C.perfringens C. PERFRINGENS NA Antibody


Catalog #: ABCESPA1271
Product Features
Immunogen: Recombinant Clostridium Perfringens Neuraminidase Protein 
Clonality:  Mouse MAb
Cloneno: 2D7C1
Isotype: Mouse IgG1
Buffer: 0.2 μm filtered solution in PBS with 5% trehalose
Reactivity: C.perfringens
Specificity: Clostridium Perfringens NeuraminidaseNo cross-reactivity in ELISA withE.coli cell lysate
Application: WB, ELISA
Recommend dilution:  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.
Storage: 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.
Background: 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

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