Recombinant C. perfringens Neuraminidase Protein, CF

R&D Systems | Catalog # 5080-NM

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Key Product Details

  • R&D Systems E. coli-derived Recombinant C. perfringens Neuraminidase Protein (5080-NM)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

P10481

Applications

Enzyme Activity
View all Bacterial Neuraminidase Proteins and Enzymes »

Product Specifications

Source

E. coli-derived c. perfringens Bacterial Neuraminidase protein
Cys2-Gln382, with an N-terminal Met and 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

44 kDa

SDS-PAGE

40 kDa, reducing conditions

Activity

Measured by its ability to cleave a fluorogenic substrate, 2’-(4-Methylumbelliferyl)-alpha -D-N-acetylneuraminic acid.
The specific activity is >80,000 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation, and Storage

5080-NM
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and EDTA.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Bacterial Neuraminidase

Neuraminidase and Sialidase are the common names for N‑acetyl‑neuraminyl hydrolase (1-3). The enzyme catalyzes the hydrolysis of alpha 2-3 and alpha 2-6 linked N‑acetyl‑neuraminic acid residues from glycoproteins and glycolipids. It has little activity against the alpha 2-8 linked N‑acetyl‑neuraminic acid residues.

References

  1. Christensen, S. et al. (2005) Biotechnol. Appl. Biochem. 41:225.
  2. Roggentin, P. et al. (1988) FEBS Lett. 238:31.
  3. Corfield, A. et al. (1983) Biochim. Biophys. Acta 744:121.

UniProt

P10481 (C. perfringens)

Additional Bacterial Neuraminidase Products

Product Documents for Recombinant C. perfringens Neuraminidase Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

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Product Specific Notices for Recombinant C. perfringens Neuraminidase Protein, CF

For research use only

Related Research Areas

Glycobiology-related Enzymes

Citations for Recombinant C. perfringens Neuraminidase Protein, CF

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Protocols

View specific protocols for Recombinant C. perfringens Neuraminidase Protein, CF (5080-NM):

Materials
  • Assay Buffer: 50 mM MES, 100 mM NaCl, 0.05% (w/v) Brij-35, pH 6.5
  • Recombinant C. perfringens Neuraminidase (rCpNA) (Catalog # 5080-NM)
  • Substrate: 2’-(4-Methylumbelliferyl)-alpha -D-N-acetylneuraminic acid (Sigma, Catalog # M8639), 10 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rCpNA to 0.04 ng/µL in Assay Buffer.
  2. Dilute Substrate to 400 µM in Assay Buffer.
  3. Load 50 µL of 0.04 ng/µL rCpNA into a plate, and start the reaction by adding 50 µL of 400 µM Substrate.
  4. Read at excitation and emission wavelengths of 365 nm and 445 nm (top read), respectively in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmoles/min/µg) =

 Adjusted Vmax* (RFU/min) x Conversion Factor** (pmole/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank

     **Derived using calibration standard 4-Methylumbelliferone (Sigma, Catalog # M1381).

Per Well:
  • rCpNA: 0.002 µg
  • Substrate: 200 µM

FAQs

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