococcus pneumoniae is a sialidase enzyme that cleaves terminal sialic acid residues from glycoconjugates, but with narrower substrate specificity compared to NanA and NanB. NanC preferentially acts on α2-3-linked sialic acids and exhibits limited activity toward α2-6 linkages. It typically releases free sialic acid rather than cyclic products and is believed to function synergistically with other pneumococcal neuraminidases in modulating host-pathogen interactions. Due to its selective yet less aggressive desialylation profile, NanC is useful in applications requiring controlled removal of specific sialic acid linkages while preserving overall glycan structure integrity. (Ref).
Additonal Information
| Product Name | Sialidase C |
|---|---|
| Synonyms | Neuraminidase C, NanC. |
| Source (Organism/Expression) | Streptococcus pneumoniae, expressed in E. coli |
| UniProt | A0A182DW00 |
| Molecular Weight | 75 kDa (appears 70–100 kDa on SDS-PAGE) |
| Isoform / Subunit Structure | Amino acids 1–659 with C-terminal 6×His tag |
| Storage Buffer | 20 mM Tris-HCl, 100 mM NaCl, 10 % vol/vol glycerol, pH 7.5 |
| Concentration | 6.4 U/μL |
| Storage Conditions | −80 °C |
| Recommended Applications | glycoprotein and glycan structural analysis, removal of sialic acids in biopharmaceutical processing, production of analytical standards for sialic acid quantification, and enzymatic synthesis or modification of glycoconjugates. |
| 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. |
