Products

Campylobacter rectus cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0145

Recombinant protein-Campylobacter rectus-infected erythrocyte surface antigen (a.a.30 to 289)

B9D3Q4

100 µg

1195

Order

RPL0145

cDNA-Campylobacter rectus-infected erythrocyte surface antigen (a.a.30 to 289)

B9D3Q4

2 µg

1554

Order

 

Campylobacter rectus 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

Campylobacter rectus is a Gram-negative bacterium that is found in the oral cavity and is associated with periodontal disease and systemic infections, including bacteremia and endocarditis. In addition, Campylobacter rectus has been identified in several other body sites such as the respiratory and gastrointestinal tracts.

Infected erythrocyte surface antigen is a key antigen associated with Campylobacter rectus. This antigen is expressed on the surface of the bacterium and plays a crucial role in the interaction of Campylobacter rectus with host cells. Infected erythrocyte surface antigen has been identified as a potential target for the development of diagnostic tests and vaccines for periodontal disease and systemic infections caused by Campylobacter rectus.

Understanding the function and interaction of the key antigen, 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 Campylobacter rectus.

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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