Products

Clostridium perfringens cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0148

Recombinant protein-Clostridium perfringens mature-parasite-infected erythrocyte surface antigen (a.a.1 to 107)

B1V809

100 µg

1195

Order

RPL0148

cDNA-Clostridium perfringens mature-parasite-infected erythrocyte surface antigen (a.a.1 to 107)

B1V809

2 µg

636

Order

Clostridium perfringens cDNA and recombinant antigen

  • Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.
  • Recombinant protein applications: Western Blot may be used for other applications determined by the user.
  • Protein Purity: >90%, as determined by SDS-PAGE under reducing conditions.
  • Protein Activity: N/A
  • Protein Tag:  Contains A 6x histidine tag at N-terminus.
  • Protein Formulation: Liquid
  • Source: Produced from E. coli

Clostridium perfringens is a gram-positive bacterium that is commonly found in soil, dust, and the gastrointestinal tract of humans and animals. This bacterium is known to cause a range of diseases, including food poisoning, gas gangrene, and necrotic enteritis in chickens.

The mature parasite-infected erythrocyte surface antigen is a key antigen associated with Clostridium perfringens. This antigen is expressed on the surface of the parasite and is involved in the modulation of the host immune response. It plays a critical role in the pathogenesis of Clostridium perfringens infections.

Understanding the function and interaction of the mature parasite-infected erythrocyte surface antigen is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of diseases caused by Clostridium perfringens. Further research on this antigen could potentially lead to the development of new treatment options for Clostridium perfringens infections.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.

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