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Clostridium Perfringens Neuram

inidase抗体
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  • 询价
  • CST
  • 中国/美国/德国
  • hz-11680-MM04
  • 2025年07月16日
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    • 保存条件

      常温,避光

    • 克隆性

      单克隆

    • 抗体名

      Clostridium Perfringens Neuraminidase抗体

    Clostridium Perfringens Neuraminidase抗体产品信息

    免疫原 :
    Recombinant Clostridium Perfringens Neuraminidase Protein (Catalog #11680-V07E)
    Antibody Type : Mouse Monoclonal Antibody ( Mouse mAb Service Platform )
    克隆号 :
    2D7C1
    抗体宿主 :
    Mouse IgG1
    缓冲液 : 0.2 μm filtered solution in PBS, 5% trehalose may be added in some batches. Please read the hardcopy of COA or contact our customer service to confirm the formulation.
    制备方法 :
    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, human cell-derived, 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抗体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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