Products

Clonorchis sinensis cDNA and recombinant antigen

Cat#

Products (Recombinant protein)

Swiss Prot#

Size

Price (US$)

Order

PL0146

Recombinant protein-Clonorchis sinensis Antigen Cs44 (a.a.18 to 274)

Q9UB18

100 µg

1195

Order

PL0147

Recombinant protein-Clonorchis sinensis Egg protein (a.a.17 to 253)

Q8I8I3

100 µg

1195

Order

RPL0146

cDNA-Clonorchis sinensis Antigen Cs44 (a.a.18 to 274)

Q9UB18

2 µg

1536

Order

RPL0147

cDNA-Clonorchis sinensis Egg protein (a.a.17 to 253)

Q8I8I3

2 µg

1416

Order

Clonorchis sinensis 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

Clonorchis sinensis is a parasitic flatworm that is primarily found in East Asia and is known to infect the liver and bile ducts of humans and other mammals, causing a range of symptoms including abdominal pain, jaundice, and liver cirrhosis.

Antigen Cs44 and egg protein are key antigens associated with Clonorchis sinensis. Antigen Cs44 is expressed on the surface of the worm and is involved in the modulation of the host immune response. Egg protein is found in the eggs produced by the female worm and is involved in the development of the worm’s egg.

Understanding the function and interaction of the key antigens associated with Clonorchis sinensis is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of diseases caused by this parasite. Further research on these antigens could potentially lead to the development of new treatment options for Clonorchis sinensis 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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