clostridium perfringens

Perfringolysin O Protein, Clostridium perfringens, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 68.7 kDa and the accession number is P0C2E9.

Phospholipase C Protein, Clostridium perfringens, Recombinant (His) is expressed in E. coli.

Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen. Microbial collagenase Protein, Clostridium perfringens, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 39.7 kDa and the accession number is P43153.

Claudin-3 Protein, Human, Recombinant (B2M & His) is expressed in E. coli.

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Claudin-3 Protein, Human, Recombinant (Cell-Free, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 26.1 kDa and the accession number is O15551.

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Claudin-3 Protein-VLP, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-10xHis tag. The predicted molecular weight is 24.7 kDa and the accession number is O15551.

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