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|Recombinant Clostridium Perfringens Neuraminidase Protein (Catalog#11680-V07E)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Clostridium Perfringens Neuraminidase (Catalog#11680-V07E; P10481.1; Cys 2-Gln 382). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.|
|Clostridium Perfringens Neuraminidase|
No cross-reactivity in ELISA with
E.coli cell lysate
WB: 1-2 μg/mL
ELISA: 0.5-1 μg/mL
This antibody can be used at 0.5-1 μg/mL with the appropriate secondary reagents to detect Clostridium Perfringens Neuraminidase. The detection limit for Clostridium Perfringens Neuraminidase is approximately 0.039 ng/well.
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Clostridium perfringens / C. perfringens (formerly known as C. welchii) is a Gram-positive, rod-shaped, anaerobic, spore-forming bacterium of the genus Clostridium. C. perfringens is ubiquitous in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of humans and other vertebrates, insects, and soil. C. perfringens is commonly encountered in infections as a benign component of the normal flora. In this case, its role in disease is minor. Infections due to C. perfringens show evidence of tissue necrosis, bacteremia, emphysematous cholecystitis, and gas gangrene, which is also known as clostridial myonecrosis. NA, also called sialidases, specifically catalyze the hydrolysis removal of terminal sialic acid residues from viral and cellular glycoconjugates. C. Perfringens neuraminidase catalyzes the hydrolysis of alpha-(2->3)-, alpha-(2->6)-, glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates, but has little activity against the α2-8 glycosidic linkages. The function of the neuraminidase is to release sialic acids for use as carbon and energy sources for the non-pathogenic bacterium, while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors